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78 results on '"Trybala, Edward"'

51. Human antibodies to herpes simplex virus type 1 glycoprotein C are neutralizing and target the heparan sulfate-binding domain

Author

Adamiak, Beata, primary, Trybala, Edward, additional, Mardberg, Kristina, additional, Johansson, Maria, additional, Liljeqvist, Jan-Ake, additional, Olofsson, Sigvard, additional, Grabowska, Agnieszka, additional, Bienkowska-Szewczyk, Krystyna, additional, Szewczyk, Boguslaw, additional, and Bergstrom, Tomas, additional

Published
2010
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52. Anti-HSV-1 and anti-HIV-1 activity of gallic acid and pentyl gallate

Author

Kratz, Jadel Müller, primary, Andrighetti-Fröhner, Carla Regina, additional, Kolling, Deise Juliana, additional, Leal, Paulo César, additional, Cirne-Santos, Cláudio César, additional, Yunes, Rosendo Augusto, additional, Nunes, Ricardo José, additional, Trybala, Edward, additional, Bergström, Tomas, additional, Frugulhetti, Izabel CPP, additional, Barardi, Célia Regina Monte, additional, and Simões, Cláudia Maria Oliveira, additional

Published
2008
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53. Evaluation of Anti-HSV-2 Activity of Gallic Acid and Pentyl Gallate

Author

Kratz, Jadel Müller, primary, Andrighetti-Fröhner, Carla Regina, additional, Leal, Paulo César, additional, Nunes, Ricardo José, additional, Yunes, Rosendo Augusto, additional, Trybala, Edward, additional, Bergström, Tomas, additional, Barardi, Célia Regina Monte, additional, and Simões, Cláudia Maria Oliveira, additional

Published
2008
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64. Structural requirement of heparan sulfate for interaction with herpes simplex virus type 1 virions and isolated glycoprotein C

Author

Feyzi, Emadoldin, Trybala, Edward, Bergström, Tomas, Lindahl, Ulf, Spillmann, Dorothe, Feyzi, Emadoldin, Trybala, Edward, Bergström, Tomas, Lindahl, Ulf, and Spillmann, Dorothe

Abstract

Cell surface heparan sulfates mediate primary attachment of herpes simplex virus type 1, the first step in virus invasion of the cells. Removal of the host cell heparan sulfate results in a significantly diminished susceptibility of the cell to virus infection. On the virus envelope, glycoprotein C has been identified as the major binding site for heparan sulfate in the primary attachment of the virus to host cells. Using selectively desulfated heparins and metabolically labeled host cell heparan sulfate, we have analyzed the structural requirements of heparan sulfate to provide binding sites for glycoprotein C and the whole virus. Employing glycoprotein C affinity chromatography and a virus binding assay, we subfractionated oligosaccharides derived from heparan sulfate and partially desulfated heparin into selectively bound and unbound pools. These were chemically depolymerized and analyzed at the disaccharide level. The shortest glycoprotein C-binding fragment consisted of 10-12 monosaccharide units containing at least one 2-O- and one 6-O-sulfate group that have to be localized in a sequence-specific way, based on the finding that bound and unbound HS fragments do not differ in charge or composition. The binding sequence is found within N-sulfated blocks of heparan sulfate, although several N-acetyl groups can be tolerated within the minimal binding sequence. These minimal requirements for herpes simplex virus type 1 binding to heparan sulfate are clearly distinct from other identified protein binding sites.

Published
1997
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75. The Cholestanol-Conjugated Sulfated Oligosaccharide PG545 Disrupts the Lipid Envelope of Herpes Simplex Virus Particles

Author

Said, Joanna S., Trybala, Edward, Görander, Staffan, Ekblad, Maria, Liljeqvist, Jan-Åke, Jennische, Eva, Lange, Stefan, and Bergström, Tomas

Abstract

ABSTRACTHerpes simplex virus (HSV) and many other viruses, including HIV, initiate infection of host cells by binding to glycosaminoglycan (GAG) chains of cell surface proteoglycans. Although GAG mimetics, such as sulfated oligo- and polysaccharides, exhibit potent antiviral activities in cultured cells, the prophylactic application of these inhibitors as vaginal microbicides failed to protect women upon their exposure to HIV. A possible explanation for this failure is that sulfated oligo- and polysaccharides exhibit no typical virucidal activity, as their interaction with viral particles is largely electrostatic and reversible and thereby vulnerable to competition with GAG-binding proteins of the genital tract. Here we report that the cholestanol-conjugated sulfated oligosaccharide PG545, but not several other sulfated oligosaccharides lacking this modification, exhibited virucidal activity manifested as disruption of the lipid envelope of HSV-2 particles. The significance of the virus particle-disrupting activity of PG545 was also demonstrated in experimental animals, as this compound, in contrast to unmodified sulfated oligosaccharide, protected mice against genital infection with HSV-2. Thus, PG545 offers a novel prophylaxis option against infections caused by GAG-binding viruses.

