Functional characterization of heptad repeat 1 and 2 mutants of the spike protein of severe acute respiratory syndrome coronavirus.
Identifieur interne : 002310 ( PubMed/Corpus ); précédent : 002309; suivant : 002311Functional characterization of heptad repeat 1 and 2 mutants of the spike protein of severe acute respiratory syndrome coronavirus.
Auteurs : Woan-Eng Chan ; Chin-Kai Chuang ; Shiou-Hwei Yeh ; Mau-Sun Chang ; Steve S-L ChenSource :
- Journal of virology [ 0022-538X ] ; 2006.
English descriptors
- KwdEn :
- Amino Acid Substitution, Animals, Biotinylation, Cell Line, Chloramphenicol O-Acetyltransferase (metabolism), Chlorocebus aethiops, Humans, Luciferases (metabolism), Membrane Fusion, Models, Molecular, Molecular Weight, Precipitin Tests, Proline (metabolism), Protein Structure, Secondary, Protein Structure, Tertiary, Repetitive Sequences, Amino Acid (genetics), SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (metabolism), Vero Cells, Viral Fusion Proteins (metabolism).
- MESH :
- chemical , metabolism : Chloramphenicol O-Acetyltransferase, Luciferases, Proline, Viral Fusion Proteins.
- chemistry : SARS Virus.
- genetics : Repetitive Sequences, Amino Acid, SARS Virus.
- metabolism : SARS Virus.
- Amino Acid Substitution, Animals, Biotinylation, Cell Line, Chlorocebus aethiops, Humans, Membrane Fusion, Models, Molecular, Molecular Weight, Precipitin Tests, Protein Structure, Secondary, Protein Structure, Tertiary, Vero Cells.
Abstract
To understand the roles of heptad repeat 1(HR1) and HR2 of the spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) in virus-cell interactions, the conserved Leu or Ile residues located at positions 913, 927, 941, and 955 in HR1 and 1151, 1165, and 1179 in HR2 were individually replaced with an alpha-helix-breaker Pro residue. The 913P mutant was expressed mainly as a faster-migrating, lower-molecular-weight S(L) form, while the wild type and all other mutants produced similar levels of both the S(L) form and the slower-migrating, higher-molecular-weight S(H) form. The wild-type S(L) form was processed to the S(H) form, whereas the S(L) form of the 913P mutant was inefficiently converted to the S(H) form after biosynthesis. None of these mutations affected cell surface expression or binding to its cognate ACE2 receptor. In a human immunodeficiency virus type 1/SARS S coexpression study, all mutants except the 913P mutant incorporated the S(H) form into the virions as effectively as did the wild-type S(H) form. The mutation at Ile-1151 did not affect membrane fusion or viral entry. The impaired viral entry of the 927P, 941P, 955P, and 1165P mutants was due to their inability to mediate membrane fusion, whereas the defect in viral entry of the 1179P mutant occurred not at the stage of membrane fusion but rather at a postfusion stage. Our study demonstrates the functional importance of HR1 and HR2 of the SARS-CoV spike protein in membrane fusion and viral entry.
DOI: 10.1128/JVI.80.7.3225-3237.2006
PubMed: 16537590
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The 913P mutant was expressed mainly as a faster-migrating, lower-molecular-weight S(L) form, while the wild type and all other mutants produced similar levels of both the S(L) form and the slower-migrating, higher-molecular-weight S(H) form. The wild-type S(L) form was processed to the S(H) form, whereas the S(L) form of the 913P mutant was inefficiently converted to the S(H) form after biosynthesis. None of these mutations affected cell surface expression or binding to its cognate ACE2 receptor. In a human immunodeficiency virus type 1/SARS S coexpression study, all mutants except the 913P mutant incorporated the S(H) form into the virions as effectively as did the wild-type S(H) form. The mutation at Ile-1151 did not affect membrane fusion or viral entry. The impaired viral entry of the 927P, 941P, 955P, and 1165P mutants was due to their inability to mediate membrane fusion, whereas the defect in viral entry of the 1179P mutant occurred not at the stage of membrane fusion but rather at a postfusion stage. Our study demonstrates the functional importance of HR1 and HR2 of the SARS-CoV spike protein in membrane fusion and viral entry.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16537590</PMID><DateCompleted><Year>2006</Year><Month>04</Month><Day>13</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>80</Volume><Issue>7</Issue><PubDate><Year>2006</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Functional characterization of heptad repeat 1 and 2 mutants of the spike protein of severe acute respiratory syndrome coronavirus.</ArticleTitle><Pagination><MedlinePgn>3225-37</MedlinePgn></Pagination><Abstract><AbstractText>To understand the roles of heptad repeat 1(HR1) and HR2 of the spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) in virus-cell interactions, the conserved Leu or Ile residues located at positions 913, 927, 941, and 955 in HR1 and 1151, 1165, and 1179 in HR2 were individually replaced with an alpha-helix-breaker Pro residue. The 913P mutant was expressed mainly as a faster-migrating, lower-molecular-weight S(L) form, while the wild type and all other mutants produced similar levels of both the S(L) form and the slower-migrating, higher-molecular-weight S(H) form. The wild-type S(L) form was processed to the S(H) form, whereas the S(L) form of the 913P mutant was inefficiently converted to the S(H) form after biosynthesis. None of these mutations affected cell surface expression or binding to its cognate ACE2 receptor. In a human immunodeficiency virus type 1/SARS S coexpression study, all mutants except the 913P mutant incorporated the S(H) form into the virions as effectively as did the wild-type S(H) form. The mutation at Ile-1151 did not affect membrane fusion or viral entry. The impaired viral entry of the 927P, 941P, 955P, and 1165P mutants was due to their inability to mediate membrane fusion, whereas the defect in viral entry of the 1179P mutant occurred not at the stage of membrane fusion but rather at a postfusion stage. Our study demonstrates the functional importance of HR1 and HR2 of the SARS-CoV spike protein in membrane fusion and viral entry.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chan</LastName><ForeName>Woan-Eng</ForeName><Initials>WE</Initials><AffiliationInfo><Affiliation>Institute of Biomedical Sciences, Academia Sinica, Nankang, Taipei 11529, Taiwan, Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chuang</LastName><ForeName>Chin-Kai</ForeName><Initials>CK</Initials></Author><Author ValidYN="Y"><LastName>Yeh</LastName><ForeName>Shiou-Hwei</ForeName><Initials>SH</Initials></Author><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>Mau-Sun</ForeName><Initials>MS</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Steve S-L</ForeName><Initials>SS</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative 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HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:16537590" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |