| Detailed mapping of determinants within the porcine endogenous retrovirus envelope surface unit identifies critical residues for human cell infection within the proline-rich region. | |
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MedLine Citation:
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PMID: 22696659 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Replication-competent porcine endogenous retroviruses (PERVs) are either human cell tropic (PERV-A and PERV-B) or non-human cell tropic (PERV-C). We previously demonstrated that PERV in vitro cell tropism is modulated by 2 residues within the C terminus of SU and that the PERV receptor binding domain (RBD) extends beyond the variable regions A and B (VRA and VRB, respectively), to include the proline rich-region (PRR) of SU (M. Gemeniano et al., Virology 346:108-117, 2000; T. Argaw et al., J. Virol. 82:7483-7489, 2008). The present study aimed to identify the specific elements within the PERV RBD that interact with the C-terminal elements of SU to facilitate human cell infection. We constructed a series of chimeric and mutated envelopes between PERV-A and PERV-C and using pseudotyped retroviral vectors to map the human cell tropism-determining sequences within the PERV RBD. We show that the PRR from PERV-A is both necessary and sufficient to allow human cell infection when substituted into the homologous region of the PERV-C envelope carrying two C-terminal amino acid substitutions shown to influence human cell tropism, Q374R and I412V (PERV-Crv). Furthermore, substitution of a single amino acid residue in the PRR of the non-human-tropic PERV-Crv envelope allows vectors carrying this envelope to infect human cells. Receptor interference assays showed that these modified PERV-C envelopes do not bind either of the human PERV-A receptors, suggesting the presence of a distinct human PERV-C receptor. Finally, vectors carrying these modified PERV-C envelopes infect primary human endothelial cells, a cell type likely to be exposed to PERV in clinical use of certain porcine xenotransplantation products. |
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Authors:
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Takele Argaw; Carolyn A Wilson |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-06-13 |
Journal Detail:
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Title: Journal of virology Volume: 86 ISSN: 1098-5514 ISO Abbreviation: J. Virol. Publication Date: 2012 Sep |
Date Detail:
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Created Date: 2012-08-10 Completed Date: 2012-11-05 Revised Date: 2013-04-15 |
Medline Journal Info:
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Nlm Unique ID: 0113724 Medline TA: J Virol Country: United States |
Other Details:
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Languages: eng Pagination: 9096-104 Citation Subset: IM |
Affiliation:
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Gene Transfer and Immunogenicity Branch, Division of Cellular and Gene Therapies, Center for Biologics Evaluation and Research, FDA, Bethesda, Maryland, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Motifs Amino Acid Sequence Animals Cell Line Endogenous Retroviruses / chemistry, genetics, physiology* Gammaretrovirus / chemistry, genetics, physiology* Gene Products, env / chemistry*, genetics, metabolism* Humans Molecular Sequence Data Proline / genetics, metabolism Protein Structure, Tertiary Swine / virology* Viral Tropism Virus Internalization |
| Grant Support | |
ID/Acronym/Agency:
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//Howard Hughes Medical Institute |
| Chemical | |
Reg. No./Substance:
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0/Gene Products, env; 147-85-3/Proline |
| Comments/Corrections | |
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