37 results on '"Bienkowska-Szewczyk, Krystyna"'
Search Results
2. Alterations in N-glycosylation of HCV E2 Protein in Children Patients with IFN-RBV Therapy Failure
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Zimmer, Karolina, primary, Chmielewska, Alicja M., additional, Jackowiak, Paulina, additional, Figlerowicz, Marek, additional, and Bienkowska-Szewczyk, Krystyna, additional
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- 2024
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3. Recombinant Flag-tagged E1E2 glycoproteins from three hepatitis C virus genotypes are biologically functional and elicit cross-reactive neutralizing antibodies in mice
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Krapchev, Vasil B., Rychłowska, Malgorzata, Chmielewska, Alicja, Zimmer, Karolina, Patel, Arvind H., and Bieńkowska-Szewczyk, Krystyna
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- 2018
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4. HtrA3 is a cellular partner of cytoskeleton proteins and TCP1α chaperonin
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Wenta, Tomasz, Zurawa-Janicka, Dorota, Rychlowski, Michal, Jarzab, Miroslaw, Glaza, Przemyslaw, Lipinska, Andrea, Bienkowska-Szewczyk, Krystyna, Herman-Antosiewicz, Anna, Skorko-Glonek, Joanna, and Lipinska, Barbara
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- 2018
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5. Inhibition of apoptosis in BHV-1-infected cells depends on Us3 serine/threonine kinase and its enzymatic activity
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Brzozowska, Agnieszka, Lipińska, Andrea D., Derewońko, Natalia, Lesiak, Dorota, Rychłowski, Michał, Rąbalski, Łukasz, and Bieńkowska-Szewczyk, Krystyna
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- 2018
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6. Varicelloviruses Avoid T Cell Recognition by UL49.5-Mediated Inactivation of the Transporter Associated with Antigen Processing
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Koppers-Lalic, Danijela, Ressing, Maaike E., Lipinska, Andrea D., Abele, Rupert, Koch, Joachim, Rezende, Marisa Marcondes, Admiraal, Pieter, van Leeuwen, Daphne, Bienkowska-Szewczyk, Krystyna, Mettenleiter, Thomas C., Tampé, Robert, Neefjes, Jacques, and van Rood, Johannes
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- 2005
7. The herpesvirus UL49.5 protein hijacks a cellular C-degron pathway to drive TAP transporter degradation
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Wachalska, Magda, primary, Riepe, Celeste, additional, Slusarz, Magdalena J., additional, Graul, Malgorzata, additional, Borowski, Lukasz S., additional, Qiao, Wenjie, additional, Foltynska, MIchalina, additional, Carette, Jan E., additional, Bienkowska-Szewczyk, Krystyna, additional, Szczesny, Roman J., additional, Kopito, Ron R., additional, and Lipinska, Andrea D., additional
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- 2023
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8. Effect of Glycan Shift on Antibodies against Hepatitis C Virus E2 412–425 Epitope Elicited by Chimeric sHBsAg-Based Virus-Like Particles
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Czarnota, Anna, Offersgaard, Anna, Owsianka, Ania, Alzua, Garazi Peña, Bukh, Jens, Gottwein, Judith Margarete, Patel, Arvind H., Bienkowska-Szewczyk, Krystyna, Grzyb, Katarzyna, Czarnota, Anna, Offersgaard, Anna, Owsianka, Ania, Alzua, Garazi Peña, Bukh, Jens, Gottwein, Judith Margarete, Patel, Arvind H., Bienkowska-Szewczyk, Krystyna, and Grzyb, Katarzyna
- Abstract
Two of the most important mechanisms of hepatitis C virus (HCV) immune evasion are the high variability of the amino acid sequence and epitope shielding via heavy glycosylation of the envelope (E) proteins. Previously, we showed that chimeric sHBsAg (hepatitis B virus [HBV] small surface antigen)-based virus-like particles (VLPs) carrying highly conserved epitope I from the HCV E2 glycoprotein (sHBsAg_412–425) elicit broadly neutralizing antibodies (bnAbs). However, many reports have identified escape mutations for such bnAbs that shift the N-glycosylation site from N417 to N415. This shift effectively masks the recognition of epitope I by antibodies raised against the wild-type glycoprotein. To investigate if glycan-shift-mediated immune evasion could be overcome by targeted vaccination strategies, we designed sHBsAg-based VLPs carrying epitope I with an N417S change (sHBsAg_N417S). Studies in BALB/c mice revealed that both sHBsAg_412–425 and sHBsAg_N417S VLPs were immunogenic, eliciting antibodies that recognized peptides encompassing epitope I regardless of the N417S change. However, we observed substantial differences in E1E2 glycoprotein binding and cell culture-derived HCV (HCVcc) neutralization between the sera elicited by sHBsAg_412–425 and those elicited by sHBsAg_N417S VLPs. Our results suggest a complex interplay among antibodies targeting epitope I, the E1E2 glycosylation status, and the epitope or global E1E2 conformation. Additionally, we observed striking similarities in the E1E2 glycoprotein binding patterns and HCVcc neutralization between sHBsAg_412–425 sera and AP33, suggesting that the immunization of mice with sHBsAg_412–425 VLPs can elicit AP33-like antibodies. This study emphasizes the role of antibodies against epitope I and represents an initial effort toward designing an antigen that elicits an immune response against epitope I with a glycan shift change. IMPORTANCE Epitope I, located within amino acids 412 to 423 of the HCV E2 glycoprot
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- 2023
9. Structural and functional analysis of the TAP-inhibiting UL49.5 proteins of varicelloviruses
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Verweij, Marieke C., Lipińska, Andrea D., Koppers-Lalic, Danijela, Quinten, Edwin, Funke, Jessica, van Leeuwen, Hans C., Bieńkowska-Szewczyk, Krystyna, Koch, Joachim, Ressing, Maaike E., and Wiertz, Emmanuel J.H.J.
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- 2011
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10. Zoonotic spill-over of SARS-CoV-2: mink-adapted virus in humans
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Rabalski, Lukasz, primary, Kosinski, Maciej, additional, Mazur-Panasiuk, Natalia, additional, Szewczyk, Boguslaw, additional, Bienkowska-Szewczyk, Krystyna, additional, Kant, Ravi, additional, Sironen, Tarja, additional, Pyrc, Krzysztof, additional, and Grzybek, Maciej, additional
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- 2022
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11. Human antibodies to herpes simplex virus type 1 glycoprotein C are neutralizing and target the heparan sulfate-binding domain
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Adamiak, Beata, Trybala, Edward, Mardberg, Kristina, Johansson, Maria, Liljeqvist, Jan-Ake, Olofsson, Sigvard, Grabowska, Agnieszka, Bienkowska-Szewczyk, Krystyna, Szewczyk, Boguslaw, and Bergstrom, Tomas
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- 2010
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12. New baculovirus recombinants expressing Pseudorabies virus (PRV) glycoproteins protect mice against lethal challenge infection
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Grabowska, Agnieszka K., Lipińska, Andrea D., Rohde, Jörg, Szewczyk, Boguslaw, Bienkowska-Szewczyk, Krystyna, and Rziha, Hanns-Joachim
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- 2009
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13. Expansion of a SARS-CoV-2 Delta variant with an 872 nt deletion encompassing ORF7a, ORF7b and ORF8, Poland, July to August 2021
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Mazur-Panasiuk, Natalia, primary, Rabalski, Lukasz, additional, Gromowski, Tomasz, additional, Nowicki, Grzegorz, additional, Kowalski, Michal, additional, Wydmanski, Witold, additional, Szulc, Piotr, additional, Kosinski, Maciej, additional, Gackowska, Karolina, additional, Drweska-Matelska, Natalia, additional, Grabowski, Jakub, additional, Piotrowska-Mietelska, Anna, additional, Szewczyk, Boguslaw, additional, Bienkowska-Szewczyk, Krystyna, additional, Swadzba, Jakub, additional, Labaj, Pawel, additional, Grzybek, Maciej, additional, and Pyrc, Krzysztof, additional
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- 2021
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14. Zoonotic spillover of SARS-CoV-2: mink-adapted virus in humans
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Rabalski, Lukasz, primary, Kosinski, Maciej, additional, Mazur-Panasiuk, Natalia, additional, Szewczyk, Boguslaw, additional, Bienkowska-Szewczyk, Krystyna, additional, Kant, Ravi, additional, Sironen, Tarja, additional, Pyrć, Krysztof, additional, and Grzybek, Maciej, additional
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- 2021
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15. Fasciola hepatica procathepsin L3 protein expressed by a baculovirus recombinant can partly protect rats against fasciolosis
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Reszka, Natalia, Cornelissen, Jan B.W.J., Harmsen, Michiel M., Bieńkowska-Szewczyk, Krystyna, de Bree, Joop, Boersma, Wim J., and Rijsewijk, Frans A.M.
