Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer
Identifieur interne : 000351 ( Istex/Corpus ); précédent : 000350; suivant : 000352Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer
Auteurs : David Cavanagh ; Philip J. Davis ; Darryl J. C. PappinSource :
- Virus Research [ 0168-1702 ] ; 1986.
English descriptors
- Teeft :
- Acid sequencing, Amino acid residues, Binns, Boursnell, Bromelain, Cavanagh, Chymotrypsin, Cleavage, Coronavirus, Glycans, Glycopolypeptide, Glycopolypeptides, Hydrophobic sequence, Isoleucine, Isoleucine residues, Molecular weight, Nucleotide sequence analysis, Outer membrane surface, Papain, Polypeptide, Pronase, Protease, Proteinase, Residue, Saponin, Sequencing, Several proteases, Small amount, Spike, Subtilisin, Trypsin, Viral, Virion, Virus membrane.
Abstract
Abstract: [35S]methionine-labelled avian infectious bronchitis virus (IBV) (strain 41) and its purified protein components and virions of IBV-Beaudette were incubated with 10 proteases. Several proteases hydrolysed all or some of the membrane glycopoly-peptide (M; Mr 30K) and removed about 1.3K of peptide from the amino-(N-)-terminus plus both glycans, as determined by SDS-polyacrylamide gel electrophoresis. N-terminal analysis of [3H]isoleucine-labelled M after hydrolysis by bromelain revealed that the first nine residues had been removed. After the virions had been permeabilised with saponin, a further 2.5K decrease in molecular weight was produced and this was shown to be from the carboxy-(C-)terminus. When considered with the hydropathicity plot analysis of the amino acid sequence of M (Boursnell, M.E.G. et al., 1984, Virus Res. 1, 303–313) these results suggest that as few as 9–20 N-terminal amino acid residues may protrude at the outer membrane surface and that there is a highly protease sensitive sequence of an estimated 20–25 residues at the C-terminus of M exposed in the lumen of the virion. S2 but not SI was cleaved to a major glycopolypeptide of approximately 71K by several proteases, and to 76K by trypsin. N-terminal sequencing of the 71K glycopolypeptide revealed that it had the same N-terminus as intact S2. After hydrolysis in the presence and absence of saponin it was concluded that S2 is very sensitive to hydrolysis near its carboxy terminus at residues close to the outer membrane surface.
Url:
DOI: 10.1016/0168-1702(86)90038-9
Links to Exploration step
ISTEX:A8F422E0ECB35CFED53D87C278AFAD8BBDE70433Le document en format XML
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PE17 2DA, U.K.</mods:affiliation></affiliation></author><author><name sortKey="Davis, Philip J" sort="Davis, Philip J" uniqKey="Davis P" first="Philip J." last="Davis">Philip J. Davis</name><affiliation><mods:affiliation>Houghton Poultry Research Station, Houghton, Huntingdon, Cambs. PE17 2DA, U.K.</mods:affiliation></affiliation></author><author><name sortKey="Pappin, Darryl J C" sort="Pappin, Darryl J C" uniqKey="Pappin D" first="Darryl J. C." last="Pappin">Darryl J. C. Pappin</name><affiliation><mods:affiliation>Department of Biochemistry, University of Leeds, Leeds LS2 9JT, U.K.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Virus Research</title><title level="j" type="abbrev">VIRUS</title><idno type="ISSN">0168-1702</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1986">1986</date><biblScope unit="volume">4</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="145">145</biblScope><biblScope unit="page" to="156">156</biblScope></imprint><idno type="ISSN">0168-1702</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0168-1702</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acid sequencing</term><term>Amino acid residues</term><term>Binns</term><term>Boursnell</term><term>Bromelain</term><term>Cavanagh</term><term>Chymotrypsin</term><term>Cleavage</term><term>Coronavirus</term><term>Glycans</term><term>Glycopolypeptide</term><term>Glycopolypeptides</term><term>Hydrophobic sequence</term><term>Isoleucine</term><term>Isoleucine residues</term><term>Molecular weight</term><term>Nucleotide sequence analysis</term><term>Outer membrane surface</term><term>Papain</term><term>Polypeptide</term><term>Pronase</term><term>Protease</term><term>Proteinase</term><term>Residue</term><term>Saponin</term><term>Sequencing</term><term>Several proteases</term><term>Small amount</term><term>Spike</term><term>Subtilisin</term><term>Trypsin</term><term>Viral</term><term>Virion</term><term>Virus