Crystallization and preliminary crystallographic analysis of the measles virus hemagglutinin in complex with the CD46 receptor

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):91-4. doi: 10.1107/S1744309109050593. Epub 2009 Dec 25.

Abstract

The measles virus (MV) hemagglutinin (MV-H) mediates the attachment of MV particles to cell-surface receptors for entry into host cells. MV uses two receptors for attachment to host cells: the complement-control protein CD46 and the signalling lymphocyte activation molecule (SLAM). The MV-H glycoprotein from an Edmonston MV variant and the MV-binding fragment of the CD46 receptor were overproduced in mammalian cells and used to crystallize an MV-H-CD46 complex. Well diffracting crystals containing two complexes in the asymmetric unit were obtained and the structure of the complex was solved by the molecular-replacement method.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CHO Cells
  • Cricetinae
  • Cricetulus
  • Hemagglutinins, Viral / chemistry*
  • Humans
  • Measles virus
  • Membrane Cofactor Protein / chemistry*
  • Receptors, Virus / chemistry*

Substances

  • Hemagglutinins, Viral
  • Membrane Cofactor Protein
  • Receptors, Virus