Mutation prone position within neuraminidase of H7N9: An important information for predicting drug-resistance

How to cite this article:
Wiwanitkit V. Mutation prone position within neuraminidase of H7N9: An important information for predicting drug-resistance. Ann Trop Med Public Health 2014;7:80

 

How to cite this URL:
Wiwanitkit V. Mutation prone position within neuraminidase of H7N9: An important information for predicting drug-resistance. Ann Trop Med Public Health [serial online] 2014 [cited 2021 Mar 2];7:80. Available from: https://www.atmph.org/text.asp?2014/7/1/80/145048

Dear Sir,

The emerging H7N9 influenza is an important concern in present global public health. This infection is a new infection, and the present concern is on the drug resistance. The problem of antiviral drug-resistance in H7N9 influenza is first mentioned by Hu et al. in Lancet. [1] Focusing on the underlying mechanism of drug resistance, the mutation within neuraminidase is mentioned as a necessary pathobiological process.­ [2],[3] Here, the author uses a bioinformatics technique to assess the mutation prone position within neuraminidase of H7N9. The technique is a standard technique as previously used in the mutation prone position assessment in the previous outbreak of H5N1 bird flu. [4] The template in this study is GenBank: AGI60300.1. According to the assessment, from overall 465 amino acids, the mutation resistance position can be seen at 34-51, 136-143, 158-166, 175-196, 235-247, 285-296, 316-351, 401-406. This means there are more mutation prone positions than mutation resistant positions within the neuraminidase of H7N9. It is no doubt that the problem of drug-resistance will increase if the H7N9 influenza virus circulates for a long time.

References

 

1.
Hu Y, Lu S, Song Z, Wang W, Hao P, Li J, et al. Association between adverse clinical outcome in human disease caused by novel influenza A H7N9 virus and sustained viral shedding and emergence of antiviral resistance. Lancet 2013;381:2273-9.
2.
Wu Y, Bi Y, Vavricka CJ, Sun X, Zhang Y, Gao F, et al. Characterization of two distinct neuraminidases from avian-origin human-infecting H7N9 influenza viruses. Cell Res 2013;23:1347-55.
3.
Sleeman K, Guo Z, Barnes J, Shaw M, Stevens J, Gubareva LV. R292K substitution and drug susceptibility of influenza A(H7N9) viruses. Emerg Infect Dis 2013;19:1521-4.
4.
Wiwanitkit V. HA cleavage site mutation in bird flu virus in Thailand: Relation to pathogenic degree and further surveillance. Am J Infect Control 2006;34:468.

Source of Support: None, Conflict of Interest: None

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DOI: 10.4103/1755-6783.145048

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