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Structural basis of efficient contagion: measles variations on a theme by parainfluenza viruses

Identifieur interne : 000338 ( Main/Exploration ); précédent : 000337; suivant : 000339

Structural basis of efficient contagion: measles variations on a theme by parainfluenza viruses

Auteurs : Mathieu Mateo ; Chanakha K. Navaratnarajah ; Roberto Cattaneo

Source :

Current opinion in virology [ 1879-6257 ] ; 2014.

RBID : PMC:4028398

Abstract

A quartet of attachment proteins and a trio of fusion protein subunits play the cell entry concert of parainfluenza viruses. While many of these viruses bind sialic acid to enter cells, wild type measles binds exclusively two tissue-specific proteins, the lymphatic receptor signaling lymphocytic activation molecule (SLAM), and the epithelial receptor nectin-4. SLAM binds near the stalk-head junction of the hemagglutinin. Nectin-4 binds a hydrophobic groove located between blades 4 and 5 of the hemagglutinin β-propeller head. The mutated vaccine strain hemagglutinin binds in addition the ubiquitous protein CD46, which explains attenuation. The measles virus entry concert has four movements. Andante misterioso: the virus takes over the immune system. Allegro con brio: it rapidly spreads in the upper airway’s epithelia. “Targeting” fugue: the versatile orchestra takes off. Presto furioso: the virus exits the host with thunder. Be careful: music is contagious.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4028398

DOI: 10.1016/j.coviro.2014.01.004
PubMed: 24492202
PubMed Central: 4028398

Affiliations:

Le document en format XML

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<author><name sortKey="Navaratnarajah, Chanakha K" sort="Navaratnarajah, Chanakha K" uniqKey="Navaratnarajah C" first="Chanakha K." last="Navaratnarajah">Chanakha K. Navaratnarajah</name>
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<front><div type="abstract" xml:lang="en"><p id="P1">A quartet of attachment proteins and a trio of fusion protein subunits play the cell entry concert of parainfluenza viruses. While many of these viruses bind sialic acid to enter cells, wild type measles binds exclusively two tissue-specific proteins, the lymphatic receptor signaling lymphocytic activation molecule (SLAM), and the epithelial receptor nectin-4. SLAM binds near the stalk-head junction of the hemagglutinin. Nectin-4 binds a hydrophobic groove located between blades 4 and 5 of the hemagglutinin β-propeller head. The mutated vaccine strain hemagglutinin binds in addition the ubiquitous protein CD46, which explains attenuation. The measles virus entry concert has four movements. <italic>Andante misterioso</italic>
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: it rapidly spreads in the upper airway’s epithelia. <italic>“Targeting” fugue</italic>
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<name sortKey="Navaratnarajah, Chanakha K" sort="Navaratnarajah, Chanakha K" uniqKey="Navaratnarajah C" first="Chanakha K." last="Navaratnarajah">Chanakha K. Navaratnarajah</name>
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Structural basis of efficient contagion: measles variations on a theme by parainfluenza viruses

Structural basis of efficient contagion: measles variations on a theme by parainfluenza viruses

Source :

Abstract

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Le document en format XML

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