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

被引：26

作者：

Duffy, Margaret R.

Bradshaw, Angela C.

Parker, Alan L.

McVey, John H. ^{[2
]}

Baker, Andrew H. ^{[1
]}

机构：

[1] Univ Glasgow, Inst Cardiovasc & Med Sci, BHF Glasgow Cardiovasc Res Ctr, Coll Med Vet & Life Sci, Glasgow G12 8TA, Lanark, Scotland

[2] Thrombosis Res Inst, London SW3 6LR, England

来源：

JOURNAL OF VIROLOGY | 2011年 / 85卷 / 20期

基金：

英国生物技术与生命科学研究理事会;

关键词：

HEPARIN-BINDING EXOSITE; GENE-TRANSFER; HEXON; LIVER; IDENTIFICATION; INFECTION; CELLS;

D O I：

10.1128/JVI.05382-11

中图分类号：

Q93 [微生物学];

学科分类号：

071005 [微生物学];

摘要：

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.

引用

页码：10914 / 10919

页数：6

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