Antigenic Architecture of the H7N2 Influenza Virus Hemagglutinin Belonging to the North American Lineage

Antigenic Architecture of the H7N2 Influenza Virus Hemagglutinin Belonging to the North American Lineage

The North American low pathogenic H7N2 avian influenza A viruses, which lack the 220-loop in the hemagglutinin (HA), possess dual receptor specificity for avian- and human-like receptors. The purpose of this work was to determine which amino acid substitutions in HA affect viral antigenic and phenot...

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Bibliographic Details
Published in:International journal of molecular sciences Vol. 25; no. 1; p. 212
Main Authors: Lyashko, Aleksandr V, Timofeeva, Tatiana A, Rudneva, Irina A, Lomakina, Natalia F, Treshchalina, Anastasia A, Gambaryan, Alexandra S, Sorokin, Evgenii V, Tsareva, Tatiana R, Adams, Simone E, Prilipov, Alexey G, Sadykova, Galina K, Timofeev, Boris I, Logunov, Denis Y, Gintsburg, Alexander L
Format: Journal Article
Language:English
Published: Switzerland MDPI AG 22-12-2023
MDPI
Subjects:
Amino acids
antigenic mapping
antigenic variation
Avian influenza
Birds
escape mutant
H7N2 influenza virus
hemagglutinin
Influenza
Influenza viruses
Lectins
Monoclonal antibodies
Mutation
Poultry
Viruses
Netherlands
North America
China
Russia
New York
United Kingdom > UK
United States > US
H7N2 influenza virus
antigenic variation
escape mutant
hemagglutinin
antigenic mapping
monoclonal antibodies
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Summary:The North American low pathogenic H7N2 avian influenza A viruses, which lack the 220-loop in the hemagglutinin (HA), possess dual receptor specificity for avian- and human-like receptors. The purpose of this work was to determine which amino acid substitutions in HA affect viral antigenic and phenotypic properties that may be important for virus evolution. By obtaining escape mutants under the immune pressure of treatment with monoclonal antibodies, antigenically important amino acids were determined to be at positions 125, 135, 157, 160, 198, 200, and 275 (H3 numbering). These positions, except 125 and 275, surround the receptor binding site. The substitutions A135S and A135T led to the appearance of an N-glycosylation site at 133N, which reduced affinity for the avian-like receptor analog and weakened binding with tested monoclonal antibodies. Additionally, the A135S substitution is associated with the adaptation of avian viruses to mammals (cat, human, or mouse). The mutation A160V decreased virulence in mice and increased affinity for the human-type receptor analog. Conversely, substitution G198E, in combination with 157N or 160E, displayed reduced affinity for the human-type receptor analog.
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content type line 23
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms25010212