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- 2005
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16. A highly specific and sensitive sandwich blocking ELISA based on baculovirus expressed pseudorabies virus glycoprotein B
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Gut-Winiarska, Monika, Jacobs, Liesbeth, Kerstens, Hinri, and Bienkowska-Szewczyk, Krystyna
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- 2000
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17. Cholesterol conjugation potentiates the antiviral activity of an HIV immunoadhesin
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Urbanowicz, Richard A., Lacek, Krzysztof, Lahm, Armin, Bienkowska-Szewczyk, Krystyna, Ball, Jonathan K., Nicosia, Alfredo, Cortese, Riccardo, Pessi, Antonello, Urbanowicz, Richard A., Lacek, Krzysztof, Lahm, Armin, Bienkowska-Szewczyk, Krystyna, Ball, Jonathan K., Nicosia, Alfredo, Cortese, Riccardo, and Pessi, Antonello
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Antiviral Agent ,Pharmacology ,antibody engineering ,fusion inhibitor ,peptide antiviral ,Drug Discovery3003 Pharmaceutical Science ,Organic Chemistry ,Virus Internalization ,emerging viru ,Biochemistry ,lipid raft ,enveloped viru ,human immunodeficiency virus (HIV) ,Cholesterol ,HEK293 Cell ,Structural Biology ,Drug Design ,Peptide ,HIV-1 ,cholesterol conjugation ,Molecular Medicine ,viral entry ,HIV Infection ,Molecular Biology ,Human - Abstract
Immunoadhesins are engineered proteins combining the constant domain (Fc) of an antibody with a ligand-binding (adhesion) domain. They have significant potential as therapeutic agents, because they maintain the favourable pharmacokinetics of antibodies with an expanded repertoire of ligand-binding domains: proteins, peptides, or small molecules. We have recently reported that the addition of a cholesterol group to two HIV antibodies can dramatically improve their antiviral potency. Cholesterol, which can be conjugated at various positions in the antibody, including the constant (Fc) domain, endows the conjugate with affinity for the membrane lipid rafts, thus increasing its concentration at the site where viral entry occurs. Here, we extend this strategy to an HIV immunoadhesin, combining a cholesterol-conjugated Fc domain with the peptide fusion inhibitor C41. The immunoadhesin C41-Fc-chol displayed high affinity for Human Embryonic Kidney (HEK) 293 cells, and when tested on a panel of HIV-1 strains, it was considerably more potent than the unconjugated C41-Fc construct. Potentiation of antiviral activity was comparable to what was previously observed for the cholesterol-conjugated HIV antibodies. Given the key role of cholesterol in lipid raft formation and viral fusion, we expect that the same strategy should be broadly applicable to enveloped viruses, for many of which it is already known the sequence of a peptide fusion inhibitor similar to C41. Moreover, the sequence of heptad repeat-derived fusion inhibitors can often be predicted from genomic information alone, opening a path to immunoadhesins against emerging viruses.
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- 2015
18. How short RNAs impact the human ribonuclease Dicer activity: putative regulatory feedback-loops and other RNA-mediated mechanisms controlling microRNA processing
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Koralewska, Natalia, primary, Hoffmann, Weronika, primary, Pokornowska, Maria, primary, Milewski, Marek Cezary, primary, Lipinska, Andrea, primary, Bienkowska-Szewczyk, Krystyna, primary, Figlerowicz, Marek, primary, and Kurzynska-Kokorniak, Anna, primary
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- 2017
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19. Revealing a new activity of the human Dicer DUF283 domain in vitro
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Kurzynska-Kokorniak, Anna, primary, Pokornowska, Maria, additional, Koralewska, Natalia, additional, Hoffmann, Weronika, additional, Bienkowska-Szewczyk, Krystyna, additional, and Figlerowicz, Marek, additional
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- 2016
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20. Identification of T4 gene 25 product, a component of the tail baseplate, as a 15K lysozyme
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Szewczyk, Boguslaw, Bienkowska-Szewczyk, Krystyna, and Kozloff, Lloyd M.
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- 1986
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21. Combined Adenovirus Vector and Hepatitis C Virus Envelope Protein Prime-Boost Regimen Elicits T Cell and Neutralizing Antibody Immune Responses
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Chmielewska, Alicja M., primary, Naddeo, Mariarosaria, additional, Capone, Stefania, additional, Ammendola, Virginia, additional, Hu, Ke, additional, Meredith, Luke, additional, Verhoye, Lieven, additional, Rychlowska, Malgorzata, additional, Rappuoli, Rino, additional, Ulmer, Jeffrey B., additional, Colloca, Stefano, additional, Nicosia, Alfredo, additional, Cortese, Riccardo, additional, Leroux-Roels, Geert, additional, Balfe, Peter, additional, Bienkowska-Szewczyk, Krystyna, additional, Meuleman, Philip, additional, McKeating, Jane A., additional, and Folgori, Antonella, additional
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- 2014
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22. Varicellovirus UL 49.5 proteins differentially affect the function of the transporter associated with antigen processing, TAP
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Koppers-Lalic, Danijela, Verweij, Marieke C., Lipinska, Andrea D., Wang, Ying, Quinten, Edwin, Reits, Eric A., Koch, Joachim, Loch, Sandra, Marcondes Rezende, Marisa, Daus, Franz, Bienkowska-Szewczyk, Krystyna, Osterrieder, Nikolaus, Mettenleiter, Thomas C., Heemskerk, Mirjam H. M., Tampé, Robert, Neefjes, Jacques J., Chowdhury, Shafiqul I., Ressing, Maaike E., Rijsewijk, Frans A. M., Wiertz, Emmanuel J. H. J., Koppers-Lalic, Danijela, Verweij, Marieke C., Lipinska, Andrea D., Wang, Ying, Quinten, Edwin, Reits, Eric A., Koch, Joachim, Loch, Sandra, Marcondes Rezende, Marisa, Daus, Franz, Bienkowska-Szewczyk, Krystyna, Osterrieder, Nikolaus, Mettenleiter, Thomas C., Heemskerk, Mirjam H. M., Tampé, Robert, Neefjes, Jacques J., Chowdhury, Shafiqul I., Ressing, Maaike E., Rijsewijk, Frans A. M., and Wiertz, Emmanuel J. H. J.
- Abstract
Cytotoxic T-lymphocytes play an important role in the protection against viral infections, which they detect through the recognition of virus-derived peptides, presented in the context of MHC class I molecules at the surface of the infected cell. The transporter associated with antigen processing (TAP) plays an essential role in MHC class I–restricted antigen presentation, as TAP imports peptides into the ER, where peptide loading of MHC class I molecules takes place. In this study, the UL49.5 proteins of the varicelloviruses bovine herpesvirus 1 (BHV-1), pseudorabies virus (PRV), and equine herpesvirus 1 and 4 (EHV-1 and EHV-4) are characterized as members of a novel class of viral immune evasion proteins. These UL49.5 proteins interfere with MHC class I antigen presentation by blocking the supply of antigenic peptides through inhibition of TAP. BHV-1, PRV, and EHV-1 recombinant viruses lacking UL49.5 no longer interfere with peptide transport. Combined with the observation that the individually expressed UL49.5 proteins block TAP as well, these data indicate that UL49.5 is the viral factor that is both necessary and sufficient to abolish TAP function during productive infection by these viruses. The mechanisms through which the UL49.5 proteins of BHV-1, PRV, EHV-1, and EHV-4 block TAP exhibit surprising diversity. BHV-1 UL49.5 targets TAP for proteasomal degradation, whereas EHV-1 and EHV-4 UL49.5 interfere with the binding of ATP to TAP. In contrast, TAP stability and ATP recruitment are not affected by PRV UL49.5, although it has the capacity to arrest the peptide transporter in a translocation-incompetent state, a property shared with the BHV-1 and EHV-1 UL49.5. Taken together, these results classify the UL49.5 gene products of BHV-1, PRV, EHV-1, and EHV-4 as members of a novel family of viral immune evasion proteins, inhibiting TAP through a variety of mechanisms.
