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611 results on '"Hokke, Cornelis H."'

156. Corrigendum to “Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function” [Virology 401 (2010) 236–247]

Author

Eggink, Dirk, primary, Melchers, Mark, additional, Wuhrer, Manfred, additional, van Montfort, Thijs, additional, Dey, Antu K., additional, Naaijkens, Benno A., additional, David, Kathryn B., additional, Le Douce, Valentin, additional, Deelder, André M., additional, Kang, Kenneth, additional, Olson, William C., additional, Berkhout, Ben, additional, Hokke, Cornelis H., additional, Moore, John P., additional, and Sanders, Rogier W., additional

Published
2010
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159. Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function

Author

Eggink, Dirk, primary, Melchers, Mark, additional, Wuhrer, Manfred, additional, van Montfort, Thijs, additional, Dey, Antu K., additional, Naaijkens, Benno A., additional, David, Kathryn B., additional, Le Douce, Valentin, additional, Deelder, André M., additional, Kang, Kenneth, additional, Olson, William C., additional, Berkhout, Ben, additional, Hokke, Cornelis H., additional, Moore, John P., additional, and Sanders, Rogier W., additional

Published
2010
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162. Omega-1, a glycoprotein secreted by Schistosoma mansoni eggs, drives Th2 responses

Author

Everts, Bart, primary, Perona-Wright, Georgia, additional, Smits, Hermelijn H., additional, Hokke, Cornelis H., additional, van der Ham, Alwin J., additional, Fitzsimmons, Colin M., additional, Doenhoff, Michael J., additional, van der Bosch, Jürgen, additional, Mohrs, Katja, additional, Haas, Helmut, additional, Mohrs, Markus, additional, Yazdanbakhsh, Maria, additional, and Schramm, Gabriele, additional

Published
2009
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173. Monomeric Ig A can be produced in planta as efficient as Ig G, yet receives different N-glycans.

Author

Westerhof, Lotte B., Wilbers, Ruud H. P., Raaij, Debbie R., Nguyen, Dieu‐Linh, Goverse, Aska, Henquet, Maurice G. L., Hokke, Cornelis H., Bosch, Dirk, Bakker, Jaap, and Schots, Arjen

Subjects
IMMUNOGLOBULIN A, IMMUNOGLOBULIN G, GLYCANS, CYTOKINES, INFLIXIMAB, ADALIMUMAB, IMMUNOSUPPRESSION, RECOMBINANT proteins
Abstract

The unique features of Ig A, such as the ability to recruit neutrophils and suppress the inflammatory responses mediated by Ig G and Ig E, make it a promising antibody isotype for several therapeutic applications. However, in contrast to Ig G, reports on plant production of Ig A are scarce. We produced Ig A1κ and Ig G1κ versions of three therapeutic antibodies directed against pro-inflammatory cytokines in Nicotiana benthamiana: Infliximab and Adalimumab, directed against TNF-α, and Ustekinumab, directed against the interleukin-12p40 subunit. We evaluated antibody yield, quality and N-glycosylation. All six antibodies had comparable levels of expression between 3.5 and 9% of total soluble protein content and were shown to have neutralizing activity in a cell-based assay. However, Ig A1κ-based Adalimumab and Ustekinumab were poorly secreted compared to their Ig G counterparts. Infliximab was poorly secreted regardless of isotype backbone. This corresponded with the observation that both Ig A1κ- and Ig G1κ-based Infliximab were enriched in oligomannose-type N-glycan structures. For Ig G1κ-based Ustekinumab and Adalimumab, the major N-glycan type was the typical plant complex N-glycan, biantennary with terminal N-acetylglucosamine, β1,2-xylose and core α1,3-fucose. In contrast, the major N-glycan on the Ig A-based antibodies was xylosylated, but lacked core α1,3-fucose and one terminal N-acetylglucosamine. This type of N-glycan occurs usually in marginal percentages in plants and was never shown to be the main fraction of a plant-produced recombinant protein. Our data demonstrate that the antibody isotype may have a profound influence on the type of N-glycan an antibody receives. [ABSTRACT FROM AUTHOR]

Published
2014
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174. Efficient introduction of a bisecting GlcNAc residue in tobacco N-glycans by expression of the gene encoding human N-acetylglucosaminyltransferase III

