Cleavage of the Papillomavirus Minor Capsid Protein, L2, at a Furin Consensus Site Is Necessary for Infection
Papillomaviruses (PV) comprise a large family of nonenveloped DNA viruses that include the oncogenic PV types that are the causative agents of human cervical cancer. As is true of many animal DNA viruses, PV are taken into the cell by endocytosis and must escape from the endosomal compartment to the...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2006-01, Vol.103 (5), p.1522-1527 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Richards, Rebecca M. Lowy, Douglas R. Schiller, John T. Day, Patricia M. |
| description | Papillomaviruses (PV) comprise a large family of nonenveloped DNA viruses that include the oncogenic PV types that are the causative agents of human cervical cancer. As is true of many animal DNA viruses, PV are taken into the cell by endocytosis and must escape from the endosomal compartment to the cytoplasm to initiate infection. Here we show that this step depends on the site-specific enzymatic cleavage of the PV minor virion protein L2 at a consensus furin recognition site. Cleavage by furin, a cellencoded proprotein convertase, is known to be required for endosome escape by many bacterial toxins. However, to our knowledge, furin has not been previously implicated in the viral entry process. This step is potentially a target for PV inhibition. |
| doi_str_mv | 10.1073/pnas.0508815103 |
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As is true of many animal DNA viruses, PV are taken into the cell by endocytosis and must escape from the endosomal compartment to the cytoplasm to initiate infection. Here we show that this step depends on the site-specific enzymatic cleavage of the PV minor virion protein L2 at a consensus furin recognition site. Cleavage by furin, a cellencoded proprotein convertase, is known to be required for endosome escape by many bacterial toxins. However, to our knowledge, furin has not been previously implicated in the viral entry process. 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This step is potentially a target for PV inhibition.</description><subject>Antibodies</subject><subject>Binding sites</subject><subject>Biological Sciences</subject><subject>Capsid</subject><subject>Capsid Proteins - chemistry</subject><subject>Capsid Proteins - metabolism</subject><subject>Cell lines</subject><subject>DNA, Complementary - metabolism</subject><subject>Dose-Response Relationship, Drug</subject><subject>Endocytosis</subject><subject>Endosomes</subject><subject>Endosomes - metabolism</subject><subject>Enzymes</subject><subject>Female</subject><subject>Furin - chemistry</subject><subject>Genomes</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Infections</subject><subject>Microbiology</subject><subject>Microscopy, Fluorescence</subject><subject>Oncogene Proteins, Viral - chemistry</subject><subject>Oncogene Proteins, Viral - metabolism</subject><subject>Papillomavirus</subject><subject>Phylogeny</subject><subject>Plasmids - metabolism</subject><subject>Proteins</subject><subject>Time Factors</subject><subject>Transfection</subject><subject>Uterine Cervical Neoplasms - metabolism</subject><subject>Uterine Cervical Neoplasms - virology</subject><subject>Virions</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAURS0EokNhzQpksYBN0z5_Jc4GCUUURhqgErC2PInTepSxU9sZwb_HYUadwgJWXrxzj97zReg5gXMCFbsYnY7nIEBKIgiwB2hBoCZFyWt4iBYAtCokp_wEPYlxAwC1kPAYnZCSM0pBLtC2GYze6WuDfY_TjcFXerTD4Ld6Z8MU8SfrfMCNHqPt8FXwyVh3hlf0DOuENb6cgnW48S4aFzP-1SaDlxF_Nq2JUYefuM_xpetNm6x3T9GjXg_RPDu8p-j75ftvzcdi9eXDsnm3KlpR01QI3sm-qqWpypJ2a9FRXgGttejazrR5thZ9z_S6a5kmDAjpDK1ZSTmhmlLB2Sl6u_eO03pruta4FPSgxmC3eSfltVV_Tpy9Udd-pwgrQfwWvD4Igr-dTExqa2NrhkE746eoKqhoJYH-FyQ1pwJgNr76C9z4Kbj8C4oCybKSyQxd7KE2-BiD6e9WJqDmwtVcuDoWnhMv71965A8N3wPm5FHHlFBE0PmCN_8EVD8NQzI_UiZf7MlNTD7coSyfJzkI9gu1EsgC</recordid><startdate>20060131</startdate><enddate>20060131</enddate><creator>Richards, Rebecca M.</creator><creator>Lowy, Douglas R.</creator><creator>Schiller, John T.</creator><creator>Day, Patricia M.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20060131</creationdate><title>Cleavage of the Papillomavirus Minor Capsid Protein, L2, at a Furin Consensus Site Is Necessary for Infection</title><author>Richards, Rebecca M. ; 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| subjects | Antibodies Binding sites Biological Sciences Capsid Capsid Proteins - chemistry Capsid Proteins - metabolism Cell lines DNA, Complementary - metabolism Dose-Response Relationship, Drug Endocytosis Endosomes Endosomes - metabolism Enzymes Female Furin - chemistry Genomes HeLa Cells Humans Infections Microbiology Microscopy, Fluorescence Oncogene Proteins, Viral - chemistry Oncogene Proteins, Viral - metabolism Papillomavirus Phylogeny Plasmids - metabolism Proteins Time Factors Transfection Uterine Cervical Neoplasms - metabolism Uterine Cervical Neoplasms - virology Virions Viruses |
| title | Cleavage of the Papillomavirus Minor Capsid Protein, L2, at a Furin Consensus Site Is Necessary for Infection |
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