The cytoplasmic tail of influenza A/H1N1 virus hemagglutinin is β-structural

Influenza A/H1N1 virus hemagglutinin (HA) is an integral type I glycoprotein that contains a large glycosylated ectodomain, a transmembrane domain, and a cytoplasmic tail (CT) of 10-14 amino acid residues. There are absolutely no data on the secondary or tertiary structure of the HA CT, which is imp...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biomolecular structure & dynamics 2022-06, Vol.40 (10), p.4642-4661
Main Authors: Khrustalev, Vladislav V., Kordyukova, Larisa V., Arutyunyan, Alexander M., Poboinev, Victor V., Khrustaleva, Tatyana A., Stojarov, Aleksander N., Baratova, Lyudmila A., Sapon, Alena S., Lugin, Valery G.
Format: Article
Language:English
Subjects:
3D homology modeling
circular dichroism
fluorescence spectroscopy
Influenza virus hemagglutinin cytoplasmic tail
intrinsic disorder
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Influenza A/H1N1 virus hemagglutinin (HA) is an integral type I glycoprotein that contains a large glycosylated ectodomain, a transmembrane domain, and a cytoplasmic tail (CT) of 10-14 amino acid residues. There are absolutely no data on the secondary or tertiary structure of the HA CT, which is important for virus pathogenesis. Three highly conserved cysteines are post-translationally modified by the attachment of fatty acid residues that pin the CT to the lipid membrane inside the virion. We applied circular dichroism (CD) and fluorescence spectroscopy analysis to examine four synthetic peptides corresponding to 14-15 C-terminal residues of H1 subtype HA (NH 2 -WMCSNGSLQCRICI-COOH; NH 2 -FWMCSNGSLQCRICI-COOH), with free or acetaminomethylated cysteines, in the reduced or non-reduced state, at various pH values and temperatures. The CD analysis detected the formation of a β-structure (30-65% according to the new BeStSel algorithm), in addition to an unstructured random coil, in every peptide in various conditions. It was completely or partially recognized as an antiparallel β-structure that was also confirmed by the multi-bounce Horizontal Attenuated Total Reflectance Fourier Transformed Infrared (HATR-FTIR) spectroscopy analysis. According to the experimental data, as well as 3 D modeling, we assume that the amino acid sequence corresponding to the HA CT may form a short antiparallel β-structure under the lipid membrane within a virion. Communicated by Ramaswamy H. Sarma
ISSN:0739-1102
1538-0254
DOI:10.1080/07391102.2020.1860827