A Cluster of Basic Amino Acids in the Factor X Serine Protease Mediates Surface Attachment of Adenovirus/FX Complexes

Duffy, Margaret R., Bradshaw, Angela C., Parker, Alan L. ORCID: https://orcid.org/0000-0002-9302-1761, McVey, John H. and Baker, Andrew H. 2011. A Cluster of Basic Amino Acids in the Factor X Serine Protease Mediates Surface Attachment of Adenovirus/FX Complexes. Journal of Virology 85 (20) , pp. 10914-10919. 10.1128/JVI.05382-11

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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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine
Subjects:	Q Science > QR Microbiology > QR355 Virology R Medicine > RM Therapeutics. Pharmacology
Additional Information:	Pdf uploaded in accordance with publisher's policy at http://www.sherpa.ac.uk/romeo/issn/0022-538X/ (accessed 25/02/2014)
Publisher:	American Society for Microbiology
ISSN:	0022-538X
Date of First Compliant Deposit:	30 March 2016
Last Modified:	11 May 2023 07:21
URI:	https://orca.cardiff.ac.uk/id/eprint/43280

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