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 |
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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 > School of Cardiovascular & Metabolic Health |
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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