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- 2008
23. How short RNAs impact the human ribonuclease Dicer activity: putative regulatory feedback-loops and other RNA-mediated mechanisms controlling microRNA processing.
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Koralewska, Natalia, Hoffmann, Weronika, Pokornowska, Maria, Milewski, Marek, Lipinska, Andrea, Bienkowska-Szewczyk, Krystyna, Figlerowicz, Marek, and Kurzynska-Kokorniak, Anna
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- 2016
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24. Application of Baculovirus-Insect Cell Expression System for Human Therapy
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Rychlowska, Malgorzata, primary, Gromadzka, Beata, additional, Bienkowska-Szewczyk, Krystyna, additional, and Szewczyk, Boguslaw, additional
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- 2011
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25. Haemonchus contortus: Characterization of the baculovirus expressed form of aminopeptidase H11
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Reszka, Natalia, Rijsewijk, Frans A.M., Zelnik, Vladimir, Moskwa, Bożena, and Bieńkowska-Szewczyk, Krystyna
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- 2007
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26. Identification of Conserved Residues in the E2 Envelope Glycoprotein of the Hepatitis C Virus That Are Critical for CD81 Binding
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Owsianka, Ania M., primary, Timms, Judith M., additional, Tarr, Alexander W., additional, Brown, Richard J. P., additional, Hickling, Timothy P., additional, Szwejk, Aleksandra, additional, Bienkowska-Szewczyk, Krystyna, additional, Thomson, Brian J., additional, Patel, Arvind H., additional, and Ball, Jonathan K., additional
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- 2006
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27. Pseudorabies Virus Glycoprotein gD Contains a Functional Endocytosis Motif That Acts in Concert with an Endocytosis Motif in gB To Drive Internalization of Antibody-Antigen Complexes from the Surface of Infected Monocytes
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Ficinska, Jolanta, primary, Van Minnebruggen, Geert, additional, Nauwynck, Hans J., additional, Bienkowska-Szewczyk, Krystyna, additional, and Favoreel, Herman W., additional
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- 2005
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28. Elution of glycoproteins from replicas of sodium dodecyl sulfate‐polyacrylamide gel electrophoresis gels
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Szewczyk, Boguslaw, primary, Pilat, Zbigniew, additional, Bienkowska‐Szewczyk, Krystyna, additional, and Summers, Donald F., additional
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- 1998
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29. Evasion of antiviral host responses by a multifunctional serine/threonine kinase of alphaherpesviruses
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Bartoszewska, Dorota, Brzozowska, Agnieszka, Rychłowski, Michał, Bieńkowska-Szewczyk, Krystyna, and Lipińska, Andrea
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- 2012
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30. Use of different fluorochromes for monitoring protein elution and transfer.
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Szewczyk, Boguslaw, Bienkowska-Szewczyk, Krystyna, and Kozloff, Lloyd M.
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- 1987
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31. Formation of poliovirus RNA polymerase 3D in Escherichia coli by cleavage of fusion proteins expressed from cloned viral cDNA
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Richards, Oliver C., primary, Ivanoff, Lucinda A., additional, Bienkowska-Szewczyk, Krystyna, additional, Butt, Brian, additional, Petteway, Stephen R., additional, Rothstein, Mark A., additional, and Ehrenfeld, Ellie, additional
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- 1987
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32. Murein transglycosylase from phage λ lysate purification and properties
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Bieńkowska-Szewczyk, Krystyna and Taylor, Alina
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- 1980
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33. Combined adenovirus vector and hepatitis C virus envelope protein prime-boost regimen elicits T cell and neutralizing antibody immune responses
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Alicja M Chmielewska, Stefano Colloca, Philip Meuleman, Rino Rappuoli, Jane A. McKeating, Lieven Verhoye, Ke Hu, Virginia Ammendola, Riccardo Cortese, Krystyna Bieńkowska-Szewczyk, Jeffrey B. Ulmer, Antonella Folgori, M. Naddeo, Luke W. Meredith, Alfredo Nicosia, Geert Leroux-Roels, Peter Balfe, Stefania Capone, Małgorzata Rychłowska, Chmielewska, Alicja M., Naddeo, Mariarosaria, Capone, Stefania, Ammendola, Virginia, Hu, Ke, Meredith, Luke, Verhoye, Lieven, Rychlowska, Malgorzata, Rappuoli, Rino, Ulmer, Jeffrey B., Colloca, Stefano, Nicosia, Alfredo, Cortese, Riccardo, Leroux Roels, Geert, Balfe, Peter, Bienkowska Szewczyk, Krystyna, Meuleman, Philip, Mckeating, Jane A., and Folgori, Antonella
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T-Lymphocytes ,Polysorbates ,Hepacivirus ,Mice ,Viral Envelope Proteins ,Neutralizing antibody ,Mice, Inbred BALB C ,Vaccines, Synthetic ,Viral Vaccine ,Vaccination ,Viral Envelope Protein ,Polysorbate ,Adenovirus vaccine ,medicine.anatomical_structure ,Female ,Genetic Vector ,medicine.drug ,Squalene ,T cell ,Recombinant Fusion Proteins ,Immunology ,Genetic Vectors ,Guinea Pigs ,Biology ,Microbiology ,Guinea Pig ,DNA vaccination ,Viral vector ,Adenoviridae ,Antigen ,Adjuvants, Immunologic ,Virology ,Vaccines and Antiviral Agents ,medicine ,Animals ,Hepaciviru ,Animal ,Viral Vaccines ,Hepatitis C Antibodies ,Antibodies, Neutralizing ,Mice, Inbred C57BL ,T-Lymphocyte ,Insect Science ,biology.protein ,Hepatitis C Antibodie ,Recombinant Fusion Protein - Abstract
Despite the recent progress in the development of new antiviral agents, hepatitis C virus (HCV) infection remains a major global health problem, and there is a need for a preventive vaccine. We previously reported that adenoviral vectors expressing HCV nonstructural proteins elicit protective T cell responses in chimpanzees and were immunogenic in healthy volunteers. Furthermore, recombinant HCV E1E2 protein formulated with adjuvant MF59 induced protective antibody responses in chimpanzees and was immunogenic in humans. To develop an HCV vaccine capable of inducing both T cell and antibody responses, we constructed adenoviral vectors expressing full-length and truncated E1E2 envelope glycoproteins from HCV genotype 1b. Heterologous prime-boost immunization regimens with adenovirus and recombinant E1E2 glycoprotein (genotype 1a) plus MF59 were evaluated in mice and guinea pigs. Adenovirus prime and protein boost induced broad HCV-specific CD8 + and CD4 + T cell responses and functional Th1-type IgG responses. Immune sera neutralized luciferase reporter pseudoparticles expressing HCV envelope glycoproteins (HCVpp) and a diverse panel of recombinant cell culture-derived HCV (HCVcc) strains and limited cell-to-cell HCV transmission. This study demonstrated that combining adenovirus vector with protein antigen can induce strong antibody and T cell responses that surpass immune responses achieved by either vaccine alone. IMPORTANCE HCV infection is a major health problem. Despite the availability of new directly acting antiviral agents for treating chronic infection, an affordable preventive vaccine provides the best long-term goal for controlling the global epidemic. This report describes a new anti-HCV vaccine targeting the envelope viral proteins based on adenovirus vector and protein in adjuvant. Rodents primed with the adenovirus vaccine and boosted with the adjuvanted protein developed cross-neutralizing antibodies and potent T cell responses that surpassed immune responses achieved with either vaccine component alone. If combined with the adenovirus vaccine targeting the HCV NS antigens now under clinical testing, this new vaccine might lead to a stronger and broader immune response and to a more effective vaccine to prevent HCV infection. Importantly, the described approach represents a valuable strategy for other infectious diseases in which both T and B cell responses are essential for protection.