membrane</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: [35S]methionine-labelled avian infectious bronchitis virus (IBV) (strain 41) and its purified protein components and virions of IBV-Beaudette were incubated with 10 proteases. Several proteases hydrolysed all or some of the membrane glycopoly-peptide (M; Mr 30K) and removed about 1.3K of peptide from the amino-(N-)-terminus plus both glycans, as determined by SDS-polyacrylamide gel electrophoresis. N-terminal analysis of [3H]isoleucine-labelled M after hydrolysis by bromelain revealed that the first nine residues had been removed. After the virions had been permeabilised with saponin, a further 2.5K decrease in molecular weight was produced and this was shown to be from the carboxy-(C-)terminus. When considered with the hydropathicity plot analysis of the amino acid sequence of M (Boursnell, M.E.G. et al., 1984, Virus Res. 1, 303–313) these results suggest that as few as 9–20 N-terminal amino acid residues may protrude at the outer membrane surface and that there is a highly protease sensitive sequence of an estimated 20–25 residues at the C-terminus of M exposed in the lumen of the virion. S2 but not SI was cleaved to a major glycopolypeptide of approximately 71K by several proteases, and to 76K by trypsin. N-terminal sequencing of the 71K glycopolypeptide revealed that it had the same N-terminus as intact S2. After hydrolysis in the presence and absence of saponin it was concluded that S2 is very sensitive to hydrolysis near its carboxy terminus at residues close to the outer membrane surface.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>saponin</json:string><json:string>bromelain</json:string><json:string>polypeptide</json:string><json:string>virion</json:string><json:string>protease</json:string><json:string>trypsin</json:string><json:string>subtilisin</json:string><json:string>papain</json:string><json:string>coronavirus</json:string><json:string>boursnell</json:string><json:string>glycopolypeptide</json:string><json:string>viral</json:string><json:string>proteinase</json:string><json:string>pronase</json:string><json:string>glycopolypeptides</json:string><json:string>sequencing</json:string><json:string>binns</json:string><json:string>glycans</json:string><json:string>chymotrypsin</json:string><json:string>isoleucine</json:string><json:string>outer membrane surface</json:string><json:string>isoleucine residues</json:string><json:string>molecular weight</json:string><json:string>cavanagh</json:string><json:string>several proteases</json:string><json:string>residue</json:string><json:string>amino acid residues</json:string><json:string>hydrophobic sequence</json:string><json:string>small amount</json:string><json:string>virus membrane</json:string><json:string>nucleotide sequence analysis</json:string><json:string>acid sequencing</json:string><json:string>cleavage</json:string><json:string>spike</json:string></teeft></keywords><author><json:item><name>David Cavanagh</name><affiliations><json:string>Houghton Poultry Research Station, Houghton, Huntingdon, Cambs. PE17 2DA, U.K.</json:string></affiliations></json:item><json:item><name>Philip J. Davis</name><affiliations><json:string>Houghton Poultry Research Station, Houghton, Huntingdon, Cambs. PE17 2DA, U.K.</json:string></affiliations></json:item><json:item><name>Darryl J.C. Pappin</name><affiliations><json:string>Department of Biochemistry, University of Leeds, Leeds LS2 9JT, U.K.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>coronavirus IBV</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>glycopolypep tides</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>proteases</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>saponin</value></json:item></subject><arkIstex>ark:/67375/6H6-X4R14KTL-C</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: [35S]methionine-labelled avian infectious bronchitis virus (IBV) (strain 41) and its purified protein components and virions of IBV-Beaudette were incubated with 10 proteases. Several proteases hydrolysed all or some of the membrane glycopoly-peptide (M; Mr 30K) and removed about 1.3K of peptide from the amino-(N-)-terminus plus both glycans, as determined by SDS-polyacrylamide gel electrophoresis. N-terminal analysis of [3H]isoleucine-labelled M after hydrolysis by bromelain revealed that the first nine residues had been removed. After the virions had been permeabilised with saponin, a further 2.5K