Distribution of drug resistance mutations in type 3 poliovirus identifies three regions involved in uncoating functions.
Identifieur interne : 000D04 ( Pmc/Checkpoint ); précédent : 000D03; suivant : 000D05Distribution of drug resistance mutations in type 3 poliovirus identifies three regions involved in uncoating functions.
Auteurs : A G Mosser ; J Y Sgro ; R R RueckertSource :
- Journal of Virology [ 0022-538X ] ; 1994.
Abstract
We have previously described the use of an uncoating inhibitor, WIN 51711, to select drug-resistant mutants of the Sabin strain of poliovirus type 3. Two-thirds of the mutants proved to be dependent on the drug for plaque formation because of extreme thermolability (A. G. Mosser and R. R. Rueckert, J. Virol. 67:1246-1254, 1993). Here we report the responsible mutations; all were traced to single amino acid substitutions. Mutations conferring dependence and thermolability occurred in all four capsid proteins (VP1 to VP4), but all were clustered near residue 53 of VP4 at the inner capsid surface. Amino acid substitutions of the remaining non-drug-dependent mutants were mapped to three distinct loci: (i) on or near the inner capsid surface, at VP4 residue 46 or VP1 residue 129, in the vicinity of the drug dependence substitutions; (ii) at residues 192, 194, and 260 in the lining of the VP1 beta barrel, which is the drug-binding site; and (iii) at VP1 residue 105 on the edge of the canyon surrounding the fivefold axis of symmetry, the putative receptor-binding site. All of the mutations increased the eclipse rate of cell-attached virus. Such mutants help identify parts of the capsid that play a role in viral uncoating functions.
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PubMed: 7966611
PubMed Central: 237285
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Distribution of drug resistance mutations in type 3 poliovirus identifies three regions involved in uncoating functions.</title><author><name sortKey="Mosser, A G" sort="Mosser, A G" uniqKey="Mosser A" first="A G" last="Mosser">A G Mosser</name></author><author><name sortKey="Sgro, J Y" sort="Sgro, J Y" uniqKey="Sgro J" first="J Y" last="Sgro">J Y Sgro</name></author><author><name sortKey="Rueckert, R R" sort="Rueckert, R R" uniqKey="Rueckert R" first="R R" last="Rueckert">R R Rueckert</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">7966611</idno><idno type="pmc">237285</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC237285</idno><idno type="RBID">PMC:237285</idno><date when="1994">1994</date><idno type="wicri:Area/Pmc/Corpus">000414</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000414</idno><idno type="wicri:Area/Pmc/Curation">000414</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000414</idno><idno type="wicri:Area/Pmc/Checkpoint">000D04</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000D04</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Distribution of drug resistance mutations in type 3 poliovirus identifies three regions involved in uncoating functions.</title><author><name sortKey="Mosser, A G" sort="Mosser, A G" uniqKey="Mosser A" first="A G" last="Mosser">A G Mosser</name></author><author><name sortKey="Sgro, J Y" sort="Sgro, J Y" uniqKey="Sgro J" first="J Y" last="Sgro">J Y Sgro</name></author><author><name sortKey="Rueckert, R R" sort="Rueckert, R R" uniqKey="Rueckert R" first="R R" last="Rueckert">R R Rueckert</name></author></analytic><series><title level="j">Journal of Virology</title><idno type="ISSN">0022-538X</idno><idno type="eISSN">1098-5514</idno><imprint><date when="1994">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>We have previously described the use of an uncoating inhibitor, WIN 51711, to select drug-resistant mutants of the Sabin strain of poliovirus type 3. Two-thirds of the mutants proved to be dependent on the drug for plaque formation because of extreme thermolability (A. G. Mosser and R. R. Rueckert, J. Virol. 