- Published
- 2014
34. Bovine Herpesvirus 1 UL49.5 Protein Inhibits the Transporter Associated with Antigen Processing despite Complex Formation with Glycoprotein M.
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Lipinska, Andrea D., Koppers-Lalic, Danijela, Rychlowski, Michal, Admiraal, Pieter, Rijsewijk, Frans A. M., Bienkowska-Szewczyk, Krystyna, and Wiertz, Emmanuel J. H.
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- *
HERPESVIRUSES , *DNA viruses , *PEPTIDES , *ANTIGENS , *CELLS , *CELL lines - Abstract
Bovine herpesvirus 1 (BHV-1) interferes with peptide translocation by the transporter associated with antigen processing (TAP). Recently, the UL49.5 gene product of BHV-1 was identified as the protein responsible for the observed inhibition of TAP. In BHV-1-infected cells and virions, the UL49.5 protein forms a complex with glycoprotein M (gM). Hence, it was investigated whether UL49.5 can combine the interactions with gM and the TAP complex. In cell lines constitutively expressing both UL49.5 and gM, UL49.5 appears to be required for functional processing of gM. Immunofluorescence-confocal laser scanning microscopy demonstrated that both proteins are interdependent for their redistribution from the endoplasmic reticulum to the trans-Golgi network. Remarkably, expression of cloned gM results in the abrogation of the UL49.5-mediated inhibition of TAP and prevents the degradation of the transporter. However, in BHV-1-infected cells, differences in UL49.5 and gM expression kinetics were seen to create a window of opportunity at the early stages of infection, during which time the UL49.5 protein can act on TAP without gM interference. Moreover, in later periods, non-gM-associated UL49.5 can be detected in addition to the UL49.5/gM complex. Thus, it has been deduced that different functions of UL49.5, editing of gM processing and inhibition of TAP, can be combined during BHV-1 infection. [ABSTRACT FROM AUTHOR]
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- 2006
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35. Geographical and temporal distribution of SARS-CoV-2 clades in the WHO European Region, January to June 2020
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Alm E., Broberg E.K., Connor T., Hodcroft E.B., Komissarov A.B., Maurer-Stroh S., Melidou A., Neher R.A., O'Toole A., Pereyaslov D., Beerenwinkel N., Posada-Cespedes S., Jablonski K.P., Ferreira P.F., Topolsky I., Avsic-Zupanc T., Korva M., Poljak M., Zakotnik S., Zorec T.M., Bragstad K., Hungnes O., Stene-Johansen K., Reusken C., Meijer A., Vennema H., Ruiz-Roldan L., Bracho M.A., Garcia-Gonzalez N., Chiner-Oms A., Cancino-Munoz I., Comas I., Goig G.A., Torres-Puente M., Lopez M.G., Martinez-Priego L., D'Auria G., Ruiz-Hueso P., Ferrus-Abad L., de Marco G., Galan-Vendrell I., Carbo-Ramirez S., Ruiz-Rodriguez P., Coscolla M., Polackova K., Kramna L., Cinek O., Richter J., Krashias G., Tryfonos C., Bashiardes S., Koptides D., Christodoulou C., Bartolini B., Gruber C.E., Di Caro A., Castilletti C., Stefani F., Rimoldi S.G., Romeri F., Salerno F., Polesello S., Nagy A., Jirincova H., Vecerova J., Novakova L., Cordey S., Murtskhvaladze M., Kotaria N., Schar T., Beisel C., Vugrek O., Rokic F., Trgovec-Greif L., Jurak I., Rukavina T., Sucic N., Schonning K., Karst S.M., Kirkegaard R.H., Michaelsen T.Y., Sorensen E.A., Knutson S., Brandt J., Le-Quy V., Sorensen T., Petersen C., Pedersen M.S., Larsen S.L., Skov M.N., Rasmussen M., Fonager J., Fomsgaard A., Maksyutov R.A., Gavrilova E.V., Pyankov O.V., Bodnev S.A., Tregubchak T.V., Shvalov A.N., Antonets D.V., Resende P.C., Goya S., Perrin A., Lee R.T., Yadahalli S., Han A.X., Russell C.A., Schmutz S., Zaheri M., Kufner V., Huber M., Trkola A., Antwerpen M., Walter M.C., van der Werf S., Gambaro F., Behillil S., Enouf V., Donati F., Ustinova M., Rovite V., Klovins J., Savicka O., Wienecke-Baldacchino A.K., Ragimbeau C., Fournier G., Mossong J., Aberle S.W., Haukland M., Enkirch T., Advani A., Karlberg M.L., Lindsjo O.K., Broddesson S., Slavikova M., Lickova M., Klempa B., Staronova E., Ticha E., Szemes T., Rusnakova D., Stadler T., Quer J., Anton A., Andres C., Pinana M., Garcia-Cehic D., Pumarola T., Izopet J., Gioula G., Exindari M., Papa A., Chatzidimitriou D., Metallidis S., Pappa S., Macek M., Geryk J., Broz P., Briksi A., Hubacek P., Drevinek P., Zajac M., Kvapil P., Holub M., Kvapilova K., Novotny A., Kasny M., Klempt P., Vapalahti O., Smura T., Sironen T., Selhorst P., Anthony C., Arien K., Simon-Loriere E., Rabalski L., Bienkowska-Szewczyk K., Borges V., Isidro J., Gomes J.P., Guiomar R., Pechirra P., Costa I., Duarte S., Vieira L., Pyrc K., Zuckerman N.S., Turdikulova S., Abdullaev A., Dalimova D., Abdurakhimov A., Tagliabracci A., Alessandrini F., Melchionda F., Onofri V., Turchi C., Bagnarelli P., Menzo S., Caucci S., Di Sante L., Popa A., Genger J.-W., Agerer B., Lercher A., Endler L., Smyth M., Penz T., Schuster M., Senekowitsch M., Laine J., Bock C., Bergthaler A., Shevtsov A., Kalendar R., Ramanculov Y., Graf A., Muenchhoff M., Keppler O.T., Krebs S., Blum H., Marcello A., Licastro D., D'Agaro P., Laubscher F., Vidanovic D., Tesovic B., Volkening J., Clementi N., Mancini N., Rupnik M., Mahnic A., Walker A., Houwaart T., Wienemann T., Vasconcelos M.K., Strelow D., Jensen B.-E.O., Senff T., Hulse L., Adams O., Andree M., Hauka S., Feldt T., Keitel V., Kindgen-Milles D., Timm J., Pfeffer K., Dilthey A.T., Moore C., Ozdarendeli A., Pavel S.T.I., Yetiskin H., Aydin G., Holyavkin C., Uygut M.A., Cevik C., Shchetinin A., Gushchin V., Dinler-Doganay G., Doganay L., Kizilboga-Akgun T., Karacan I., Pancer K., Maes P., Marti-Carreras J., Wawina-Bokalanga T., Vanmechelen B., Thurmer A., Wedde M., Durrwald R., von Kleist M., Drechsel O., Wolff T., Fuchs S., Kmiecinski R., Michel J., Nitsche A., Casas I., Caballero M.I., Zaballos A., Jimenez P., Jimenez M., Fernandez S.M., Fernandez S.V., de la Plaza I.C., Fadeev A., Ivanova A., Sergeeva M., Stefanelli P., Estee Torok M., Hall G., da Silva Filipe A., Turtle L., Afifi S., McCluggage K., Beer R., Ledesma J., Maksimovic J., Spellman K., Hamilton W.L., Marchbank A., Southgate J.A., Underwood A., Taylor B., Yeats C., Abudahab K., Gemmell M.R., Eccles R., Lucaci A., Nelson C.A., Rainbow