The cowpox virus fusion regulator proteins SPI-3 and hemagglutinin interact in infected and uninfected cells
The serpin SPI-3 and the hemagglutinin (HA) encoded by cowpox virus (CPV) block cell–cell fusion, and colocalize at the cell surface. wtCPV does not fuse cells, but inactivation of either gene leads to fusion. SPI-3 mAb added to wtCPV-infected cells caused fusion, confirming that SPI-3 protein at th...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2006-03, Vol.347 (1), p.88-99 |
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| description | The serpin SPI-3 and the hemagglutinin (HA) encoded by cowpox virus (CPV) block cell–cell fusion, and colocalize at the cell surface. wtCPV does not fuse cells, but inactivation of either gene leads to fusion. SPI-3 mAb added to wtCPV-infected cells caused fusion, confirming that SPI-3 protein at the cell surface prevents fusion. The SPI-3 mAb epitope mapped to an 85-amino acid region at the C-terminus. Removal of either 44 residues from the SPI-3 C-terminus or 48 residues following the N-terminal signal sequence resulted in fusion. Interaction between SPI-3 and HA proteins in infected cells was shown by coimmunoprecipitation. SPI-3/HA was not associated with the A27L “fusion” protein. SPI-3 and HA were able to associate in uninfected cells in the absence of other viral proteins. The HA-binding domain in SPI-3 resided in the C-terminal 229 residues, and did not include helix D, which mediates cofactor interaction in many other serpins. |
| doi_str_mv | 10.1016/j.virol.2005.11.012 |
| format | Article |
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SPI-3 mAb added to wtCPV-infected cells caused fusion, confirming that SPI-3 protein at the cell surface prevents fusion. The SPI-3 mAb epitope mapped to an 85-amino acid region at the C-terminus. Removal of either 44 residues from the SPI-3 C-terminus or 48 residues following the N-terminal signal sequence resulted in fusion. Interaction between SPI-3 and HA proteins in infected cells was shown by coimmunoprecipitation. SPI-3/HA was not associated with the A27L “fusion” protein. SPI-3 and HA were able to associate in uninfected cells in the absence of other viral proteins. 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SPI-3 mAb added to wtCPV-infected cells caused fusion, confirming that SPI-3 protein at the cell surface prevents fusion. The SPI-3 mAb epitope mapped to an 85-amino acid region at the C-terminus. Removal of either 44 residues from the SPI-3 C-terminus or 48 residues following the N-terminal signal sequence resulted in fusion. Interaction between SPI-3 and HA proteins in infected cells was shown by coimmunoprecipitation. SPI-3/HA was not associated with the A27L “fusion” protein. SPI-3 and HA were able to associate in uninfected cells in the absence of other viral proteins. The HA-binding domain in SPI-3 resided in the C-terminal 229 residues, and did not include helix D, which mediates cofactor interaction in many other serpins.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Antibodies, Viral</subject><subject>Cell Line</subject><subject>Cell Membrane - virology</subject><subject>Cell–cell fusion</subject><subject>Cercopithecus aethiops</subject><subject>Coimmunoprecipitation</subject><subject>Cowpox virus</subject><subject>Cowpox virus - genetics</subject><subject>Cowpox virus - immunology</subject><subject>Cowpox virus - pathogenicity</subject><subject>Cowpox virus - physiology</subject><subject>Epitope Mapping</subject><subject>Hemagglutinin (HA)</subject><subject>Hemagglutinins, Viral - genetics</subject><subject>Hemagglutinins, Viral - immunology</subject><subject>Hemagglutinins, Viral - physiology</subject><subject>Membrane Fusion - genetics</subject><subject>Membrane Fusion - physiology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Poxvirus</subject><subject>Protein Conformation</subject><subject>Protein–protein interaction</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serpin</subject><subject>Serpins - chemistry</subject><subject>Serpins - genetics</subject><subject>Serpins - immunology</subject><subject>Serpins - physiology</subject><subject>SPI-3</subject><subject>Transfection</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - immunology</subject><subject>Viral Proteins - physiology</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtr3TAQhUVpSW4ev6BQtOrOjkayLXnRRQnNAwIJNFkLWR7f6OIr3Up2mvz76j5odu1qNPDNmdE5hHwGVgKD5mJVvrgYxpIzVpcAJQP-gSyAtU3BRAUfyYKxiheN4vyYnKS0YrmXkh2RY2iEVA1vF2R8fEZqw-9NeKVZbk50mJMLnkZczqOZQqSbGCZ0PtGfD7eFoMb39BnXZrkc58l556nzE0ZjJ7p7D2gn7HfY7P-2FscxnZFPgxkTnh_qKXm6-vF4eVPc3V_fXn6_K6xQaiqEYNCqWlRo20rxDo3t6nqQTVVJqxQqy9nQd7a2g2na2ra8rWTXgujyv2rsxCn5utfNp_-aMU167dL2AuMxzEk3UkqlOPsvCBIUh0pkUOxBG0NKEQe9iW5t4psGprdp6JXepaG3aWgAndPIU18O8nO3xv595mB_Br7tAcxuvDiMOlmH3mLvYvZN98H9c8EfnAidfA</recordid><startdate>20060330</startdate><enddate>20060330</enddate><creator>Turner, Peter C.