decrease in molecular weight was produced and this was shown to be from the carboxy-(C-)terminus. When considered with the hydropathicity plot analysis of the amino acid sequence of M (Boursnell, M.E.G. et al., 1984, Virus Res. 1, 303–313) these results suggest that as few as 9–20 N-terminal amino acid residues may protrude at the outer membrane surface and that there is a highly protease sensitive sequence of an estimated 20–25 residues at the C-terminus of M exposed in the lumen of the virion. S2 but not SI was cleaved to a major glycopolypeptide of approximately 71K by several proteases, and to 76K by trypsin. N-terminal sequencing of the 71K glycopolypeptide revealed that it had the same N-terminus as intact S2. After hydrolysis in the presence and absence of saponin it was concluded that S2 is very sensitive to hydrolysis near its carboxy terminus at residues close to the outer membrane surface.</abstract><qualityIndicators><score>8.669</score><pdfWordCount>3861</pdfWordCount><pdfCharCount>25436</pdfCharCount><pdfVersion>1.4</pdfVersion><pdfPageCount>12</pdfPageCount><pdfPageSize>432 x 648 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>234</abstractWordCount><abstractCharCount>1530</abstractCharCount><keywordCount>4</keywordCount></qualityIndicators><title>Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer</title><pmid><json:string>3010596</json:string></pmid><pii><json:string>0168-1702(86)90038-9</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. 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Davis</json:string><json:string>The</json:string><json:string>J.C. Pappin</json:string><json:string>M.M. Binns</json:string><json:string>Arthur</json:string><json:string>Miss Judy</json:string></persName><placeName><json:string>Leeds</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Sturman et al., 1980</json:string><json:string>Stern et al.</json:string><json:string>Rottier et al. (1984)</json:string><json:string>Binns et al.. 1985</json:string><json:string>Rottier et al., 1984</json:string><json:string>Stern et al., 1982</json:string><json:string>Stern and Sefton, 1982b</json:string><json:string>Boursnell et al., 1984</json:string><json:string>Cavanagh, 1981</json:string><json:string>Armstrong et al., 1984</json:string><json:string>Binns et al., 1985</json:string><json:string>Wilson et al., 1981</json:string><json:string>Weigel et al., 1983</json:string><json:string>Houmard and Drapeau, 1972</json:string><json:string>Stern and Sefton, 1982a</json:string><json:string>IBV strains M41 and Beaudette; Cavanagh 1981, 1983a</json:string><json:string>Boursnell et al.</json:string><json:string>Laemmli, 1970</json:string><json:string>Stern and Sefton, 1982</json:string><json:string>Cavanagh, 1983b</json:string><json:string>Chamberlain, 1979</json:string><json:string>Cavanagh, 1983a</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-X4R14KTL-C</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - virology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - virology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Cancer Research</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - Infectious Diseases</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Virology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1986</publicationDate><copyrightDate>1986</copyrightDate><doi><json:string>10.1016/0168-1702(86)90038-9</json:string></doi><id>A8F422E0ECB35CFED53D87C278AFAD8BBDE70433</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-X4R14KTL-C/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-X4R14KTL-C/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-X4R14KTL-C/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1986</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer</title><author xml:id="author-0000"><persName><forename type="first">David</forename><surname>Cavanagh</surname></persName><affiliation>Houghton Poultry Research Station, Houghton, Huntingdon, Cambs. PE17 2DA, U.K.</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Philip J.</forename><surname>Davis</surname></persName><affiliation>Houghton Poultry Research Station, Houghton, Huntingdon, Cambs. PE17 2DA, U.K.</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Darryl J.C.</forename><surname>Pappin</surname></persName><affiliation>Department of Biochemistry, University of Leeds, Leeds LS2 9JT, U.K.