Author

Rouwendal, Gerard J.A., primary, Wuhrer, Manfred, additional, Florack, Dion E.A., additional, Koeleman, Carolien A.M., additional, Deelder, André M., additional, Bakker, Hans, additional, Stoopen, Geert M., additional, van Die, Irma, additional, Helsper, Johannes P.F.G., additional, Hokke, Cornelis H., additional, and Bosch, Dirk, additional

Published
2006
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179. A multiplexed and miniaturized serological tuberculosis assay identifies antigens that discriminate maximally between TB and non-TB sera

Author

Tong, Miao, primary, Jacobi, Catharina E., additional, van de Rijke, Frans M., additional, Kuijper, Sjoukje, additional, van de Werken, Sjaak, additional, Lowary, Todd L., additional, Hokke, Cornelis H., additional, Appelmelk, Ben J., additional, Nagelkerke, Nico J.D., additional, Tanke, Hans J., additional, van Gijlswijk, Rob P.M., additional, Veuskens, Jacques, additional, Kolk, Arend H.J., additional, and Raap, Anton K., additional

Published
2005
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191. Fasciola hepaticaSurface Tegument: Glycoproteins at the Interface of Parasite and Host*

Author

Ravidà, Alessandra, Cwiklinski, Krystyna, Aldridge, Allison M., Clarke, Paul, Thompson, Roisin, Gerlach, Jared Q., Kilcoyne, Michelle, Hokke, Cornelis H., Dalton, John P., and O'Neill, Sandra M.

Abstract

Fasciola hepatica, commonly known as liver fluke, is a trematode that causes Fasciolosis in ruminants and humans. The outer tegumental coat of F. hepatica(FhTeg) is a complex metabolically active biological matrix that is continually exposed to the host immune system and therefore makes a good vaccine target. F. hepaticategumental coat is highly glycosylated and helminth-derived immunogenic oligosaccharide motifs and glycoproteins are currently being investigated as novel vaccine candidates. This report presents the first systematic characterization of FhTeg glycosylation using lectin microarrays to characterize carbohydrates motifs present, and lectin histochemistry to localize these on the F. hepaticategument. We discovered that FhTeg glycoproteins are predominantly oligomannose oligosaccharides that are expressed on the spines, suckers and tegumental coat of F. hepaticaand lectin blot analysis confirmed the abundance of N- glycosylated proteins. Although some oligosaccharides are widely distributed on the fluke surface other subsets are restricted to distinct anatomical regions. We selectively enriched for FhTeg mannosylated glycoprotein subsets using lectin affinity chromatography and identified 369 proteins by mass spectrometric analysis. Among these proteins are a number of potential vaccine candidates with known immune modulatory properties including proteases, protease inhibitors, paramyosin, Venom Allergen-like II, Enolase and two proteins, nardilysin and TRIL, that have not been previously associated with F. hepatica. Furthermore, we provide a comprehensive insight regarding the putative glycosylation of FhTeg components that could highlight the importance of further studies examining glycoconjugates in host-parasite interactions in the context of F. hepaticainfection and the development of an effective vaccine.

Published
2016
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192. Phase Variation in Helicobacter pylori Lipopolysaccharide due to Changes in the Lengths of Poly(C) Tracts in α3-Fucosyltransferase Genes

Author

Appelmelk, Ben J., primary, Martin, Steve L., additional, Monteiro, Mario A., additional, Clayton, Chris A., additional, McColm, Andrew A., additional, Zheng, Pengyuan, additional, Verboom, Theo, additional, Maaskant, Janneke J., additional, van den Eijnden, Dirk H., additional, Hokke, Cornelis H., additional, Perry, Malcolm B., additional, Vandenbroucke-Grauls, Christina M. J. E., additional, and Kusters, Johannes G., additional

Published
1999
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195. Cross-reactivity of glycan-reactive HIV-1 broadly neutralizing antibodies with parasite glycans.

