Comparative thermostability analysis of zoonotic and human influenza virus A and B neuraminidase

• Published in: Archives of virology Vol. 165; no. 1; pp. 201 - 206
• Main Authors: Evseenko, Vasily A., Svyatchenko, Svetlana V., Kolosova, Natalia P., Kovrizhkina, Valentina L., Marchenko, Vasiliy Y., Durymanov, Aleksander G., Goncharova, Natalia I., Ryzhikov, Alexander B.
• Format: Journal Article
• Language: English
• Published: Vienna Springer Vienna 01-01-2020; Springer Nature B.V
• Subjects: Alphainfluenzavirus - enzymology; Amino acid sequence; Animals; Avian flu; Betainfluenzavirus - enzymology; Binding sites; Biomedical and Life Sciences; Biomedicine; Birds - virology; Body Temperature; Brief Report; Calcium-binding protein; Enzyme Stability; Exo-a-sialidase; Humans; Infectious Diseases; Influenza; Influenza A; Medical Microbiology; Neuraminidase - chemistry; Swine; Thermal stability; Thermodynamics; Viral Proteins - chemistry; Virology; Viruses; Zoonoses - virology
• ISSN: 0304-8608; 1432-8798
• DOI: 10.1007/s00705-019-04465-w

Neuraminidase (NA) thermostability of influenza A and B viruses isolated from birds, swine and humans was measured to evaluate its variability associated with host body temperature. The highest 50% inactivation temperature (IT
50
) was observed with H3N8 avian influenza virus (74 °C), and the lowest IT
50
was observed with the seasonal human H3N2 virus (45.5 °C). The IT
50
values of A(H1N1)pdm09 viruses 56.4-58.5 °C were statistically higher than that of the prepandemic strain A/Solomon Islands/03/06 (52.5 °C). An analysis of Ca
2+
binding sites revealed the correspondence of amino acid changes to NA thermostability. This study demonstrates that changes in NA thermostability correspond to differences in host body temperature.