67:1246-1254, 1993). Here we report the responsible mutations; all were traced to single amino acid substitutions. Mutations conferring dependence and thermolability occurred in all four capsid proteins (VP1 to VP4), but all were clustered near residue 53 of VP4 at the inner capsid surface. Amino acid substitutions of the remaining non-drug-dependent mutants were mapped to three distinct loci: (i) on or near the inner capsid surface, at VP4 residue 46 or VP1 residue 129, in the vicinity of the drug dependence substitutions; (ii) at residues 192, 194, and 260 in the lining of the VP1 beta barrel, which is the drug-binding site; and (iii) at VP1 residue 105 on the edge of the canyon surrounding the fivefold axis of symmetry, the putative receptor-binding site. All of the mutations increased the eclipse rate of cell-attached virus. Such mutants help identify parts of the capsid that play a role in viral uncoating functions.</p><sec sec-type="scanned-figures"><title>Images</title><fig id="F1"><graphic xlink:href="jvirol00021-0542-a" xlink:role="8196"></graphic></fig><fig id="F2"><graphic xlink:href="jvirol00021-0544-a" xlink:role="8198"></graphic></fig></sec></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Virol</journal-id><journal-title>Journal of Virology</journal-title><issn pub-type="ppub">0022-538X</issn><issn pub-type="epub">1098-5514</issn></journal-meta><article-meta><article-id pub-id-type="pmid">7966611</article-id><article-id pub-id-type="pmc">237285</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Distribution of drug resistance mutations in type 3 poliovirus identifies three regions involved in uncoating functions.</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Mosser</surname><given-names>A G</given-names></name></contrib><contrib contrib-type="author"><name><surname>Sgro</surname><given-names>J Y</given-names></name></contrib><contrib contrib-type="author"><name><surname>Rueckert</surname><given-names>R R</given-names></name></contrib></contrib-group><aff>Institute for Molecular Virology, University of Wisconsin, Madison 53706.</aff><pub-date pub-type="ppub"><month>12</month><year>1994</year></pub-date><volume>68</volume><issue>12</issue><fpage>8193</fpage><lpage>8201</lpage><abstract><p>We have previously described the use of an uncoating inhibitor, WIN 51711, to select drug-resistant mutants of the Sabin strain of poliovirus type 3. Two-thirds of the mutants proved to be dependent on the drug for plaque formation because of extreme thermolability (A. G. Mosser and R. R. Rueckert, J. Virol. 67:1246-1254, 1993). Here we report the responsible mutations; all were traced to single amino acid substitutions. Mutations conferring dependence and thermolability occurred in all four capsid proteins (VP1 to VP4), but all were clustered near residue 53 of VP4 at the inner capsid surface. Amino acid substitutions of the remaining non-drug-dependent mutants were mapped to three distinct loci: (i) on or near the inner capsid surface, at VP4 residue 46 or VP1 residue 129, in the vicinity of the drug dependence substitutions; (ii) at residues 192, 194, and 260 in the lining of the VP1 beta barrel, which is the drug-binding site; and (iii) at VP1 residue 105 on the edge of the canyon surrounding the fivefold axis of symmetry, the putative receptor-binding site. All of the mutations increased the eclipse rate of cell-attached virus. Such mutants help identify parts of the capsid that play a role in viral uncoating functions.</p><sec sec-type="scanned-figures"><title>Images</title><fig id="F1"><graphic xlink:href="jvirol00021-0542-a" xlink:role="8196"></graphic></fig><fig id="F2"><graphic xlink:href="jvirol00021-0544-a" xlink:role="8198"></graphic></fig></sec></abstract></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Mosser, A G" sort="Mosser, A G" uniqKey="Mosser A" first="A G" last="Mosser">A G Mosser</name><name sortKey="Rueckert, R R" sort="Rueckert, R R" uniqKey="Rueckert R" first="R R" last="Rueckert">R R Rueckert</name><name sortKey="Sgro, J Y" sort="Sgro, J Y" uniqKey="Sgro J" first="J Y" last="Sgro">J Y Sgro</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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