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Identification of Amino Acid Residues Involved in the Interaction between Measles Virus Haemagglutin (MVH) and Its Human Cell Receptor(Signaling Lymphocyte Activation Molecule, SLAM)

  • Xu, Qin (State Key Laboratory of Virology, College of Life Sciences, Wuhan University) ;
  • Zhang, Peng (State Key Laboratory of Virology, College of Life Sciences, Wuhan University) ;
  • Hu, Chunling (State Key Laboratory of Virology, College of Life Sciences, Wuhan University) ;
  • Liu, Xin (State Key Laboratory of Virology, College of Life Sciences, Wuhan University) ;
  • Qi, Yipeng (State Key Laboratory of Virology, College of Life Sciences, Wuhan University) ;
  • Liu, Yingle (State Key Laboratory of Virology, College of Life Sciences, Wuhan University)
  • Received : 2006.02.27
  • Accepted : 2006.04.10
  • Published : 2006.07.31

Abstract

Signaling lymphocyte activation molecule (SLAM; also known as CD150) is a newly identified cellular receptor for measles virus (MV). The interaction between MV Haemagglutin (MVH) and SLAM is an initial step for MV entry. We have identified several novel SLAM binding sites at residues S429, T436 and H437 of MVH protein and MVH mutants in these residues dramatically decrease the ability to interaction with the cell surface SLAM and fail to co-precipitation with SLAM in vivo as well as malfunction in syncytium formation. At the same time, K58, S59 and H61 of SLAM was also identified to be critical for MVH and SLAM binding. Further, these residues may be useful targets for the development of measles therapy.

Keywords

References

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