The structural variability of the influenza A hemagglutinin receptor-binding site
Identifieur interne : 000260 ( Main/Exploration ); précédent : 000259; suivant : 000261The structural variability of the influenza A hemagglutinin receptor-binding site
Auteurs : Michal Lazniewski [Pologne] ; Wayne K. Dawson [Pologne] ; Teresa Szczepi Ska [Pologne] ; Dariusz Plewczynski [Pologne]Source :
- Briefings in Functional Genomics [ 2041-2649 ] ; 2017.
Abstract
Hemagglutinin (HA) is a transmembrane protein of the influenza A virus and a key component in its life cycle. The protein allows the virus to enter a host cell by recognizing specific glycans attached to transmembrane proteins of the host, which leads to viral endocytosis. In recent years, significant progress has been made in understanding the structural relationship between changes in the HA receptor-binding site (RBS) and the sialylated glycans that bind them. Several mutations were identified in the HA RBS that allows the virus to change host tropism. Their impact on binding the analogs of human and avian receptors was determined with X-ray crystallography. In this article, we provide a short overview of the HA protein structure and briefly discuss the adaptive mutations introduced to different HA subtypes.
Url:
DOI: 10.1093/bfgp/elx042
PubMed: 29253080
PubMed Central: 6252403
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en"><title>Abstract</title>
<p>Hemagglutinin (HA) is a transmembrane protein of the influenza A virus and a key component in its life cycle. The protein allows the virus to enter a host cell by recognizing specific glycans attached to transmembrane proteins of the host, which leads to viral endocytosis. In recent years, significant progress has been made in understanding the structural relationship between changes in the HA receptor-binding site (RBS) and the sialylated glycans that bind them. Several mutations were identified in the HA RBS that allows the virus to change host tropism. Their impact on binding the analogs of human and avian receptors was determined with X-ray crystallography. In this article, we provide a short overview of the HA protein structure and briefly discuss the adaptive mutations introduced to different HA subtypes.</p>
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<affiliations><list><country><li>Pologne</li>
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<tree><country name="Pologne"><noRegion><name sortKey="Lazniewski, Michal" sort="Lazniewski, Michal" uniqKey="Lazniewski M" first="Michal" last="Lazniewski">Michal Lazniewski</name>
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