Structural characterization of CD81-Claudin-1 hepatitis C virus receptor complexes

Nicklas Bonander, Mohammed Jamshad, Ke Hu, Michelle J. Farquhar, Zania Stamataki, Peter Balfe, Jane A. McKeating, Roslyn M Bill

Research output: Contribution to journalArticle


Tetraspanins are thought to exert their biological function(s) by co-ordinating the lateral movement and trafficking of associated molecules into tetraspanin-enriched microdomains. A second four-TM (transmembrane) domain protein family, the Claudin superfamily, is the major structural component of cellular TJs (tight junctions). Although the Claudin family displays low sequence homology and appears to be evolutionarily distinct from the tetraspanins, CD81 and Claudin-1 are critical molecules defining HCV (hepatitis C virus) entry; we recently demonstrated that CD81-Claudin-1 complexes have an essential role in this process. To understand the molecular basis of CD81-Claudin-1 complex formation, we produced and purified milligram quantities of full-length CD81 and Claudin-1, alone and in complex, in both detergent and lipid contexts. Structural characterization of these purified proteins will allow us to define the mechanism(s) underlying virus-cell interactions and aid the design of therapeutic agents targeting early steps in the viral life cycle.
Original languageEnglish
Pages (from-to)537-540
Number of pages4
JournalBiochemical Society Transactions
Issue number2
Publication statusPublished - Apr 2011
Event4th European Conference on Tetraspanins - Birmingham, United Kingdom
Duration: 8 Sept 20109 Sept 2010


  • animals
  • CD antigens
  • CD81 antigens
  • hepacivirus
  • humans
  • membrane proteins
  • biological models
  • molecular conformation
  • multiprotein complexes
  • virus receptors
  • virus internalization
  • Claudin-1
  • hepatitis C virus
  • oligomerization
  • tetraspanin


Dive into the research topics of 'Structural characterization of CD81-Claudin-1 hepatitis C virus receptor complexes'. Together they form a unique fingerprint.

Cite this