L., Whitehead M., Gregory R., Haldenby S., Paterson S., Hughes M.A., Curran M.D., Baker D., Tucker R., Green L.R., Feltwell T., Halstead F.D., Wyles M., Jahun A.S., Ahmad S.S.Y., Georgana I., Goodfellow I., Yakovleva A., Meredith L.W., Gavriil A., Awan A.R., Fisher C., Edgeworth J., Lynch J., Moore N., Williams R., Kidd S.P., Cortes N., Brunker K., McCrone J.T., Quick J., Duckworth N., Walsh S., Sloan T., Ludden C., George R.P., Eltringham G., Brown J.R., Aranday-Cortes E., Shepherd J.G., Hughes J., Li K.K., Williams T.C., Johnson N., Jesudason N., Mair D., Thomson E., Shah R., Parr Y.A., Carmichael S., Robertson D.L., Nomikou K., Broos A., Niebel M., Smollett K., Tong L., Miah S., Wittner A., Phillips N., Payne B., Dewar R., Holmes A., Bolt F., Price J.R., Mookerjee S., Sethi D.K., Potter W., Stanley R., Prakash R., Dervisevic S., Graham J.C., Nelson A., Smith D., Young G.R., Yew W.C., Todd J.A., Trebes A., Andersson M., Bull M., Watkins J., Birchley A., Gatica-Wilcox B., Gilbert L., Kumziene-Summerhayes S., Rey S., Chauhan A., Butcher E., Bicknell K., Elliott S., Glaysher S., Lackenby A., Bibby D., Platt S., Mohamed H., Machin N.W., Mbisa J.L., Evans J., Perry M., Pacchiarini N., Corden S., Adams A.G., Gaskin A., Coombs J., Graham L.J., Cottrell S., Morgan M., Gifford L., Kolyva A., Rudder S.J., Trotter A.J., Mather A.E., Aydin A., Page A.J., Kay G.L., de Oliveira Martins L., Yasir M., Alikhan N.-F., Thomson N.M., Gilroy R., Kingsley R.A., O'Grady J., Gutierrez A.V., Diaz M., Viet T.L., Tedim A.P., Adriaenssens E.M., Patrick Mcclure C., Sang F., Clark G., Howson-Wells H.C., Debebe J., Ball J., Chappell J., Khakh M., Carlile M., Loose M., Lister M.M., Holmes N., Tsoleridis T., Fleming V.M., Wright V., Smith W., Gallagher M.D., Parker M., Partridge D.G., Evans C., Baker P., Essex S., Liggett S., Keeley A.J., Bashton M., Rooke S., Dervisavic S., Meader E.J., Lopez C.E.B., Angyal A., Kristiansen M., Tutill H.J., Findlay J., Mestek-Boukhibar L., Forrest L., Dyal P., Williams R.J., Panchbhaya Y., Williams C.A., Roy S., Pandey S., Stockton J., Loman N.J., Poplawski R., Nicholls S., Rowe W.P.M., Khokhar F., Pinckert M.L., Hosmillo M., Chaudhry Y., Caller L.G., Davidson R.K., Griffith L., Rambaut A., Jackson B., Colquhoun R., Hill V., Nichols J., Asamaphan P., Darby A., Jackson K.A., Iturriza-Gomara M., Vamos E.E., Green A., Aanensen D., Bonsall D., Buck D., Macintyre-Cockett G., de Cesare M., Pybus O., Golubchik T., Scarlett G., Loveson K.F., Robson S.C., Beckett A., Lindsey B., Groves D.C., Parsons P.J., McHugh M.P., Barnes J.D., Manso C.F., Grammatopoulos D., Menger K.E., Harrison E., Gunson R., Peacock S.J., Gonzalez G., Carr M., Mihaela L., Popovici O., Brytting M., Bresner C., Fuller W., Workman T., Mentis A.F., Kossyvakis A., Karamitros T., Pogka V., Kalliaropoulos A., Horefti E., Kontou A., Martinez-Gonzalez B., Labropoulou V., Voulgari-Kokota A., Evangelidou M., Bizta P., Belimezi M., Lambrechts L., Doymaz M.Z., Yazici M.K., Cetin N.S., Karaaslan E., Kallio-Kokko H., Virtanen J., Suvanto M., Nguyen P.T., Ellonen P., Hannula S., Kangas H., Sreenu V.B., Burian K., Terhes G., Gombos K., Gyenesei A., Urban P., Herczeg R., Jakab F., Kemenesi G., Toth G.E., Somogyi B., Zana B., Zeghbib S., Kuczmog A., Foldes F., Lanszki Z., Madai M., Papp H., Pereszlenyi C.I., Babinszky G.C., Dudas G., Csoma E., Abou Tayoun A.N., Alsheikh-Ali A.A., Loney T., Nowotny N., Abdul-Wahab O., Gonzalez-Candelas F., Andersen M.H., Taylor S., MARTI CARRERAS, Joan, Vanmechelen, Bert, Wawina, Tony, Medical Microbiology and Infection Prevention, AII - Infectious diseases, WHO European Region Sequencing Lab, GISAID EpiCoV Grp, Erik, Alm, Eeva K, Broberg, Thomas, Connor, Emma B, Hodcroft, Andrey B, Komissarov, Sebastian, Maurer-Stroh, Angeliki, Melidou, Richard A, Neher, Áine, O’Toole, Dmitriy, Pereyaslov, WHO European Region sequencing laboratories and GISAID EpiCoV group (Niko Beerenwinkel, The, Posada-Céspedes, Susana, Philipp, Kim, Jablonski, Falé Ferreira, Pedro, Topolsky, Ivan, Avšičžupanc, Tatjana, Korva, Miša, Poljak, Mario, Zakotnik, Samo, Tomaž, Zorec, Mark, Bragstad, Karoline, Hungnes, Olav, Stene-Johansen, Kathrine, Reusken, Chantal, Meijer, Adam, Vennema, Harry, Ruiz-Roldán, Lidia, Alma Bracho, María, García-González, Neri, Chiner-Oms, Álvaro, Cancino-Muñoz, Irving, Comas, Iñaki, A Goig, Galo, Torres-Puente, Manuela, G López, Mariana, Martínez-Priego, Llúcia, D’Auria, Giuseppe, LoretoFerrús-Abad, de Marco, Griselda, Galan-Vendrell, Inmaculada, Carbó-Ramirez, Sandra, Ruíz-Hueso, Paula, Coscollá, Mireia, Polackova, Katerina, Kramna, Lenka, Cinek, Ondrej, Richter, Jan, Krashias, George, Tryfonos, Christina, Bashiardes, Stavro, Koptides, Dana, Christodoulou, Christina, Bartolini, Barbara, Em Gruber, Cesare, Di Caro, Antonino, Castilletti, Concetta, Stefani, Fabrizio, Giordana Rimoldi, Sara, Romeri, Francesca, Salerno, Franco, Polesello, Stefano, Nagy, Alexander, Jirincova, Helena, Vecerova, Jaromira, Novakova, Ludmila, Cordey, Samuel, Murtskhvaladze, Marine, Kotaria, Nato, Schär, Tobia, Beisel, Christian, Vugrek, Oliver, Rokić, Filip, Trgovecgreif, Lovro, Jurak, Igor, Rukavina, Tomislav, Sučić, Neven, Schønning, Kristian, M Karst, Søren, H Kirkegaard, Rasmu, Y Michaelsen, Thoma, Aa Sørensen, Emil, Knutson, Simon, Brandt, Jakob, Le-Quy, Vang, Sørensen, Trine, Petersen, Celine, Schou Pedersen, Martin, Løkkegaard Larsen, Sanne, Nielsine Skov, Marianne, Rasmussen, Morten, Fonager, Jannik, Fomsgaard, Ander, Amirovich Maksyutov, Rinat, Vasil’Evna Gavrilova, Elena, Victorovich Pyankov, Oleg, Alexandrovich Bodnev, Sergey, Vladimirovna Tregubchak, Tatyana, Nikolayevich Shvalov, Alexander, Victorovich Antonets, Deni, Cristina Resende, Paola, Goya, Stephanie, Perrin, Amandine, Tc Lee, Raphael, Yadahalli, Shilpa, X Han, Alvin, A Russell, Colin, Schmutz, Stefan, Zaheri, Maryam, Kufner, Verena, Huber, Michael, Trkola, Alexandra, Antwerpen, Marku, C Walter, Mathia, van der Werf, Sylvie, Gambaro, Fabiana, Behillil, Sylvie, Enouf, Vincent, Donati, Flora, Ustinova, Monta, Rovite, Vita, Klovins, Jani, Savicka, Oksana, K Wienecke-Baldacchino, Anke, Ragimbeau, Catherine, Fournier, Guillaume, Mossong, Joël, W Aberle, Stephan, Haukland, Mattia, Enkirch, Theresa, Advani, Abdolreza, Lind Karlberg, Maria, Karlsson