</affiliation></author><idno type="istex">A8F422E0ECB35CFED53D87C278AFAD8BBDE70433</idno><idno type="ark">ark:/67375/6H6-X4R14KTL-C</idno><idno type="DOI">10.1016/0168-1702(86)90038-9</idno><idno type="PII">0168-1702(86)90038-9</idno></analytic><monogr><title level="j">Virus Research</title><title level="j" type="abbrev">VIRUS</title><idno type="pISSN">0168-1702</idno><idno type="PII">S0168-1702(00)X0126-8</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1986"></date><biblScope unit="volume">4</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="145">145</biblScope><biblScope unit="page" to="156">156</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1986</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: [35S]methionine-labelled avian infectious bronchitis virus (IBV) (strain 41) and its purified protein components and virions of IBV-Beaudette were incubated with 10 proteases. Several proteases hydrolysed all or some of the membrane glycopoly-peptide (M; Mr 30K) and removed about 1.3K of peptide from the amino-(N-)-terminus plus both glycans, as determined by SDS-polyacrylamide gel electrophoresis. N-terminal analysis of [3H]isoleucine-labelled M after hydrolysis by bromelain revealed that the first nine residues had been removed. After the virions had been permeabilised with saponin, a further 2.5K decrease in molecular weight was produced and this was shown to be from the carboxy-(C-)terminus. When considered with the hydropathicity plot analysis of the amino acid sequence of M (Boursnell, M.E.G. et al., 1984, Virus Res. 1, 303–313) these results suggest that as few as 9–20 N-terminal amino acid residues may protrude at the outer membrane surface and that there is a highly protease sensitive sequence of an estimated 20–25 residues at the C-terminus of M exposed in the lumen of the virion. S2 but not SI was cleaved to a major glycopolypeptide of approximately 71K by several proteases, and to 76K by trypsin. N-terminal sequencing of the 71K glycopolypeptide revealed that it had the same N-terminus as intact S2. After hydrolysis in the presence and absence of saponin it was concluded that S2 is very sensitive to hydrolysis near its carboxy terminus at residues close to the outer membrane surface.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>coronavirus IBV</term></item><item><term>glycopolypep tides</term></item><item><term>proteases</term></item><item><term>saponin</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1986">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-X4R14KTL-C/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>VIRUS</jid><aid>86900389</aid><ce:pii>0168-1702(86)90038-9</ce:pii><ce:doi>10.1016/0168-1702(86)90038-9</ce:doi><ce:copyright type="unknown" year="1986"></ce:copyright></item-info><head><ce:title>Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer</ce:title><ce:author-group><ce:author><ce:given-name>David</ce:given-name><ce:surname>Cavanagh</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Philip J.</ce:given-name><ce:surname>Davis</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Darryl J.C.</ce:given-name><ce:surname>Pappin</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>1</ce:label><ce:textfn>Houghton Poultry Research Station, Houghton, Huntingdon, Cambs. PE17 2DA, U.K.</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>2</ce:label><ce:textfn>Department of Biochemistry, University of Leeds, Leeds LS2 9JT, U.K.</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="7" month="3" year="1985"></ce:date-received><ce:date-accepted day="8" month="10" year="1985"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>[<ce:sup loc="pre">35</ce:sup>S]methionine-labelled avian infectious bronchitis virus (IBV) (strain 41) and its purified protein components and virions of IBV-Beaudette were incubated with 10 proteases. Several proteases hydrolysed all or some of the membrane glycopoly-peptide (M; <ce:italic>M</ce:italic><ce:inf><ce:italic>r</ce:italic></ce:inf> 30K) and removed about 1.3K of peptide from the amino-(N-)-terminus plus both glycans, as determined by SDS-polyacrylamide gel electrophoresis. N-terminal analysis of [<ce:sup loc="pre">3</ce:sup>H]isoleucine-labelled M after hydrolysis by bromelain revealed that the first nine residues had been removed. After the virions had been permeabilised with saponin, a further 2.5K decrease in molecular weight was produced and this was shown to be from the carboxy-(C-)terminus. When considered with the hydropathicity plot analysis of