Oseltamivir resistance depends on the amino acid at the 273rd position of neuraminidase of influenza a virus (H1N1) circulating in the human population

The structure of neuraminidase of influenza A virus (H1N1) spreading in the human population was analyzed. The results indicate a significant correlation between the virus sensitivity to oseltamivir and the nature of amino acids at positions 274 and 273 of neuraminidase. Phenylalanine at position 27...

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Bibliographic Details
Published in:Russian journal of bioorganic chemistry 2011-09, Vol.37 (5), p.640-643, Article 640
Main Authors: Ryabinin, V. A., Kostina, E. V., Sinyakov, A. N.
Format: Article
Language:English
Subjects:
Amino acids
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Influenza
Influenza A virus
Letter to the Editor
Life Sciences
Mutation
Organic Chemistry
Phenylalanine
Viruses
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Summary:The structure of neuraminidase of influenza A virus (H1N1) spreading in the human population was analyzed. The results indicate a significant correlation between the virus sensitivity to oseltamivir and the nature of amino acids at positions 274 and 273 of neuraminidase. Phenylalanine at position 273 indicates a higher propensity of the influenza virus to mutation H274Y, which leads to resistant strains. It is suggested that the mutation at position 273 may be one of the characteristics that allow the type-A influenza virus to be ascribed to a pandemic or a seasonal type.
ISSN:1068-1620
1608-330X
DOI:10.1134/S1068162011050153