Identification of amino acids of influenza virus HA responsible for resistance to a fusion inhibitor, Stachyflin.

Abstract

We have recently described a novel hemagglutinin (HA) conformational change inhibitor of human influenza virus, Stachyflin (Yoshimoto et al, Arch. Virol., 144, 1-14, 1999). Stachyflin-resistant variants of human influenza A/WSN/33 (H1N1) virus were isolated in vitro and the nucleotide sequences of their HA genes were determined. The relation of amino acid substitutions and Stachyflin resistance was analyzed with in vitro membrane fusion between HA-expressing cells and octadecylrhodamine (R18)-labelled chick erythrocytes (RBC). The amino acid substitutions, lysine to arginine at position 51 or lysine to glutamic acid at position 121 of the HA2 subunit of the HA protein was enough to confer a Stachyflin-resistant phenotype of HA protein. The molecular mechanism of anti-HA conformational change activity of Stachyflin is discussed.

• Authors: J Yoshimoto, M Kakui, H Iwasaki, H Sugimoto, T Fujiwara, N Hattori
• Journal: Microbiology and immunology (Microbiol Immunol) Vol. 44 Issue 8 Pg. 677-85 ( 2000) ISSN: 0385-5600 [Print] Australia
• PMID: 11021398 (Publication Type: Journal Article)

Chemical References

• Amino Acids
• Antiviral Agents
• Hemagglutinin Glycoproteins, Influenza Virus
• Sesquiterpenes
• stachyflin

Topics

• Amino Acid Substitution
• Amino Acids (physiology)
• Animals
• Antiviral Agents (pharmacology)
• Cattle
• Cell Fusion
• Cell Line
• Chickens
• DNA Mutational Analysis
• Dogs
• Genes, Viral
• Hemagglutinin Glycoproteins, Influenza Virus (genetics, physiology)
• Influenza A virus (drug effects, genetics, pathogenicity)
• Models, Molecular
• Sesquiterpenes (pharmacology)