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

J Virol. 2011 Oct;85(20):10914-9. doi: 10.1128/JVI.05382-11. Epub 2011 Aug 17.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

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


  • Amino Acids, Basic
  • Heparan Sulfate Proteoglycans
  • Mutant Proteins
  • Factor X