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Ligands for Antibody to M-Protein are Exposed at the Surface of Influenza Virions: Effect of Proteolytic Treatment on their Activity
Université de Liège, Laboratoire de Microbiologie générale et médicale, Institut de Pathologie, B-4000, Liège, Belgium Antiserum to pure M-protein extracted from PR8 virions neutralized the infectivity and inhibited the haemagglutinating activity of various influenza A virions. It agglutinated conce...
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| Published in: | Journal of general virology 1979-11, Vol.45 (2), p.283-289 |
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| Main Authors: | , , |
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| Language: | English |
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| container_end_page | 289 |
| container_issue | 2 |
| container_start_page | 283 |
| container_title | Journal of general virology |
| container_volume | 45 |
| creator | Reginster, Monique Joassin, Luc Fontaine-Delcambe, Patricia |
| description | Université de Liège, Laboratoire de Microbiologie générale et médicale, Institut de Pathologie, B-4000, Liège, Belgium
Antiserum to pure M-protein extracted from PR8 virions neutralized the infectivity and inhibited the haemagglutinating activity of various influenza A virions. It agglutinated concentrated suspensions of these virions and fixed complement in their presence. Antibodies to M-protein were readily absorbed by intact virions or by spikeless particles obtained after proteolytic treatment, giving clear evidence that M-protein is exposed at the surface of the virus envelope. The data suggest that when antibodies to M-protein occupy specific ligands exposed at the surface of the virion they interfere with sites critical for infectivity and haemagglutinating activity.
Received 16 February 1979;
accepted 2 May 1979. |
| doi_str_mv | 10.1099/0022-1317-45-2-283 |
| format | article |
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Antiserum to pure M-protein extracted from PR8 virions neutralized the infectivity and inhibited the haemagglutinating activity of various influenza A virions. It agglutinated concentrated suspensions of these virions and fixed complement in their presence. Antibodies to M-protein were readily absorbed by intact virions or by spikeless particles obtained after proteolytic treatment, giving clear evidence that M-protein is exposed at the surface of the virus envelope. The data suggest that when antibodies to M-protein occupy specific ligands exposed at the surface of the virion they interfere with sites critical for infectivity and haemagglutinating activity.
Received 16 February 1979;
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Antiserum to pure M-protein extracted from PR8 virions neutralized the infectivity and inhibited the haemagglutinating activity of various influenza A virions. It agglutinated concentrated suspensions of these virions and fixed complement in their presence. Antibodies to M-protein were readily absorbed by intact virions or by spikeless particles obtained after proteolytic treatment, giving clear evidence that M-protein is exposed at the surface of the virus envelope. The data suggest that when antibodies to M-protein occupy specific ligands exposed at the surface of the virion they interfere with sites critical for infectivity and haemagglutinating activity.
Received 16 February 1979;
accepted 2 May 1979.</description><subject>Animals</subject><subject>Antibodies, Viral - immunology</subject><subject>Binding Sites, Antibody</subject><subject>Blood Proteins - immunology</subject><subject>Complement Fixation Tests</subject><subject>Hemagglutination Inhibition Tests</subject><subject>Immunoglobulins</subject><subject>Influenza A virus - drug effects</subject><subject>Influenza A virus - immunology</subject><subject>Neutralization Tests</subject><subject>Orthomyxoviridae - immunology</subject><subject>Peptide Hydrolases - pharmacology</subject><subject>Rabbits - immunology</subject><subject>Viral Proteins - immunology</subject><subject>Virion - immunology</subject><issn>0022-1317</issn><issn>1465-2099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><recordid>eNo9kM2O0zAUhS3EXxl4AcTCq2EV8F8ah91oVGCkIpAY2Fq2c90aJXaxnYGy5sFx6KgrX-uc-13pQ-glJW8o6fu3hDDWUE67RrQNa5jkD9CKinX91PghWp0LT9GznH8QQoVouyfoMe_XvJUr9HfrdzoMGbuY8FUo3sThiEvEn5ovKRbwAesEePP7EDMMWBdc9oC_zslpCzg6fBPcOEP4o_F3n3wM-R3eOAe2LOF_RByPxVt8m0CXCUINwgLx9Z4t_s6X43P0yOkxw4v79wJ9e7-5vf7YbD9_uLm-2jaWd7w0mnY9MMIo14NZW-kYSNYSNujWaMsMiMHWWRrbDVKK3glDW0PB6TXtuWD8Al2euIcUf86Qi5p8tjCOOkCcs-pET6SUS5GdijbFnBM4dUh-0umoKFGLebWIVYtYJVrFVDVfl17d02czwXBeOamu8etTvPe7_S-fQO0gTL5eMD6qO5_OoH--bY4a</recordid><startdate>197911</startdate><enddate>197911</enddate><creator>Reginster, Monique</creator><creator>Joassin, Luc</creator><creator>Fontaine-Delcambe, Patricia</creator><general>Soc General Microbiol</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>197911</creationdate><title>Ligands for Antibody to M-Protein are Exposed at the Surface of Influenza Virions: Effect of Proteolytic Treatment on their Activity</title><author>Reginster, Monique ; Joassin, Luc ; Fontaine-Delcambe, Patricia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c373t-a179e20213adb6c8f2e82502da5bac2be4dcda58bc7d8849f4b15b1efa6193423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Animals</topic><topic>Antibodies, Viral - immunology</topic><topic>Binding Sites, Antibody</topic><topic>Blood Proteins - immunology</topic><topic>Complement Fixation Tests</topic><topic>Hemagglutination Inhibition Tests</topic><topic>Immunoglobulins</topic><topic>Influenza A virus - drug effects</topic><topic>Influenza A virus - immunology</topic><topic>Neutralization Tests</topic><topic>Orthomyxoviridae - immunology</topic><topic>Peptide Hydrolases - pharmacology</topic><topic>Rabbits - immunology</topic><topic>Viral Proteins - immunology</topic><topic>Virion - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reginster, Monique</creatorcontrib><creatorcontrib>Joassin, Luc</creatorcontrib><creatorcontrib>Fontaine-Delcambe, Patricia</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of general virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reginster, Monique</au><au>Joassin, Luc</au><au>Fontaine-Delcambe, Patricia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ligands for Antibody to M-Protein are Exposed at the Surface of Influenza Virions: Effect of Proteolytic Treatment on their Activity</atitle><jtitle>Journal of general virology</jtitle><addtitle>J Gen Virol</addtitle><date>1979-11</date><risdate>1979</risdate><volume>45</volume><issue>2</issue><spage>283</spage><epage>289</epage><pages>283-289</pages><issn>0022-1317</issn><eissn>1465-2099</eissn><abstract>Université de Liège, Laboratoire de Microbiologie générale et médicale, Institut de Pathologie, B-4000, Liège, Belgium
Antiserum to pure M-protein extracted from PR8 virions neutralized the infectivity and inhibited the haemagglutinating activity of various influenza A virions. It agglutinated concentrated suspensions of these virions and fixed complement in their presence. Antibodies to M-protein were readily absorbed by intact virions or by spikeless particles obtained after proteolytic treatment, giving clear evidence that M-protein is exposed at the surface of the virus envelope. The data suggest that when antibodies to M-protein occupy specific ligands exposed at the surface of the virion they interfere with sites critical for infectivity and haemagglutinating activity.
Received 16 February 1979;
accepted 2 May 1979.</abstract><cop>England</cop><pub>Soc General Microbiol</pub><pmid>396358</pmid><doi>10.1099/0022-1317-45-2-283</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-1317 |
| ispartof | Journal of general virology, 1979-11, Vol.45 (2), p.283-289 |
| issn | 0022-1317 1465-2099 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_74908882 |
| source | Freely Accessible Journals |
| subjects | Animals Antibodies, Viral - immunology Binding Sites, Antibody Blood Proteins - immunology Complement Fixation Tests Hemagglutination Inhibition Tests Immunoglobulins Influenza A virus - drug effects Influenza A virus - immunology Neutralization Tests Orthomyxoviridae - immunology Peptide Hydrolases - pharmacology Rabbits - immunology Viral Proteins - immunology Virion - immunology |
| title | Ligands for Antibody to M-Protein are Exposed at the Surface of Influenza Virions: Effect of Proteolytic Treatment on their Activity |
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