Single amino acid substitutions in the severe acute respiratory syndrome coronavirus spike glycoprotein determine viral entry and immunogenicity of a major neutralizing domain.
Identifieur interne : 002557 ( PubMed/Corpus ); précédent : 002556; suivant : 002558Single amino acid substitutions in the severe acute respiratory syndrome coronavirus spike glycoprotein determine viral entry and immunogenicity of a major neutralizing domain.
Auteurs : Christopher E. Yi ; Lei Ba ; Linqi Zhang ; David D. Ho ; Zhiwei ChenSource :
- Journal of virology [ 0022-538X ] ; 2005.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Animals, Antibodies, Viral (biosynthesis), Antigens, Viral (chemistry), Antigens, Viral (genetics), Cell Line, Female, Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Membrane Glycoproteins (physiology), Mice, Mice, Inbred BALB C, Microscopy, Electron, Mutagenesis, Site-Directed, Neutralization Tests, Protein Structure, Tertiary, SARS Virus (genetics), SARS Virus (immunology), SARS Virus (pathogenicity), SARS Virus (physiology), Sequence Deletion, Spike Glycoprotein, Coronavirus, Vaccines, DNA (administration & dosage), Vaccines, DNA (genetics), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Viral Envelope Proteins (physiology), Viral Vaccines (administration & dosage), Viral Vaccines (genetics), Virulence (genetics), Virulence (immunology), Virulence (physiology).
- MESH :
- chemical , administration & dosage : Vaccines, DNA, Viral Vaccines.
- chemical , biosynthesis : Antibodies, Viral.
- chemical , chemistry : Antigens, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Antigens, Viral, Membrane Glycoproteins, Vaccines, DNA, Viral Envelope Proteins, Viral Vaccines.
- chemical , immunology : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , physiology : Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : SARS Virus, Virulence.
- immunology : SARS Virus, Virulence.
- pathogenicity : SARS Virus.
- physiology : SARS Virus, Virulence.
- Amino Acid Sequence, Amino Acid Substitution, Animals, Cell Line, Female, Humans, Mice, Mice, Inbred BALB C, Microscopy, Electron, Mutagenesis, Site-Directed, Neutralization Tests, Protein Structure, Tertiary, Sequence Deletion, Spike Glycoprotein, Coronavirus.
Abstract
Neutralizing antibodies (NAbs) against severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) spike (S) glycoprotein confer protection to animals experimentally infected with the pathogenic virus. We and others previously demonstrated that a major mechanism for neutralizing SARS-CoV was through blocking the interaction between the S glycoprotein and the cellular receptor angiotensin-converting enzyme 2 (ACE2). In this study, we used in vivo electroporation DNA immunization and a pseudovirus-based assay to functionally evaluate immunogenicity and viral entry. We characterized the neutralization and viral entry determinants within the ACE2-binding domain of the S glycoprotein. The deletion of a positively charged region Sdelta(422-463) abolished the capacity of the S glycoprotein to induce NAbs in mice vaccinated by in vivo DNA electroporation. Moreover, the Sdelta(422-463) pseudovirus was unable to infect HEK293T-ACE2 cells. To determine the specific residues that contribute to related phenotypes, we replaced eight basic amino acids with alanine. We found that a single amino acid substitution (R441A) in the full-length S DNA vaccine failed to induce NAbs and abolished viral entry when pseudoviruses were generated. However, another substitution (R453A) abolished viral entry while retaining the capacity for inducing NAbs. The difference between R441A and R453A suggests that the determinants for immunogenicity and viral entry may not be identical. Our findings provide direct evidence that these basic residues are essential for immunogenicity of the major neutralizing domain and for viral entry. Our data have implications for the rational design of vaccine and antiviral agents as well as for understanding viral tropism.
DOI: 10.1128/JVI.79.18.11638-11646.2005
PubMed: 16140741
Links to Exploration step
pubmed:16140741Le document en format XML
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We and others previously demonstrated that a major mechanism for neutralizing SARS-CoV was through blocking the interaction between the S glycoprotein and the cellular receptor angiotensin-converting enzyme 2 (ACE2). In this study, we used in vivo electroporation DNA immunization and a pseudovirus-based assay to functionally evaluate immunogenicity and viral entry. We characterized the neutralization and viral entry determinants within the ACE2-binding domain of the S glycoprotein. The deletion of a positively charged region Sdelta(422-463) abolished the capacity of the S glycoprotein to induce NAbs in mice vaccinated by in vivo DNA electroporation. Moreover, the Sdelta(422-463) pseudovirus was unable to infect HEK293T-ACE2 cells. To determine the specific residues that contribute to related phenotypes, we replaced eight basic amino acids with alanine. We found that a single amino acid substitution (R441A) in the full-length S DNA vaccine failed to induce NAbs and abolished viral entry when pseudoviruses were generated. However, another substitution (R453A) abolished viral entry while retaining the capacity for inducing NAbs. The difference between R441A and R453A suggests that the determinants for immunogenicity and viral entry may not be identical. Our findings provide direct evidence that these basic residues are essential for immunogenicity of the major neutralizing domain and for viral entry. Our data have implications for the rational design of vaccine and antiviral agents as well as for understanding viral tropism.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16140741</PMID><DateCompleted><Year>2005</Year><Month>10</Month><Day>05</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>79</Volume><Issue>18</Issue><PubDate><Year>2005</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Single amino acid substitutions in the severe acute respiratory syndrome coronavirus spike glycoprotein determine viral entry and immunogenicity of a major neutralizing domain.</ArticleTitle><Pagination><MedlinePgn>11638-46</MedlinePgn></Pagination><Abstract><AbstractText>Neutralizing antibodies (NAbs) against severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) spike (S) glycoprotein confer protection to animals experimentally infected with the pathogenic virus. We and others previously demonstrated that a major mechanism for neutralizing SARS-CoV was through blocking the interaction between the S glycoprotein and the cellular receptor angiotensin-converting enzyme 2 (ACE2). In this study, we used in vivo electroporation DNA immunization and a pseudovirus-based assay to functionally evaluate immunogenicity and viral entry. We characterized the neutralization and viral entry determinants within the ACE2-binding domain of the S glycoprotein. The deletion of a positively charged region Sdelta(422-463) abolished the capacity of the S glycoprotein to induce NAbs in mice vaccinated by in vivo DNA electroporation. Moreover, the Sdelta(422-463) pseudovirus was unable to infect HEK293T-ACE2 cells. To determine the specific residues that contribute to related phenotypes, we replaced eight basic amino acids with alanine. We found that a single amino acid substitution (R441A) in the full-length S DNA vaccine failed to induce NAbs and abolished viral entry when pseudoviruses were generated. However, another substitution (R453A) abolished viral entry while retaining the capacity for inducing NAbs. The difference between R441A and R453A suggests that the determinants for immunogenicity and viral entry may not be identical. Our findings provide direct evidence that these basic residues are essential for immunogenicity of the major neutralizing domain and for viral entry. Our data have implications for the rational design of vaccine and antiviral agents as well as for understanding viral tropism.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yi</LastName><ForeName>Christopher E</ForeName><Initials>CE</Initials><AffiliationInfo><Affiliation>Aaron Diamond AIDS Research Center, The Rockefeller University, 455 1st Avenue, 7th Floor, New York, NY 10016, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ba</LastName><ForeName>Lei</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Linqi</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Ho</LastName><ForeName>David D</ForeName><Initials>DD</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Zhiwei</ForeName><Initials>Z</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 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