tetano
Editor, Senior Moderator
J Mol Graph Model. 2020 Mar 8;97:107580. doi: 10.1016/j.jmgm.2020.107580. [Epub ahead of print]
Structural insights into the potential changes in receptor binding site found in the 1998-2018 influenza B/Yamagata hemagglutinin: A putative correlation between receptor binding site structural variability and seasonal infection.
Cueno ME[SUP]1[/SUP], Iguchi K[SUP]2[/SUP], Suemitsu K[SUP]2[/SUP], Hirano M[SUP]2[/SUP], Hanzawa K[SUP]2[/SUP], Isoda T[SUP]3[/SUP], Ueno M[SUP]3[/SUP], Iguchi R[SUP]3[/SUP], Otani A[SUP]3[/SUP], Imai K[SUP]4[/SUP].
Author information
Abstract
Influenza B virus has two distinct lineages (Victoria and Yamagata) and are associated with seasonal influenza epidemics that cause respiratory illness. Influenza B hemagglutinin (HA) is a major surface glycoprotein with the receptor-binding site (RBS) primarily involved in viral pathogenesis. Generally, influenza B exclusively infects the human population which would insinuate that the structural variability of the influenza B HA RBS rarely changes. However, to our knowledge, the potential impact of variations in the influenza B HA RBS structural variability was not fully elucidated. Throughout this study, we generated models from the transitioning (evolving viral lineage) 1998-2018 influenza B/Yamagata HA, verified the quality of each HA model, performed HA RBS structural variability measurements, superimposed varying HA models for comparison, and designed a phylogenetic tree network for further analyses. We found that measurements of the transitioning HA RBS structural variability were generally maintained and, similarly, measurements of the altered (years that differed from the evolving viral lineage, specifically 2003, 2007, 2017) HA RBS structural variability differed from the transitioning HA RBS. Moreover, we observed that the altered HA RBS structural variability favored the formation of a putative Y202-H191 hydrogen bond which we postulate may increase structural stability, thereby, allowing for a winter infection of the virus. Furthermore, we established that changes in HA RBS structural variability does not influence viral evolution, but putatively seasonal infection.
Copyright ? 2020 Elsevier Inc. All rights reserved.
KEYWORDS:
Hemagglutinin; Influenza B; Receptor binding site; Structural variability; Yamagata lineage
PMID:32193088DOI:10.1016/j.jmgm.2020.107580
Structural insights into the potential changes in receptor binding site found in the 1998-2018 influenza B/Yamagata hemagglutinin: A putative correlation between receptor binding site structural variability and seasonal infection.
Cueno ME[SUP]1[/SUP], Iguchi K[SUP]2[/SUP], Suemitsu K[SUP]2[/SUP], Hirano M[SUP]2[/SUP], Hanzawa K[SUP]2[/SUP], Isoda T[SUP]3[/SUP], Ueno M[SUP]3[/SUP], Iguchi R[SUP]3[/SUP], Otani A[SUP]3[/SUP], Imai K[SUP]4[/SUP].
Author information
Abstract
Influenza B virus has two distinct lineages (Victoria and Yamagata) and are associated with seasonal influenza epidemics that cause respiratory illness. Influenza B hemagglutinin (HA) is a major surface glycoprotein with the receptor-binding site (RBS) primarily involved in viral pathogenesis. Generally, influenza B exclusively infects the human population which would insinuate that the structural variability of the influenza B HA RBS rarely changes. However, to our knowledge, the potential impact of variations in the influenza B HA RBS structural variability was not fully elucidated. Throughout this study, we generated models from the transitioning (evolving viral lineage) 1998-2018 influenza B/Yamagata HA, verified the quality of each HA model, performed HA RBS structural variability measurements, superimposed varying HA models for comparison, and designed a phylogenetic tree network for further analyses. We found that measurements of the transitioning HA RBS structural variability were generally maintained and, similarly, measurements of the altered (years that differed from the evolving viral lineage, specifically 2003, 2007, 2017) HA RBS structural variability differed from the transitioning HA RBS. Moreover, we observed that the altered HA RBS structural variability favored the formation of a putative Y202-H191 hydrogen bond which we postulate may increase structural stability, thereby, allowing for a winter infection of the virus. Furthermore, we established that changes in HA RBS structural variability does not influence viral evolution, but putatively seasonal infection.
Copyright ? 2020 Elsevier Inc. All rights reserved.
KEYWORDS:
Hemagglutinin; Influenza B; Receptor binding site; Structural variability; Yamagata lineage
PMID:32193088DOI:10.1016/j.jmgm.2020.107580