the amino acid sequence of M (Boursnell, M.E.G. et al., 1984, Virus Res. 1, 303–313) these results suggest that as few as 9–20 N-terminal amino acid residues may protrude at the outer membrane surface and that there is a highly protease sensitive sequence of an estimated 20–25 residues at the C-terminus of M exposed in the lumen of the virion. S2 but not SI was cleaved to a major glycopolypeptide of approximately 71K by several proteases, and to 76K by trypsin. N-terminal sequencing of the 71K glycopolypeptide revealed that it had the same N-terminus as intact S2. After hydrolysis in the presence and absence of saponin it was concluded that S2 is very sensitive to hydrolysis near its carboxy terminus at residues close to the outer membrane surface.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>coronavirus IBV</ce:text></ce:keyword><ce:keyword><ce:text>glycopolypep tides</ce:text></ce:keyword><ce:keyword><ce:text>proteases</ce:text></ce:keyword><ce:keyword><ce:text>saponin</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer</title></titleInfo><name type="personal"><namePart type="given">David</namePart><namePart type="family">Cavanagh</namePart><affiliation>Houghton Poultry Research Station, Houghton, Huntingdon, Cambs. PE17 2DA, U.K.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Philip J.</namePart><namePart type="family">Davis</namePart><affiliation>Houghton Poultry Research Station, Houghton, Huntingdon, Cambs. PE17 2DA, U.K.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Darryl J.C.</namePart><namePart type="family">Pappin</namePart><affiliation>Department of Biochemistry, University of Leeds, Leeds LS2 9JT, U.K.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1986</dateIssued><copyrightDate encoding="w3cdtf">1986</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: [35S]methionine-labelled avian infectious bronchitis virus (IBV) (strain 41) and its purified protein components and virions of IBV-Beaudette were incubated with 10 proteases. Several proteases hydrolysed all or some of the membrane glycopoly-peptide (M; Mr 30K) and removed about 1.3K of peptide from the amino-(N-)-terminus plus both glycans, as determined by SDS-polyacrylamide gel electrophoresis. N-terminal analysis of [3H]isoleucine-labelled M after hydrolysis by bromelain revealed that the first nine residues had been removed. After the virions had been permeabilised with saponin, a further 2.5K decrease in molecular weight was produced and this was shown to be from the carboxy-(C-)terminus. When considered with the hydropathicity plot analysis of the amino acid sequence of M (Boursnell, M.E.G. et al., 1984, Virus Res. 1, 303–313) these results suggest that as few as 9–20 N-terminal amino acid residues may protrude at the outer membrane surface and that there is a highly protease sensitive sequence of an estimated 20–25 residues at the C-terminus of M exposed in the lumen of the virion. S2 but not SI was cleaved to a major glycopolypeptide of approximately 71K by several proteases, and to 76K by trypsin. N-terminal sequencing of the 71K glycopolypeptide revealed that it had the same N-terminus as intact S2. After hydrolysis in the presence and absence of saponin it was concluded that S2 is very sensitive to hydrolysis near its carboxy terminus at residues close to the outer membrane surface.</abstract><subject><genre>Keywords</genre><topic>coronavirus IBV</topic><topic>glycopolypep tides</topic><topic>proteases</topic><topic>saponin</topic></subject><relatedItem type="host"><titleInfo><title>Virus Research</title></titleInfo><titleInfo type="abbreviated"><title>VIRUS</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1986</dateIssued></originInfo><identifier type="ISSN">0168-1702</identifier><identifier type="PII">S0168-1702(00)X0126-8</identifier><part><date>1986</date><detail type="volume"><number>4</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>117</start><end>212</end></extent><extent unit="pages"><start>145</start><end>156</end></extent></part></relatedItem><identifier type="istex">A8F422E0ECB35CFED53D87C278AFAD8BBDE70433</identifier><identifier type="ark">ark:/67375/6H6-X4R14KTL-C</identifier><identifier type="DOI">10.1016/0168-1702(86)90038-9</identifier><identifier type="PII">0168-1702(86)90038-9</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-X4R14KTL-C/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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