Targeting N-Glycan Cryptic Sugar Moieties for Broad-Spectrum Virus Neutralization: Progress in Identifying Conserved Molecular Targets in Viruses of Distinct Phylogenetic Origins
Identifieur interne : 002A49 ( Ncbi/Curation ); précédent : 002A48; suivant : 002A50Targeting N-Glycan Cryptic Sugar Moieties for Broad-Spectrum Virus Neutralization: Progress in Identifying Conserved Molecular Targets in Viruses of Distinct Phylogenetic Origins
Auteurs : Denong Wang ; Jin Tang ; Jiulai Tang ; Lai-Xi Wang [États-Unis]Source :
- Molecules [ 1420-3049 ] ; 2015.
Descripteurs français
- KwdFr :
- Analyse par réseau de protéines (), Anticorps anti-VIH, Anticorps monoclonaux (), Anticorps monoclonaux (métabolisme), Cartographie épitopique, Cellules HEK293, Cytomegalovirus (génétique), Cytomegalovirus (immunologie), Glycosylation, Humains, Lectines liant le mannose (), Lectines liant le mannose (métabolisme), Lectines végétales (), Lectines végétales (métabolisme), Phylogénie, Polyosides (), Polyosides (immunologie), Polyosides (métabolisme), Projets pilotes, Séquence conservée, Séquence d'acides aminés, VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (génétique), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (immunologie), Virus du SRAS (génétique), Virus du SRAS (immunologie).
- MESH :
- génétique : Cytomegalovirus, VIH-1 (Virus de l'Immunodéficience Humaine de type 1), Virus du SRAS.
- immunologie : Cytomegalovirus, Polyosides, VIH-1 (Virus de l'Immunodéficience Humaine de type 1), Virus du SRAS.
- métabolisme : Anticorps monoclonaux, Lectines liant le mannose, Lectines végétales, Polyosides.
- Analyse par réseau de protéines, Anticorps anti-VIH, Anticorps monoclonaux, Cartographie épitopique, Cellules HEK293, Glycosylation, Humains, Lectines liant le mannose, Lectines végétales, Phylogénie, Polyosides, Projets pilotes, Séquence conservée, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Antibodies, Monoclonal (chemistry), Antibodies, Monoclonal (metabolism), Broadly Neutralizing Antibodies, Conserved Sequence, Cytomegalovirus (genetics), Cytomegalovirus (immunology), Epitope Mapping, Glycosylation, HEK293 Cells, HIV Antibodies, HIV-1 (genetics), HIV-1 (immunology), Humans, Mannose-Binding Lectins (chemistry), Mannose-Binding Lectins (metabolism), Phylogeny, Pilot Projects, Plant Lectins (chemistry), Plant Lectins (metabolism), Polysaccharides (chemistry), Polysaccharides (immunology), Polysaccharides (metabolism), Protein Array Analysis (methods), SARS Virus (genetics), SARS Virus (immunology).
- MESH :
- chemical , chemistry : Antibodies, Monoclonal, Mannose-Binding Lectins, Plant Lectins, Polysaccharides.
- chemical , immunology : Polysaccharides.
- chemical , metabolism : Antibodies, Monoclonal, Mannose-Binding Lectins, Plant Lectins, Polysaccharides.
- genetics : Cytomegalovirus, HIV-1, SARS Virus.
- immunology : Cytomegalovirus, HIV-1, SARS Virus.
- methods : Protein Array Analysis.
- Amino Acid Sequence, Broadly Neutralizing Antibodies, Conserved Sequence, Epitope Mapping, Glycosylation, HEK293 Cells, HIV Antibodies, Humans, Phylogeny, Pilot Projects.
Abstract
Identifying molecular targets for eliciting broadly virus-neutralizing antibodies is one of the key steps toward development of vaccines against emerging viral pathogens. Owing to genomic and somatic diversities among viral species, identifying protein targets for broad-spectrum virus neutralization is highly challenging even for the same virus, such as HIV-1. However, viruses rely on host glycosylation machineries to synthesize and express glycans and, thereby, may display common carbohydrate moieties. Thus, exploring glycan-binding profiles of broad-spectrum virus-neutralizing agents may provide key information to uncover the carbohydrate-based virus-neutralizing epitopes. In this study, we characterized two broadly HIV-neutralizing agents, human monoclonal antibody 2G12 and Galanthus nivalis lectin (GNA), for their viral targeting activities. Although these agents were known to be specific for oligomannosyl antigens, they differ strikingly in virus-binding activities. The former is HIV-1 specific; the latter is broadly reactive and is able to neutralize viruses of distinct phylogenetic origins, such as HIV-1, severe acute respiratory syndrome coronavirus (SARS-CoV), and human cytomegalovirus (HCMV). In carbohydrate microarray analyses, we explored the molecular basis underlying the striking differences in the spectrum of anti-virus activities of the two probes. Unlike 2G12, which is strictly specific for the high-density Man9GlcNAc2Asn (Man9)-clusters, GNA recognizes a number of N-glycan cryptic sugar moieties. These include not only the known oligomannosyl antigens but also previously unrecognized tri-antennary or multi-valent GlcNAc-terminating N-glycan epitopes (Tri/m-Gn). These findings highlight the potential of N-glycan cryptic sugar moieties as conserved targets for broad-spectrum virus neutralization and suggest the GNA-model of glycan-binding warrants focused investigation.
