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

Margaret R Duffy, Angela C Bradshaw, Alan L Parker, John H McVey, Andrew H Baker

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)10914-9
Number of pages6
JournalJournal of Virology
Volume85
Issue number20
DOIs
Publication statusPublished - Oct 2011

Keywords

  • Adenoviridae
  • Amino Acid Substitution
  • Amino Acids, Basic
  • Factor X
  • Heparan Sulfate Proteoglycans
  • Humans
  • Mutagenesis, Site-Directed
  • Mutant Proteins
  • Protein Binding
  • Surface Plasmon Resonance

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