A cluster of basic amino acids in the factor X serine protease mediate surface attachment of adenovirus/FX complexes

Duffy, M.R., Bradshaw, A.C. , Parker, A.L., McVey, J.H. and Baker, A.H. (2011) A cluster of basic amino acids in the factor X serine protease mediate surface attachment of adenovirus/FX complexes. Journal of Virology, 85(20), pp. 10914-10919. (doi: 10.1128/JVI.05382-11)

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Publisher's URL: http://dx.doi.org/10.1128/JVI.05382-11

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 a 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 was abolished. A cluster of basic amino acids in the SP domain therefore mediates surface interaction of the Ad/FX complex.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Baker, Professor Andrew and Duffy, Ms Margaret and Bradshaw, Dr Angela and Parker, Dr Alan
Authors: Duffy, M.R., Bradshaw, A.C., Parker, A.L., McVey, J.H., and Baker, A.H.
Subjects:Q Science > QR Microbiology > QR355 Virology
College/School:College of Medical Veterinary and Life Sciences > Institute of Cardiovascular and Medical Sciences
Journal Name:Journal of Virology
Journal Abbr.:J. Virol.
Publisher:American Society for Microbiology
ISSN:0022-538X
ISSN (Online):1098-5514
Published Online:17 August 2011

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