Published
2015
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77. The role of a single N‐linked glycosylation site for a functional epitope of herpes simplex virus type 1 envelope glycoprotein gC.

Author

Olofsson, Sigvard, Bolmstedt, Anders, Biller, Marlene, Mårdberg, Kristina, Leckner, Johan, Malmström, Bo G., Trybala, Edward, and Bergström, Tomas

Abstract

A monoclonal antibody, B1C1, binding to an epitope of antigenic site II of the herpes simplex virus type 1 (HSV‐1) glycoprotein gC‐1, is a potent inhibitor of two important biological functions of gC‐1: its binding to cell surface heparan sulfate and its binding to the receptor for complement factor C3b. Here, we have analyzed a B1C1‐resistant HSV‐1 variant (HSV‐12762/B1C1B4.2), obtained after passage of wild type HSV‐1 (HSV‐12762) in the presence of high concentrations of B1C1. The transport of newly synthesized mutant gC‐1 to the cell surface was comparable to that of wild type glycoprotein, but no binding of surface‐associated mutant gC‐1 to B1C1 was detected. However, mutant and wild type gC‐1 bound equally well to other site II Mabs. Attachment of wild type but not mutant virus was inhibited by B1C1. Sequencing of the mutant gC‐1 gene revealed only one nucleotide change, resulting in replacement of Thr150 by an Ile, in turn destroying an N‐glycosylation site at Asn148. Loss of one complex type N‐linked glycan was confirmed by endoglycosidase digestion and subsequent SDS–polyacrylamide gel electrophoresis. Circular dichroism analysis of purified gC‐1 from cells infected with mutant or wild type virus did not reveal any difference in secondary structure between mutant and wild type gC‐1. It was not possible to obtain a B1C1‐resistant phenotype by nucleotide‐directed mutagenesis of gC‐1 where Asn148 was changed to a glutamine. These data demonstrated that the threonine of the glycosylation site and not the N‐linked glycan in itself was essential for B1C1 binding [ABSTRACT FROM PUBLISHER]

Published
1999
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78. Antiviral Rotenoids and Isoflavones Isolated from Millettia oblata ssp. teitensis .

Author

Kiganda I, Bogaerts J, Wieske LHE, Deyou T, Atilaw Y, Uwamariya C, Miah M, Said J, Ndakala A, Akala HM, Herrebout W, Trybala E, Bergström T, Yenesew A, and Erdelyi M

Subjects
Molecular Structure, Humans, Rotenone pharmacology, Rotenone chemistry, Rotenone analogs & derivatives, Plant Leaves chemistry, Plant Roots chemistry, Respiratory Syncytial Virus, Human drug effects, Respiratory Syncytial Viruses drug effects, Isoflavones pharmacology, Isoflavones chemistry, Isoflavones isolation & purification, Antiviral Agents pharmacology, Antiviral Agents chemistry, Antiviral Agents isolation & purification, Millettia chemistry
Abstract

Three new ( 1 - 3 ) and six known rotenoids ( 5 - 10 ), along with three known isoflavones ( 11 - 13 ), were isolated from the leaves of Millettia oblata ssp. teitensis . A new glycosylated isoflavone ( 4 ), four known isoflavones ( 14 - 18 ), and one known chalcone ( 19 ) were isolated from the root wood extract of the same plant. The structures were elucidated by NMR and mass spectrometric analyses. The absolute configuration of the chiral compounds was established by a comparison of experimental ECD and VCD data with those calculated for the possible stereoisomers. This is the first report on the use of VCD to assign the absolute configuration of rotenoids. The crude leaves and root wood extracts displayed anti-RSV (human respiratory syncytial virus) activity with IC 50 values of 0.7 and 3.4 μg/mL, respectively. Compounds 6 , 8 , 10 , 11 , and 14 showed anti-RSV activity with IC 50 values of 0.4-10 μM, while compound 3 exhibited anti-HRV-2 (human rhinovirus 2) activity with an IC 50 of 4.2 μM. Most of the compounds showed low cytotoxicity for laryngeal carcinoma (HEp-2) cells; however compounds 3 , 11 , and 14 exhibited low cytotoxicity also in primary lung fibroblasts. This is the first report on rotenoids showing antiviral activity against RSV and HRV viruses.

Published
2024
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