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 : 000E42 ( PubMed/Corpus ); précédent : 000E41; suivant : 000E43Targeting 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 WangSource :
- Molecules (Basel, Switzerland) [ 1420-3049 ] ; 2015.
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.
DOI: 10.3390/molecules20034610
PubMed: 25774492
Links to Exploration step
pubmed:25774492Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Targeting N-glycan cryptic sugar moieties for broad-spectrum virus neutralization: progress in identifying conserved molecular targets in viruses of distinct phylogenetic origins.</title><author><name sortKey="Wang, Denong" sort="Wang, Denong" uniqKey="Wang D" first="Denong" last="Wang">Denong Wang</name><affiliation><nlm:affiliation>Tumor Glycomics Laboratory, SRI International Biosciences Division, Menlo Park, CA 94025, USA. denong.wang@sri.com.</nlm:affiliation></affiliation></author><author><name sortKey="Tang, Jin" sort="Tang, Jin" uniqKey="Tang J" first="Jin" last="Tang">Jin Tang</name><affiliation><nlm:affiliation>Tumor Glycomics Laboratory, SRI International Biosciences Division, Menlo Park, CA 94025, USA. jiafengjushi@live.com.</nlm:affiliation></affiliation></author><author><name sortKey="Tang, Jiulai" sort="Tang, Jiulai" uniqKey="Tang J" first="Jiulai" last="Tang">Jiulai Tang</name><affiliation><nlm:affiliation>Department of Pediatrics, The First Affiliated Hospital of Anhui Medical University, Hefei 230032, China. tangjiulai8888@21cn.com.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Lai Xi" sort="Wang, Lai Xi" uniqKey="Wang L" first="Lai-Xi" last="Wang">Lai-Xi Wang</name><affiliation><nlm:affiliation>Instituteof Human Virology, Department of Biochemistry & Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. 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LWang@ihv.umaryland.edu.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Molecules (Basel, Switzerland)</title><idno type="eISSN">1420-3049</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><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="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Mannose-Binding Lectins</term><term>Plant Lectins</term><term>Polysaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Polysaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Mannose-Binding Lectins</term><term>Plant Lectins</term><term>Polysaccharides</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cytomegalovirus</term><term>HIV-1</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Cytomegalovirus</term><term>HIV-1</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Protein Array Analysis</term></keywords><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><term>Phylogeny</term><term>Pilot Projects</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25774492</PMID><DateCompleted><Year>2015</Year><Month>11</Month><Day>30</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1420-3049</ISSN><JournalIssue CitedMedium="Internet"><Volume>20</Volume><Issue>3</Issue><PubDate><Year>2015</Year><Month>Mar</Month><Day>12</Day></PubDate></JournalIssue><Title>Molecules (Basel, Switzerland)</Title><ISOAbbreviation>Molecules</ISOAbbreviation></Journal><ArticleTitle>Targeting N-glycan cryptic sugar moieties for broad-spectrum virus neutralization: progress in identifying conserved molecular targets in viruses of distinct phylogenetic origins.</ArticleTitle><Pagination><MedlinePgn>4610-22</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3390/molecules20034610</ELocationID><Abstract><AbstractText>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. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Denong</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Tumor Glycomics Laboratory, SRI International Biosciences Division, Menlo Park, CA 94025, USA. denong.wang@sri.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tang</LastName><ForeName>Jin</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Tumor Glycomics Laboratory, SRI International Biosciences Division, Menlo Park, CA 94025, USA. jiafengjushi@live.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tang</LastName><ForeName>Jiulai</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Pediatrics, The First Affiliated Hospital of Anhui Medical University, Hefei 230032, China. tangjiulai8888@21cn.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Lai-Xi</ForeName><Initials>LX</Initials><AffiliationInfo><Affiliation>Instituteof Human Virology, Department of Biochemistry & Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. LWang@ihv.umaryland.edu.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, University of Maryland at College Park, College Park, MD 20742, USA. LWang@ihv.umaryland.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI113896</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01AI113896</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R56AI108388</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R56 AI108388</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U01 CA128416</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, 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|texte= Targeting N-glycan cryptic sugar moieties for broad-spectrum virus neutralization: progress in identifying conserved molecular targets in viruses of distinct phylogenetic origins.
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