Lindsjö, Oskar, Broddesson, Sandra, Sláviková, Monika, Ličková, Martina, Klempa, Bori, Staroňová, Edita, Tichá, Elena, Szemes, Tomáš, Rusňáková, Diana, Stadler, Tanja, Quer, Josep, Anton, Andre, Andres, Cristina, Piñana, Maria, Garcia-Cehic, Damir, Pumarola, Toma, Izopet, Jacque, Gioula, Georgia, Exindari, Maria, Papa, Anna, Chatzidimitriou, Dimitrio, Metallidis, Symeon, Pappa, Stella, Macek Jr, Milan, Geryk, Jan, Brož, Petr, Briksí, Aleš, Hubáček, Petr, Dřevínek, Pavel, Zajac, Miroslav, Kvapil, Petr, Holub, Michal, Kvapilová, Kateřina, Novotný, Adam, Kašný, Martin, Klempt, Petr, Vapalahti, Olli, Smura, Teemu, Sironen, Tarja, Selhorst, Philippe, Anthony, Colin, Ariën, Kevin, Simon-Loriere, Etienne, Rabalski, Lukasz, Bienkowska-Szewczyk, Krystyna, Borges, Vítor, Isidro, Joana, Paulo Gomes, João, Guiomar, Raquel, Pechirra, Pedro, Costa, Inê, Duarte, Sílvia, Vieira, Luí, Pyrc, Krzysztof, S Zuckerman, Neta, Turdikulova, Shahlo, Abdullaev, Alisher, Dalimova, Dilbar, Abdurakhimov, Abror, Tagliabracci, Adriano, Alessandrini, Federica, Melchionda, Filomena, Onofri, Valerio, Turchi, Chiara, Bagnarelli, Patrizia, Menzo, Stefano, Caucci, Sara, Di Sante, Laura, Popa, Alexandra, Genger, Jakob-Wendelin, Agerer, Benedikt, Lercher, Alexander, Endler, Luka, Smyth, Mark, Penz, Thoma, Schuster, Michael, Senekowitsch, Martin, Laine, Jan, Bock, Christoph, Bergthaler, Andrea, Shevtsov, Alexandr, Kalendar, Ruslan, Ramanculov, Yerlan, Graf, Alexander, Muenchhoff, Maximilian, T Keppler, Oliver, Krebs, Stefan, Blum, Helmut, Marcello, Alessandro, Licastro, Danilo, D’Agaro, Pierlanfranco, Laubscher, Florian, Vidanovic, Dejan, Tesovic, Bojana, Volkening, Jeremy, Clementi, Nicola, Mancini, Nicasio, Rupnik, Maja, Mahnic, Aleksander, Walker, Andrea, Houwaart, Torsten, Wienemann, Tobia, Kohns Vasconcelos, Malte, Strelow, Daniel, Ole Jensen, Björn-Erik, Senff, Tina, Hülse, Lisanna, Adams, Ortwin, Andree, Marcel, Hauka, Sandra, Feldt, Torsten, Keitel, Verena, Kindgen-Milles, Detlef, Timm, Jörg, Pfeffer, Klau, T Dilthey, Alexander, Moore, Catherine, Ozdarendeli, Aykut, Terkis Islam Pavel, Shaikh, Yetiskin, Hazel, Aydin, Gunsu, Holyavkin, Can, Ali Uygut, Muhammet, Cevik, Ceren, Shchetinin, Alexey, Gushchin, Vladimir, Dinler-Doganay, Gizem, Doganay, Levent, Kizilboga-Akgun, Tugba, Karacan, Ilker, Pancer, Katarzyna, Maes, Piet, Martí-Carreras, Joan, Wawina-Bokalanga, Tony, Thürmer, Andrea, Wedde, Marianne, Dürrwald, Ralf, Von Kleist, Max, Drechsel, Oliver, Wolff, Thorsten, Fuchs, Stephan, Kmiecinski, Rene, Michel, Janine, Nitsche, Andrea, Casas, Inmaculada, Iglesias Caballero, María, Zaballos, Ángel, Jiménez, Pilar, Jiménez, Mercede, Monzón Fernández, Sara, Varona Fernández, Sarai, Cuesta De La Plaza, Isabel, Fadeev, Artem, Ivanova, Anna, Sergeeva, Mariia, Stefanelli, Paola, Estee Torok, M, Hall, Grant, da Silva Filipe, Ana, Turtle, Lance, Afifi, Safiah, Mccluggage, Kathryn, Beer, Robert, Ledesma, Juan, Maksimovic, Joshua, Spellman, Karla, L Hamilton, William, Marchbank, Angela, Alexander Southgate, Joel, Underwood, Anthony, Taylor, Ben, Yeats, Corin, Abudahab, Khalil, R Gemmell, Matthew, Eccles, Richard, Lucaci, Anita, Abigail Nelson, Charlotte, Rainbow, Lucille, Whitehead, Mark, Gregory, Richard, Haldenby, Sam, Paterson, Steve, A Hughes, Margaret, D Curran, Martin, Baker, David, Tucker, Rachel, R Green, Luke, Feltwell, Theresa, D Halstead, Fenella, Wyles, Matthew, S Jahun, Aminu, Y Ahmad, Shazaad S, Georgana, Iliana, Goodfellow, Ian, Yakovleva, Anna, W Meredith, Luke, Gavriil, Artemi, Raza Awan, Ali, Fisher, Chloe, Jonathan, European Centre for Disease Prevention and Control [Stockholm, Sweden] (ECDC), Cardiff University, Public Health Wales [Cardiff, Royaume uni], University of Basel (Unibas), Research Institute of Influenza, St. Petersburg, Russia, Agency for science, technology and research [Singapore] (A*STAR), National University of Singapore (NUS), University of Edinburgh, WHO Regional Office for Europe [Copenhagen], We gratefully acknowledge the authors, originating and submitting laboratories of the sequences from GISAID’s EpiCoV Database used in the phylogenetic analysis. We gratefully acknowledge all the staff working with sample collection, sample preparation, sequencing, data analysis and data sharing in all laboratories in the WHO European Region for making this work possible, The WHO European Region sequencing laboratories and GISAID EpiCoV group*: Niko Beerenwinkel, Susana Posada-Céspedes, Kim Philipp Jablonski, Pedro Falé Ferreira, Ivan Topolsky, Tatjana Avšič-Županc, Miša Korva, Mario Poljak, Samo Zakotnik, Tomaž Mark Zorec, Karoline Bragstad, Olav Hungnes, Kathrine Stene-Johansen, Chantal Reusken, Adam Meijer, Harry Vennema, Lidia Ruiz-Roldán, María Alma Bracho, Neris García-González, Álvaro Chiner-Oms, Irving Cancino-Muñoz, Iñaki Comas, Galo A Goig, Manuela Torres-Puente, Mariana G López, Llúcia Martínez-Priego, Giuseppe D'Auria, Paula Ruíz-Hueso, Loreto Ferrús-Abad, Griselda de Marco, Inmaculada Galan-Vendrell, Sandra Carbó-Ramirez, Paula Ruiz-Rodriguez, Mireia Coscollá, Katerina Polackova, Lenka Kramna, Ondrej Cinek, Jan Richter, George Krashias, Christina Tryfonos, Stavros Bashiardes, Dana Koptides, Christina Christodoulou, Barbara Bartolini, Cesare Em Gruber, Antonino Di Caro, Concetta Castilletti, Fabrizio Stefani, Sara Giordana Rimoldi, Francesca Romeri, Franco Salerno, Stefano Polesello, Alexander Nagy, Helena Jirincova, Jaromira Vecerova, Ludmila Novakova, Samuel Cordey, Marine Murtskhvaladze, Nato Kotaria, Tobias Schär, Christian Beisel, Oliver Vugrek, Filip Rokić, Lovro Trgovec-Greif, Igor Jurak, Tomislav Rukavina, Neven Sučić, Kristian Schønning, Søren M Karst, Rasmus H Kirkegaard, Thomas Y Michaelsen, Emil Aa Sørensen, Simon Knutson, Jakob Brandt, Vang Le-Quy, Trine Sørensen, Celine Petersen, Martin Schou Pedersen, Sanne Løkkegaard Larsen, Marianne Nielsine Skov, Morten Rasmussen, Jannik Fonager, Anders Fomsgaard, Rinat Amirovich Maksyutov, Elena Vasil'Evna Gavrilova, Oleg Victorovich Pyankov, Sergey Alexandrovich Bodnev, Tatyana Vladimirovna Tregubchak, Alexander Nikolayevich Shvalov, Denis Victorovich Antonets, Paola Cristina Resende, Stephanie Goya, Amandine Perrin, Raphael Tc Lee, Shilpa Yadahalli, Alvin X Han, Colin A Russell, Stefan Schmutz, Maryam Zaheri, Verena Kufner, Michael Huber, Alexandra