| Literature DB >> 21849463 |
Margaret R Duffy1, Angela C Bradshaw, Alan L Parker, John H McVey, Andrew H Baker.
Abstract
Hepatocyte transduction following intravenous administration of adenovirus 5 (Ad5) is mediated by interaction between coagulation factor X (FX) and the hexon. The FX serine protease (SP) domain tethers the Ad5/FX complex to hepatocytes through binding heparan sulfate proteoglycans (HSPGs). Here, we identify the critical HSPG-interacting residues of FX. We generated an FX mutant by modifying seven residues in the SP domain. Surface plasmon resonance demonstrated that mutations did not affect binding to Ad5. FX-mediated, HSPG-associated cell binding and transduction were abolished. A cluster of basic amino acids in the SP domain therefore mediates surface interaction of the Ad/FX complex.Entities:
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Year: 2011 PMID: 21849463 PMCID: PMC3187485 DOI: 10.1128/JVI.05382-11
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103