</creator><creator>Moyer, Richard W.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20060330</creationdate><title>The cowpox virus fusion regulator proteins SPI-3 and hemagglutinin interact in infected and uninfected cells</title><author>Turner, Peter C. ; Moyer, Richard W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-330198534ec9482beacb55f76447c88e8c20fdbc5cfa695c92947b913b1635eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Antibodies, Viral</topic><topic>Cell Line</topic><topic>Cell Membrane - virology</topic><topic>Cell–cell fusion</topic><topic>Cercopithecus aethiops</topic><topic>Coimmunoprecipitation</topic><topic>Cowpox virus</topic><topic>Cowpox virus - genetics</topic><topic>Cowpox virus - immunology</topic><topic>Cowpox virus - pathogenicity</topic><topic>Cowpox virus - physiology</topic><topic>Epitope Mapping</topic><topic>Hemagglutinin (HA)</topic><topic>Hemagglutinins, Viral - genetics</topic><topic>Hemagglutinins, Viral - immunology</topic><topic>Hemagglutinins, Viral - physiology</topic><topic>Membrane Fusion - genetics</topic><topic>Membrane Fusion - physiology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Poxvirus</topic><topic>Protein Conformation</topic><topic>Protein–protein interaction</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serpin</topic><topic>Serpins - chemistry</topic><topic>Serpins - genetics</topic><topic>Serpins - immunology</topic><topic>Serpins - physiology</topic><topic>SPI-3</topic><topic>Transfection</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - immunology</topic><topic>Viral Proteins - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Turner, Peter C.</creatorcontrib><creatorcontrib>Moyer, Richard W.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Turner, Peter C.</au><au>Moyer, Richard W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The cowpox virus fusion regulator proteins SPI-3 and hemagglutinin interact in infected and uninfected cells</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2006-03-30</date><risdate>2006</risdate><volume>347</volume><issue>1</issue><spage>88</spage><epage>99</epage><pages>88-99</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>The serpin SPI-3 and the hemagglutinin (HA) encoded by cowpox virus (CPV) block cell–cell fusion, and colocalize at the cell surface. wtCPV does not fuse cells, but inactivation of either gene leads to fusion. SPI-3 mAb added to wtCPV-infected cells caused fusion, confirming that SPI-3 protein at the cell surface prevents fusion. The SPI-3 mAb epitope mapped to an 85-amino acid region at the C-terminus. Removal of either 44 residues from the SPI-3 C-terminus or 48 residues following the N-terminal signal sequence resulted in fusion. Interaction between SPI-3 and HA proteins in infected cells was shown by coimmunoprecipitation. SPI-3/HA was not associated with the A27L “fusion” protein. SPI-3 and HA were able to associate in uninfected cells in the absence of other viral proteins. The HA-binding domain in SPI-3 resided in the C-terminal 229 residues, and did not include helix D, which mediates cofactor interaction in many other serpins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16378629</pmid><doi>10.1016/j.virol.2005.11.012</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Antibodies, Monoclonal Antibodies, Viral Cell Line Cell Membrane - virology Cell–cell fusion Cercopithecus aethiops Coimmunoprecipitation Cowpox virus Cowpox virus - genetics Cowpox virus - immunology Cowpox virus - pathogenicity Cowpox virus - physiology Epitope Mapping Hemagglutinin (HA) Hemagglutinins, Viral - genetics Hemagglutinins, Viral - immunology Hemagglutinins, Viral - physiology Membrane Fusion - genetics Membrane Fusion - physiology Models, Molecular Molecular Sequence Data Mutation Poxvirus Protein Conformation Protein–protein interaction Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - metabolism Sequence Homology, Amino Acid Serpin Serpins - chemistry Serpins - genetics Serpins - immunology Serpins - physiology SPI-3 Transfection Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - immunology Viral Proteins - physiology |
| title | The cowpox virus fusion regulator proteins SPI-3 and hemagglutinin interact in infected and uninfected cells |
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