Trkola, Markus Antwerpen, Mathias C Walter, Sylvie van der Werf, Fabiana Gambaro, Sylvie Behillil, Vincent Enouf, Flora Donati, Monta Ustinova, Vita Rovite, Janis Klovins, Oksana Savicka, Anke K Wienecke-Baldacchino, Catherine Ragimbeau, Guillaume Fournier, Joël Mossong, Stephan W Aberle, Mattias Haukland, Theresa Enkirch, Abdolreza Advani, Maria Lind Karlberg, Oskar Karlsson Lindsjö, Sandra Broddesson, Monika Sláviková, Martina Ličková, Boris Klempa, Edita Staroňová, Elena Tichá, Tomáš Szemes, Diana Rusňáková, Tanja Stadler, Josep Quer, Andres Anton, Cristina Andres, Maria Piñana, Damir Garcia-Cehic, Tomas Pumarola, Jacques Izopet, Georgia Gioula, Maria Exindari, Anna Papa, Dimitrios Chatzidimitriou, Symeon Metallidis, Stella Pappa, Milan Macek Jr, Jan Geryk, Petr Brož, Aleš Briksí, Petr Hubáček, Pavel Dřevínek, Miroslav Zajac, Petr Kvapil, Michal Holub, Kateřina Kvapilová, Adam Novotný, Martin Kašný, Petr Klempt, Olli Vapalahti, Teemu Smura, Tarja Sironen, Philippe Selhorst, Colin Anthony, Kevin Ariën, Etienne Simon-Loriere, Lukasz Rabalski, Krystyna Bienkowska-Szewczyk, Vítor Borges, Joana Isidro, João Paulo Gomes, Raquel Guiomar, Pedro Pechirra, Inês Costa, Sílvia Duarte, Luís Vieira, Krzysztof Pyrc, Neta S Zuckerman, Shahlo Turdikulova, Alisher Abdullaev, Dilbar Dalimova, Abror Abdurakhimov, Adriano Tagliabracci, Federica Alessandrini, Filomena Melchionda, Valerio Onofri, Chiara Turchi, Patrizia Bagnarelli, Stefano Menzo, Sara Caucci, Laura Di Sante, Alexandra Popa, Jakob-Wendelin Genger, Benedikt Agerer, Alexander Lercher, Lukas Endler, Mark Smyth, Thomas Penz, Michael Schuster, Martin Senekowitsch, Jan Laine, Christoph Bock, Andreas Bergthaler, Alexandr Shevtsov, Ruslan Kalendar, Yerlan Ramanculov, Alexander Graf, Maximilian Muenchhoff, Oliver T Keppler, Stefan Krebs, Helmut Blum, Alessandro Marcello, Danilo Licastro, Pierlanfranco D'Agaro, Florian Laubscher, Dejan Vidanovic, Bojana Tesovic, Jeremy Volkening, Nicola Clementi, Nicasio Mancini, Maja Rupnik, Aleksander Mahnic, Andreas Walker, Torsten Houwaart, Tobias Wienemann, Malte Kohns Vasconcelos, Daniel Strelow, Björn-Erik Ole Jensen, Tina Senff, Lisanna Hülse, Ortwin Adams, Marcel Andree, Sandra Hauka, Torsten Feldt, Verena Keitel, Detlef Kindgen-Milles, Jörg Timm, Klaus Pfeffer, Alexander T Dilthey, Catherine Moore, Aykut Ozdarendeli, Shaikh Terkis Islam Pavel, Hazel Yetiskin, Gunsu Aydin, Can Holyavkin, Muhammet Ali Uygut, Ceren Cevik, Alexey Shchetinin, Vladimir Gushchin, Gizem Dinler-Doganay, Levent Doganay, Tugba Kizilboga-Akgun, Ilker Karacan, Katarzyna Pancer, Piet Maes, Joan Martí-Carreras, Tony Wawina-Bokalanga, Bert Vanmechelen, Andrea Thürmer, Marianne Wedde, Ralf Dürrwald, Max Von Kleist, Oliver Drechsel, Thorsten Wolff, Stephan Fuchs, Rene Kmiecinski, Janine Michel, Andreas Nitsche, Inmaculada Casas, María Iglesias Caballero, Ángel Zaballos, Pilar Jiménez, Mercedes Jiménez, Sara Monzón Fernández, Sarai Varona Fernández, Isabel Cuesta De La Plaza, Artem Fadeev, Anna Ivanova, Mariia Sergeeva, Paola Stefanelli, M Estee Torok, Grant Hall, Ana da Silva Filipe, Lance Turtle, Safiah Afifi, Kathryn Mccluggage, Robert Beer, Juan Ledesma, Joshua Maksimovic, Karla Spellman, William L Hamilton, Angela Marchbank, Joel Alexander Southgate, Anthony Underwood, Ben Taylor, Corin Yeats, Khalil Abudahab, Matthew R Gemmell, Richard Eccles, Anita Lucaci, Charlotte Abigail Nelson, Lucille Rainbow, Mark Whitehead, Richard Gregory, Sam Haldenby, Steve Paterson, Margaret A Hughes, Martin D Curran, David Baker, Rachel Tucker, Luke R Green, Theresa Feltwell, Fenella D Halstead, Matthew Wyles, Aminu S Jahun, Shazaad S Y Ahmad, Iliana Georgana, Ian Goodfellow, Anna Yakovleva, Luke W Meredith, Artemis Gavriil, Ali Raza Awan, Chloe Fisher, Jonathan Edgeworth, Jessica Lynch, Nathan Moore, Rebecca Williams, Stephen P Kidd, Nicholas Cortes, Kirstyn Brunker, John T Mccrone, Joshua Quick, Nichola Duckworth, Sarah Walsh, Tim Sloan, Catherine Ludden, Ryan P George, Gary Eltringham, Julianne R Brown, Elihu Aranday-Cortes, James G Shepherd, Joseph Hughes, Kathy K Li, Thomas C Williams, Natasha Johnson, Natasha Jesudason, Daniel Mair, Emma Thomson, Rajiv Shah, Yasmin A Parr, Stephen Carmichael, David L Robertson, Kyriaki Nomikou, Alice Broos, Marc Niebel, Katherine Smollett, Lily Tong, Shahjahan Miah, Anita Wittner, Nicole Phillips, Brendan Payne, Rebecca Dewar, Alison Holmes, Frances Bolt, James R Price, Siddharth Mookerjee, Dheeraj K Sethi, Will Potter, Rachael Stanley, Reenesh Prakash, Samir Dervisevic, Jonathan Clive Graham, Andrew Nelson, Darren Smith, Gregory R Young, Wen Chyin Yew, John A Todd, Amy Trebes, Monique Andersson, Matthew Bull, Joanne Watkins, Alec Birchley, Bree Gatica-Wilcox, Lauren Gilbert, Sara Kumžiene-Summerhayes, Sara Rey, Anoop Chauhan, 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H., Taylor, S., European Centre for Disease Prevention and Control (ECDC), Public Health Wales Microbiology Cardiff, Faculty of Agriculture and Forestry, Department of Agricultural Sciences, and Institute of Biotechnology
- Subjects
Infecções Respiratórias ,0301 basic medicine ,MESH: Coronavirus Infections ,Epidemiology ,[SDV]Life Sciences [q-bio] ,Distribution (economics) ,Wastewater ,MESH: Base Sequence ,Severe Acute Respiratory Syndrome ,MESH: World Health Organization ,Pandemic ,MESH: Coronavirus ,MESH: COVID-19 ,Sequencing ,Viral ,Clade ,Nomenclature ,Genome ,biology ,COVID-19 ,Europe ,NGS ,SARS-CoV-2 ,WGS ,nomenclature ,sequencing ,Base Sequence ,Betacoronavirus ,Coronavirus ,Coronavirus Infections ,Genome, Viral ,Humans ,Phylogeography ,Pneumonia, Viral ,RNA, Viral ,RNA-Dependent RNA Polymerase ,Spatio-Temporal Analysis ,World Health Organization ,Pandemics ,C500 ,European region ,3. Good health ,Geography ,MESH: Phylogeography ,MESH: RNA-Dependent RNA Polymerase ,MESH: RNA, Viral ,MESH: Betacoronavirus ,Spatio-Temporal Analysi ,MESH: Genome, Viral ,Cartography ,Human ,Bioquímica ,MESH: Pandemics ,Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) ,Coronaviru ,030106 microbiology ,03 medical and health sciences ,MESH: Spatio-Temporal Analysis ,MESH: Severe Acute Respiratory Syndrome ,Virology ,MESH: SARS-CoV-2 ,Whole genome sequencing ,MESH: Humans ,Whole Genome Sequencing ,Betacoronaviru ,Coronavirus Infection ,business.industry ,Public Health, Environmental and Occupational Health ,Pneumonia ,biology.organism_classification ,B900 ,030104 developmental biology ,MESH: Pneumonia, Viral ,RNA ,SARS_CoV-2 ,3111 Biomedicine ,MESH: Europe ,Human medicine ,business - Abstract
