tetano
Editor, Senior Moderator
Virology. 2013 Nov;446(1-2):112-22. doi: 10.1016/j.virol.2013.07.035. Epub 2013 Aug 27.
Structural basis for the divergent evolution of influenza B virus hemagglutinin.
Ni F, Kondrashkina E, Wang Q.
Source
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA; Department of Bioengineering, Rice University, Houston, TX 77005, USA.
Abstract
Influenza A and B viruses are responsible for the severe morbidity and mortality worldwide in annual influenza epidemics. Currently circulating influenza B virus belongs to the B/Victoria or B/Yamagata lineage that was diverged from each other about 30-40 years ago. However, a mechanistic understanding of their divergent evolution is still lacking. Here we report the crystal structures of influenza B/Yamanashi/166/1998 hemagglutinin (HA) belonging to B/Yamagata lineage and its complex with the avian-like receptor analogue. Comparison of these structures with those of undiverged and diverged influenza B virus HAs, in conjunction with sequence analysis, reveals the molecular basis for the divergent evolution of influenza B virus HAs. Furthermore, HAs of diverged influenza B virus strains display much stronger molecular interactions with terminal sialic acid of bound receptors, which may allow for a different tissue tropism for current influenza B viruses, for which further investigation is required.
? 2013 Elsevier Inc. All rights reserved.
KEYWORDS:
Divergent evolution, Hemagglutinin, Influenza B virus, Positive selective pressure, Receptor binding, Sialic acid receptors
PMID:
24074573
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24074573
Structural basis for the divergent evolution of influenza B virus hemagglutinin.
Ni F, Kondrashkina E, Wang Q.
Source
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA; Department of Bioengineering, Rice University, Houston, TX 77005, USA.
Abstract
Influenza A and B viruses are responsible for the severe morbidity and mortality worldwide in annual influenza epidemics. Currently circulating influenza B virus belongs to the B/Victoria or B/Yamagata lineage that was diverged from each other about 30-40 years ago. However, a mechanistic understanding of their divergent evolution is still lacking. Here we report the crystal structures of influenza B/Yamanashi/166/1998 hemagglutinin (HA) belonging to B/Yamagata lineage and its complex with the avian-like receptor analogue. Comparison of these structures with those of undiverged and diverged influenza B virus HAs, in conjunction with sequence analysis, reveals the molecular basis for the divergent evolution of influenza B virus HAs. Furthermore, HAs of diverged influenza B virus strains display much stronger molecular interactions with terminal sialic acid of bound receptors, which may allow for a different tissue tropism for current influenza B viruses, for which further investigation is required.
? 2013 Elsevier Inc. All rights reserved.
KEYWORDS:
Divergent evolution, Hemagglutinin, Influenza B virus, Positive selective pressure, Receptor binding, Sialic acid receptors
PMID:
24074573
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24074573