Amino acid substitutions in the s2 region enhance severe acute respiratory syndrome coronavirus infectivity in rat angiotensin-converting enzyme 2-expressing cells.
Identifieur interne : 001D59 ( PubMed/Corpus ); précédent : 001D58; suivant : 001D60Amino acid substitutions in the s2 region enhance severe acute respiratory syndrome coronavirus infectivity in rat angiotensin-converting enzyme 2-expressing cells.
Auteurs : Shuetsu Fukushi ; Tetsuya Mizutani ; Kouji Sakai ; Masayuki Saijo ; Fumihiro Taguchi ; Masaru Yokoyama ; Ichiro Kurane ; Shigeru MorikawaSource :
- Journal of virology [ 0022-538X ] ; 2007.
English descriptors
- KwdEn :
- Amino Acid Substitution, Animals, Cell Line, Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Peptidyl-Dipeptidase A (metabolism), Rats, SARS Virus (genetics), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Virus Replication (genetics).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Peptidyl-Dipeptidase A.
- genetics : SARS Virus, Virus Replication.
- physiology : SARS Virus.
- Amino Acid Substitution, Animals, Cell Line, Humans, Rats, Spike Glycoprotein, Coronavirus.
Abstract
To clarify the molecular basis of severe acute respiratory syndrome coronavirus (SARS-CoV) adaptation to different host species, we serially passaged SARS-CoV in rat angiotensin-converting enzyme 2 (ACE2)-expressing cells. After 15 passages, the virus (Rat-P15) came to replicate effectively in rat ACE2-expressing cells. Two amino acid substitutions in the S2 region were found on the Rat-P15 S gene. Analyses of the infectivity of the pseudotype-bearing S protein indicated that the two substitutions in the S2 region, especially the S950F substitution, were responsible for efficient infection. Therefore, virus adaptation to different host species can be induced by amino acid substitutions in the S2 region.
DOI: 10.1128/JVI.01143-07
PubMed: 17652383
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pubmed:17652383Le document en format XML
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uniqKey="Saijo M" first="Masayuki" last="Saijo">Masayuki Saijo</name></author><author><name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name></author><author><name sortKey="Yokoyama, Masaru" sort="Yokoyama, Masaru" uniqKey="Yokoyama M" first="Masaru" last="Yokoyama">Masaru Yokoyama</name></author><author><name sortKey="Kurane, Ichiro" sort="Kurane, Ichiro" uniqKey="Kurane I" first="Ichiro" last="Kurane">Ichiro Kurane</name></author><author><name sortKey="Morikawa, Shigeru" sort="Morikawa, Shigeru" uniqKey="Morikawa S" first="Shigeru" last="Morikawa">Shigeru Morikawa</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17652383</idno><idno type="pmid">17652383</idno><idno type="doi">10.1128/JVI.01143-07</idno><idno type="wicri:Area/PubMed/Corpus">001D59</idno><idno type="wicri:explorRef" wicri:stream="PubMed" 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Sakai</name></author><author><name sortKey="Saijo, Masayuki" sort="Saijo, Masayuki" uniqKey="Saijo M" first="Masayuki" last="Saijo">Masayuki Saijo</name></author><author><name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name></author><author><name sortKey="Yokoyama, Masaru" sort="Yokoyama, Masaru" uniqKey="Yokoyama M" first="Masaru" last="Yokoyama">Masaru Yokoyama</name></author><author><name sortKey="Kurane, Ichiro" sort="Kurane, Ichiro" uniqKey="Kurane I" first="Ichiro" last="Kurane">Ichiro Kurane</name></author><author><name sortKey="Morikawa, Shigeru" sort="Morikawa, Shigeru" uniqKey="Morikawa S" first="Shigeru" last="Morikawa">Shigeru Morikawa</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Rats</term><term>SARS Virus (genetics)</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Virus Replication (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term><term>Virus Replication</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Rats</term><term>Spike Glycoprotein, Coronavirus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To clarify the molecular basis of severe acute respiratory syndrome coronavirus (SARS-CoV) adaptation to different host species, we serially passaged SARS-CoV in rat angiotensin-converting enzyme 2 (ACE2)-expressing cells. After 15 passages, the virus (Rat-P15) came to replicate effectively in rat ACE2-expressing cells. Two amino acid substitutions in the S2 region were found on the Rat-P15 S gene. Analyses of the infectivity of the pseudotype-bearing S protein indicated that the two substitutions in the S2 region, especially the S950F substitution, were responsible for efficient infection. Therefore, virus adaptation to different host species can be induced by amino acid substitutions in the S2 region.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17652383</PMID><DateCompleted><Year>2007</Year><Month>11</Month><Day>06</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>81</Volume><Issue>19</Issue><PubDate><Year>2007</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Amino acid substitutions in the s2 region enhance severe acute respiratory syndrome coronavirus infectivity in rat angiotensin-converting enzyme 2-expressing cells.</ArticleTitle><Pagination><MedlinePgn>10831-4</MedlinePgn></Pagination><Abstract><AbstractText>To clarify the molecular basis of severe acute respiratory syndrome coronavirus (SARS-CoV) adaptation to different host species, we serially passaged SARS-CoV in rat angiotensin-converting enzyme 2 (ACE2)-expressing cells. After 15 passages, the virus (Rat-P15) came to replicate effectively in rat ACE2-expressing cells. Two amino acid substitutions in the S2 region were found on the Rat-P15 S gene. Analyses of the infectivity of the pseudotype-bearing S protein indicated that the two substitutions in the S2 region, especially the S950F substitution, were responsible for efficient infection. Therefore, virus adaptation to different host species can be induced by amino acid substitutions in the S2 region.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fukushi</LastName><ForeName>Shuetsu</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Special Pathogens Laboratory, Department of Virology I, Center for Pathogens Genomics, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama, Tokyo 208-0011, Japan. fukushi@nih.go.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mizutani</LastName><ForeName>Tetsuya</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Sakai</LastName><ForeName>Kouji</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Saijo</LastName><ForeName>Masayuki</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Taguchi</LastName><ForeName>Fumihiro</ForeName><Initials>F</Initials></Author><Author 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