8 páginas, 3 figuras, We show the distribution of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) genetic clades over time and between countries and outline potential genomic surveillance objectives. We applied three genomic nomenclature systems to all sequence data from the World Health Organization European Region available until 10 July 2020. We highlight the importance of real-time sequencing and data dissemination in a pandemic situation, compare the nomenclatures and lay a foundation for future European genomic surveillance of SARS-CoV-2., We gratefully acknowledge the authors, originating and submitting laboratories of the sequences from GISAID’s EpiCoV Database used in the phylogenetic analysis. We gratefully acknowledge all the staff working with sample collection, sample preparation, sequencing, data analysis and data sharing in all laboratories in the WHO European Region for making this work possible.
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36. Cholesterol conjugation potentiates the antiviral activity of an HIV immunoadhesin.
- Author
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Urbanowicz RA, Lacek K, Lahm A, Bienkowska-Szewczyk K, Ball JK, Nicosia A, Cortese R, and Pessi A
- Subjects
- Antiviral Agents pharmacology, Drug Design, HEK293 Cells, HIV Infections drug therapy, HIV-1 drug effects, Humans, Peptides pharmacology, Virus Internalization drug effects, Antiviral Agents chemistry, Cholesterol chemistry, Peptides chemistry
- Abstract
Immunoadhesins are engineered proteins combining the constant domain (Fc) of an antibody with a ligand-binding (adhesion) domain. They have significant potential as therapeutic agents, because they maintain the favourable pharmacokinetics of antibodies with an expanded repertoire of ligand-binding domains: proteins, peptides, or small molecules. We have recently reported that the addition of a cholesterol group to two HIV antibodies can dramatically improve their antiviral potency. Cholesterol, which can be conjugated at various positions in the antibody, including the constant (Fc) domain, endows the conjugate with affinity for the membrane lipid rafts, thus increasing its concentration at the site where viral entry occurs. Here, we extend this strategy to an HIV immunoadhesin, combining a cholesterol-conjugated Fc domain with the peptide fusion inhibitor C41. The immunoadhesin C41-Fc-chol displayed high affinity for Human Embryonic Kidney (HEK) 293 cells, and when tested on a panel of HIV-1 strains, it was considerably more potent than the unconjugated C41-Fc construct. Potentiation of antiviral activity was comparable to what was previously observed for the cholesterol-conjugated HIV antibodies. Given the key role of cholesterol in lipid raft formation and viral fusion, we expect that the same strategy should be broadly applicable to enveloped viruses, for many of which it is already known the sequence of a peptide fusion inhibitor similar to C41. Moreover, the sequence of heptad repeat-derived fusion inhibitors can often be predicted from genomic information alone, opening a path to immunoadhesins against emerging viruses., (Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.)
- Published
- 2015
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37. The capacity of UL49.5 proteins to inhibit TAP is widely distributed among members of the genus Varicellovirus.
- Author
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Verweij MC, Lipinska AD, Koppers-Lalic D, van Leeuwen WF, Cohen JI, Kinchington PR, Messaoudi I, Bienkowska-Szewczyk K, Ressing ME, Rijsewijk FA, and Wiertz EJ
- Subjects
- Amino Acid Sequence, Animals, Cattle, Cattle Diseases immunology, Cattle Diseases virology, Cell Line, Herpesviridae Infections virology, Herpesvirus 1, Bovine classification, Herpesvirus 1, Bovine genetics, Humans, Molecular Sequence Data, Phylogeny, Sequence Alignment, Varicellovirus classification, Varicellovirus genetics, Varicellovirus immunology, Viral Envelope Proteins genetics, ATP-Binding Cassette Transporters immunology, Down-Regulation, Herpesviridae Infections immunology, Herpesviridae Infections veterinary, Herpesvirus 1, Bovine immunology, Viral Envelope Proteins immunology
- Abstract
The lifelong infection by varicelloviruses is characterized by a fine balance between the host immune response and immune evasion strategies used by these viruses. Virus-derived peptides are presented to cytotoxic T lymphocytes by major histocompatibility complex (MHC) class I molecules. The transporter associated with antigen processing (TAP) transports the peptides from the cytosol into the endoplasmic reticulum, where the loading of MHC-I molecules occurs. The varicelloviruses bovine herpesvirus 1 (BoHV-1), pseudorabies virus, and equid herpesviruses 1 and 4 have been found to encode a UL49.5 protein that inhibits TAP-mediated peptide transport. To investigate to what extent UL49.5-mediated TAP inhibition is conserved within the family of Alphaherpesvirinae, the homologs of another five varicelloviruses, one mardivirus, and one iltovirus were studied. The UL49.5 proteins of BoHV-5, bubaline herpesvirus 1, cervid herpesvirus 1, and felid herpesvirus 1 were identified as potent TAP inhibitors. The varicella-zoster virus and simian varicellovirus UL49.5 proteins fail to block TAP; this is not due to the absence of viral cofactors that might assist in this process, since cells infected with these viruses did not show reduced TAP function either. The UL49.5 homologs of the mardivirus Marek's disease virus 1 and the iltovirus infectious laryngotracheitis virus did not block TAP, suggesting that the capacity to inhibit TAP via UL49.5 has been acquired by varicelloviruses only. A phylogenetic analysis of viruses that inhibit TAP through their UL49.5 proteins reveals an interesting hereditary pattern, pointing toward the presence of this capacity in defined clades within the genus Varicellovirus.
- Published
- 2011
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