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Year : 2014 | Volume
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| Issue : 1 | Page : 80 |
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Mutation prone position within neuraminidase of H7N9: An important information for predicting drug-resistance |
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Viroj Wiwanitkit
Department of Medical Science, Faculty of Medicine, University of Nis, Šumatova?ka, Niš, Serbia
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Date of Web Publication | 20-Nov-2014 |
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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. |

Correspondence Address: Viroj Wiwanitkit Wiwanitkit House, Bangkhae, Bangkok 10160, Thailand
 Source of Support: None, Conflict of Interest: None  | Check |
DOI: 10.4103/1755-6783.145048

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