Author

Huettner, Isabella, Krumm, Stefanie A., Serna, Sonia, Brzezicka, Katarzyna, Monaco, Serena, Walpole, Samuel, van Diepen, Angela, Allan, Fiona, Hicks, Thomas, Kimuda, Simon, Emery, Aidan M., Landais, Elise, Hokke, Cornelis H., Angulo, Jesus, Reichardt, Niels, and Doores, Katie J.

Abstract

The HIV-1 Envelope glycoprotein (Env) is the sole target for broadly neutralizing antibodies (bnAbs). Env is heavily glycosylated with host-derived N -glycans, and many bnAbs bind to, or are dependent upon, Env glycans for neutralization. Although glycan-binding bnAbs are frequently detected in HIV-infected individuals, attempts to elicit them have been unsuccessful because of the poor immunogenicity of Env N -glycans. Here, we report cross-reactivity of glycan-binding bnAbs with self- and non-self N -glycans and glycoprotein antigens from different life-stages of Schistosoma mansoni. Using the IAVI Protocol C HIV infection cohort, we examine the relationship between S. mansoni seropositivity and development of bnAbs targeting glycan-dependent epitopes. We show that the unmutated common ancestor of the N332/V3-specific bnAb lineage PCDN76, isolated from an HIV-infected donor with S. mansoni seropositivity, binds to S. mansoni cercariae while lacking reactivity to gp120. Overall, these results present a strategy for elicitation of glycan-reactive bnAbs which could be exploited in HIV-1 vaccine development. [Display omitted] • Glycan-binding HIV-1 bnAbs cross-react with parasite self- and non-self N -glycans • These bnAbs also bind glycoprotein antigens from different life stages of S. mansoni • Unmutated precursor of an N332/V3 lineage binds S. mansoni antigens but not gp120 Huettner et al. show that glycan-binding HIV-1 broadly neutralizing antibodies (bnAbs) and the unmutated common ancestor of an N332/V3 bnAb lineage cross-react with self- and non-self N -glycans and glycoprotein antigens from the different life stages of Schistosoma mansoni. This presents a potential strategy for elicitation of glycan-reactive bnAbs through vaccination. [ABSTRACT FROM AUTHOR]

Published
2022
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197. Local Antiglycan Antibody Responses to Skin Stage and Migratory Schistosomula of Schistosoma japonicum

Author

Smit, Cornelis H., Kies, Christiaan L., McWilliam, Hamish E. G., Meeusen, Els N. T., Hokke, Cornelis H., and van Diepen, Angela

Abstract

ABSTRACTSchistosomiasis is a tropical disease affecting over 230 million people worldwide. Although effective drug treatment is available, reinfections are common, and development of immunity is slow. Most antibodies raised during schistosome infection are directed against glycans, some of which are thought to be protective. Developing schistosomula are considered most vulnerable to immune attack, and better understanding of local antibody responses raised against glycans expressed by this life stage might reveal possible glycan vaccine candidates for future vaccine research. We used antibody-secreting cell (ASC) probes to characterize local antiglycan antibody responses against migrating Schistosoma japonicumschistosomula in different tissues of rats. Analysis by shotgun Schistosomaglycan microarray resulted in the identification of antiglycan antibody response patterns that reflected the migratory pathway of schistosomula. Antibodies raised by skin lymph node (LN) ASC probes mainly targeted N-glycans with terminal mannose residues, Galβ1-4GlcNAc (LacNAc) and Galβ1-4(Fucα1-3)GlcNAc (LeX). Also, responses to antigenic and schistosome-specific glycosphingolipid (GSL) glycans containing highly fucosylated GalNAcβ1-4(GlcNAcβ1)nstretches that are believed to be present at the parasite's surface constitutively upon transformation were found. Antibody targets recognized by lung LN ASC probes were mainly N-glycans presenting GalNAcβ1-4GlcNAc (LDN) and GlcNAc motifs. Surprisingly, antibodies against highly antigenic multifucosylated motifs of GSL glycans were not observed in lung LN ASC probes, indicating that these antigens are not expressed in lung stage schistosomula or are not appropriately exposed to induce immune responses locally. The local antiglycan responses observed in this study highlight the stage- and tissue-specific expression of antigenic parasite glycans and provide insights into glycan targets possibly involved in resistance to S. japonicuminfection.

