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

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 necti...

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Main Authors: Takao eHashiguchi, Katsumi eMaenaka, Yusuke eYanagi
Format: Article
Language:English
Published: Frontiers Media S.A. 2011-12-01
Series:Frontiers in Microbiology
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fmicb.2011.00247/full
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spelling doaj-637c608907e249b6b1ba53247d0d05402020-11-24T22:51:13ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2011-12-01210.3389/fmicb.2011.0024718783Measles virus hemagglutinin: structural insights into cell entry and measles vaccineTakao eHashiguchi0Takao eHashiguchi1Katsumi eMaenaka2Katsumi eMaenaka3Yusuke eYanagi4Kyushu UniversityThe Scripps Research InstituteHokkaido UniversityCore Research for Evolutional Science and TechnologyKyushu UniversityMeasles 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.http://journal.frontiersin.org/Journal/10.3389/fmicb.2011.00247/fullMeasles VaccineMeasles virusentryreceptorStructureglycoprotein
collection DOAJ
language English
format Article
sources DOAJ
author Takao eHashiguchi
Takao eHashiguchi
Katsumi eMaenaka
Katsumi eMaenaka
Yusuke eYanagi
spellingShingle Takao eHashiguchi
Takao eHashiguchi
Katsumi eMaenaka
Katsumi eMaenaka
Yusuke eYanagi
Measles virus hemagglutinin: structural insights into cell entry and measles vaccine
Frontiers in Microbiology
Measles Vaccine
Measles virus
entry
receptor
Structure
glycoprotein
author_facet Takao eHashiguchi
Takao eHashiguchi
Katsumi eMaenaka
Katsumi eMaenaka
Yusuke eYanagi
author_sort Takao eHashiguchi
title Measles virus hemagglutinin: structural insights into cell entry and measles vaccine
title_short Measles virus hemagglutinin: structural insights into cell entry and measles vaccine
title_full Measles virus hemagglutinin: structural insights into cell entry and measles vaccine
title_fullStr Measles virus hemagglutinin: structural insights into cell entry and measles vaccine
title_full_unstemmed Measles virus hemagglutinin: structural insights into cell entry and measles vaccine
title_sort measles virus hemagglutinin: structural insights into cell entry and measles vaccine
publisher Frontiers Media S.A.
series Frontiers in Microbiology
issn 1664-302X
publishDate 2011-12-01
description 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.
topic Measles Vaccine
Measles virus
entry
receptor
Structure
glycoprotein
url http://journal.frontiersin.org/Journal/10.3389/fmicb.2011.00247/full
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