Url:
DOI: 10.3390/molecules20034610
PubMed: 25774492
PubMed Central: 4633014
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PMC:4633014Le document en format XML
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<affiliation><nlm:aff id="af1-molecules-20-04610">Tumor Glycomics Laboratory, SRI International Biosciences Division, Menlo Park, CA 94025, USA; E-Mail:<email>jiafengjushi@live.com</email>
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<author><name sortKey="Tang, Jin" sort="Tang, Jin" uniqKey="Tang J" first="Jin" last="Tang">Jin Tang</name>
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<term>Antibodies, Monoclonal (chemistry)</term>
<term>Antibodies, Monoclonal (metabolism)</term>
<term>Broadly Neutralizing Antibodies</term>
<term>Conserved Sequence</term>
<term>Cytomegalovirus (genetics)</term>
<term>Cytomegalovirus (immunology)</term>
<term>Epitope Mapping</term>
<term>Glycosylation</term>
<term>HEK293 Cells</term>
<term>HIV Antibodies</term>
<term>HIV-1 (genetics)</term>
<term>HIV-1 (immunology)</term>
<term>Humans</term>
<term>Mannose-Binding Lectins (chemistry)</term>
<term>Mannose-Binding Lectins (metabolism)</term>
<term>Phylogeny</term>
<term>Pilot Projects</term>
<term>Plant Lectins (chemistry)</term>
<term>Plant Lectins (metabolism)</term>
<term>Polysaccharides (chemistry)</term>
<term>Polysaccharides (immunology)</term>
<term>Polysaccharides (metabolism)</term>
<term>Protein Array Analysis (methods)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (immunology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Analyse par réseau de protéines ()</term>
<term>Anticorps anti-VIH</term>
<term>Anticorps monoclonaux ()</term>
<term>Anticorps monoclonaux (métabolisme)</term>
<term>Cartographie épitopique</term>
<term>Cellules HEK293</term>
<term>Cytomegalovirus (génétique)</term>
<term>Cytomegalovirus (immunologie)</term>
<term>Glycosylation</term>
<term>Humains</term>
<term>Lectines liant le mannose ()</term>
<term>Lectines liant le mannose (métabolisme)</term>
<term>Lectines végétales ()</term>
<term>Lectines végétales (métabolisme)</term>
<term>Phylogénie</term>
<term>Polyosides ()</term>
<term>Polyosides (immunologie)</term>
<term>Polyosides (métabolisme)</term>
<term>Projets pilotes</term>
<term>Séquence conservée</term>
<term>Séquence d'acides aminés</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (génétique)</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (immunologie)</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (immunologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Mannose-Binding Lectins</term>
<term>Plant Lectins</term>
<term>Polysaccharides</term>
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<term>Mannose-Binding Lectins</term>
<term>Plant Lectins</term>
<term>Polysaccharides</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cytomegalovirus</term>
<term>HIV-1</term>
<term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cytomegalovirus</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term>
<term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Cytomegalovirus</term>
<term>Polyosides</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term>
<term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Cytomegalovirus</term>
<term>HIV-1</term>
<term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Protein Array Analysis</term>
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<term>Lectines liant le mannose</term>
<term>Lectines végétales</term>
<term>Polyosides</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Broadly Neutralizing Antibodies</term>
<term>Conserved Sequence</term>
<term>Epitope Mapping</term>
<term>Glycosylation</term>
<term>HEK293 Cells</term>
<term>HIV Antibodies</term>
<term>Humans</term>
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<term>Anticorps anti-VIH</term>
<term>Anticorps monoclonaux</term>
<term>Cartographie épitopique</term>
<term>Cellules HEK293</term>
<term>Glycosylation</term>
<term>Humains</term>
<term>Lectines liant le mannose</term>
<term>Lectines végétales</term>
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<term>Polyosides</term>
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<front><div type="abstract" xml:lang="en"><p>Identifying molecular targets for eliciting broadly virus-neutralizing antibodies is one of the key steps toward development of vaccines against emerging viral pathogens. Owing to genomic and somatic diversities among viral species, identifying protein targets for broad-spectrum virus neutralization is highly challenging even for the same virus, such as HIV-1. However, viruses rely on host glycosylation machineries to synthesize and express glycans and, thereby, may display common carbohydrate moieties. Thus, exploring glycan-binding profiles of broad-spectrum virus-neutralizing agents may provide key information to uncover the carbohydrate-based virus-neutralizing epitopes. In this study, we characterized two broadly HIV-neutralizing agents, human monoclonal antibody 2G12 and Galanthus nivalis lectin (GNA), for their viral targeting activities. Although these agents were known to be specific for oligomannosyl antigens, they differ strikingly in virus-binding activities. The former is HIV-1 specific; the latter is broadly reactive and is able to neutralize viruses of distinct phylogenetic origins, such as HIV-1, severe acute respiratory syndrome coronavirus (SARS-CoV), and human cytomegalovirus (HCMV). In carbohydrate microarray analyses, we explored the molecular basis underlying the striking differences in the spectrum of anti-virus activities of the two probes. Unlike 2G12, which is strictly specific for the high-density Man<sub>9</sub>
GlcNAc<sub>2</sub>
Asn (Man9)-clusters, GNA recognizes a number of N-glycan cryptic sugar moieties. These include not only the known oligomannosyl antigens but also previously unrecognized tri-antennary or multi-valent GlcNAc-terminating N-glycan epitopes (Tri/m-Gn). These findings highlight the potential of N-glycan cryptic sugar moieties as conserved targets for broad-spectrum virus neutralization and suggest the GNA-model of glycan-binding warrants focused investigation.</p>
</div>
</front>
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<author><name sortKey="Trummer, B J" uniqKey="Trummer B">B.J. Trummer</name>
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<author><name sortKey="Deng, C" uniqKey="Deng C">C. Deng</name>
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<author><name sortKey="Wang, A" uniqKey="Wang A">A. Wang</name>
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