
Crystallization and preliminary crystallographic analysis of the measles virus hemagglutinin in complex with the CD46 receptor
Author(s) -
Santiago César,
GutiérrezRodríguez Angel,
Tucker Paul A.,
Stehle Thilo,
Casasnovas José M.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109050593
Subject(s) - measles virus , hemagglutinin (influenza) , cd46 , receptor , glycoprotein , virus , chemistry , biology , virology , crystallization , complement system , microbiology and biotechnology , crystallography , immune system , biochemistry , measles , immunology , vaccination , organic chemistry
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.
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