Published
2015
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198. Glycomic Analysis of Life Stages of the Human Parasite Schistosoma mansoniReveals Developmental Expression Profiles of Functional and Antigenic Glycan Motifs*[S]

Author

Smit, Cornelis H., van Diepen, Angela, Nguyen, D. Linh, Wuhrer, Manfred, Hoffmann, Karl F., Deelder, André M., and Hokke, Cornelis H.

Abstract

Glycans present on glycoproteins and glycolipids of the major human parasite Schistosoma mansoniinduce innate as well as adaptive immune responses in the host. To be able to study the molecular characteristics of schistosome infections it is therefore required to determine the expression profiles of glycans and antigenic glycan-motifs during a range of critical stages of the complex schistosome lifecycle. We performed a longitudinal profiling study covering schistosome glycosylation throughout worm- and egg-development using a mass spectrometry-based glycomics approach. Our study revealed that during worm development N-glycans with Galβ1–4(Fucα1–3)GlcNAc (LeX) and core-xylose motifs were rapidly lost after cercariae to schistosomula transformation, whereas GalNAcβ1–4GlcNAc (LDN)-motifs gradually became abundant and predominated in adult worms. LeX-motifs were present on glycolipids up to 2 weeks of schistosomula development, whereas glycolipids with mono- and multifucosylated LDN-motifs remained present up to the adult worm stage. In contrast, expression of complex O-glycans diminished to undetectable levels within days after transformation. During egg development, a rich diversity of N-glycans with fucosylated motifs was expressed, but with α3-core fucose and a high degree of multifucosylated antennae only in mature eggs and miracidia. N-glycan antennae were exclusively LDN-based in miracidia. O-glycans in the mature eggs were also diverse and contained LeX- and multifucosylated LDN, but none of these were associated with miracidia in which we detected only the Galβ1–3(Galβ1–6)GalNAc core glycan. Immature eggs also exhibited short O-glycan core structures only, suggesting that complex fucosylated O-glycans of schistosome eggs are derived primarily from glycoproteins produced by the subshell envelope in the developed egg. Lipid glycans with multifucosylated GlcNAc repeats were present throughout egg development, but with the longer highly fucosylated stretches enriched in mature eggs and miracidia. This global analysis of the developing schistosome's glycome provides new insights into how stage-specifically expressed glycans may contribute to different aspects of schistosome-host interactions.

Published
2015
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199. N-glycomic Profiling as a Tool to Separate Rectal Adenomas from Carcinomas*

Author

Kaprio, Tuomas, Satomaa, Tero, Heiskanen, Annamari, Hokke, Cornelis H., Deelder, André M., Mustonen, Harri, Hagström, Jaana, Carpen, Olli, Saarinen, Juhani, and Haglund, Caj

Abstract

All human cells are covered by glycans, the carbohydrate units of glycoproteins, glycolipids, and proteoglycans. Most glycans are localized to cell surfaces and participate in events essential for cell viability and function. Glycosylation evolves during carcinogenesis, and therefore carcinoma-related glycan structures are potential cancer biomarkers. Colorectal cancer is one of the world's three most common cancers, and its incidence is rising. Novel biomarkers are essential to identify patients for targeted and individualized therapy. We compared the N-glycan profiles of five rectal adenomas and 18 rectal carcinomas of different stages by matrix-assisted laser desorption-ionization time-of-flight mass spectrometry. Paraffin-embedded tumor samples were deparaffinized, and glycans were enzymatically released and purified. We found differences in glycosylation between adenomas and carcinomas: monoantennary, sialylated, pauci-mannose, and small high-mannose N-glycan structures were more common in carcinomas than in adenomas. We also found differences between stage I–II and stage III carcinomas. Based on these findings, we selected two glycan structures: pauci-mannose and sialyl Lewis a, for immunohistochemical analysis of their tissue expression in 220 colorectal cancer patients. In colorectal cancer, poor prognosis correlated with elevated expression of sialyl Lewis a, and in advanced colorectal cancer, poor prognosis correlated with elevated expression of pauci-mannose. In conclusion, by mass spectrometry we found several carcinoma related glycans, and we demonstrate a method of transforming these results into immunohistochemistry, a readily applicable method to study biomarker expression in patient samples.

Published
2015
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