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Measles virus hemagglutinin: structural insights into cell entry and measles vaccine

Journal

FRONTIERS IN MICROBIOLOGY
Volume 2, Issue -, Pages -

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fmicb.2011.00247

Keywords

measles virus; hemagglutinin; structure; fusion; entry; measles vaccine; glycoprotein; receptor

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Funding

  1. Ministry of Education, Culture, Sports, Science and Technology
  2. Ministry of Health, Labor and Welfare of japan
  3. Japan Society for the Promotion of Science Research Fellowship for Young Scientists

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Measles is one of the most contagious viral diseases, and remains a major cause of childhood morbidity and mortality worldwide. The measles virus (MV), a member of the family Paramyxoviridae, enters cells through a cellular receptor, the signaling lymphocyte activation molecule (SLAM), CD46 or nectin-4. Entry is mediated by two MV envelope glycoproteins, the hemagglutinin (H) and the fusion (F) protein. The H protein mediates receptor attachment, while the F protein causes membrane fusion. The interaction between the H and F proteins is essential to initiate the cell entry process. Recently determined crystal structures of the MV-H protein unbound and bound to SLAM or CD46 have provided insights into paramyxovirus entry and the effectiveness of measles vaccine.

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