Abstract
The recent outbreaks of avian flu in Southeast Asia and swine flu in Mexico City painfully exemplify the ability of the influenza virus to rapidly mutate and develop resistance to modern medicines. This review seeks to detail the molecular mechanism by which the influenza virus has obtained resistance to amino-adamantyls, one of only two classes of drugs that combat the flu. Amino-adamantyls target the viral M2 H+ channel and have become largely ineffective due to mutations in the transmembrane domain of the protein. Herein we describe these resistance rendering mutations and the compounded effects they have upon the protein's function and resulting virus viability.
| Original language | English |
|---|---|
| Pages (from-to) | 547-553 |
| Number of pages | 7 |
| Journal | Biochimica et Biophysica Acta - Biomembranes |
| Volume | 1808 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 2011 |
Bibliographical note
Funding Information:This work was supported in part by grants from the National Institutes of Health ( R21AI064797 ), the Israeli Science Foundation ( 784/01,1249/05,1581/08 ) and the Horowitz Foundation . I.T.A. is the Arthur Lejwa Professor of Structural Biochemistry at the Hebrew University of Jerusalem. The authors are indebted to members of the Arkin and Gilon Labs for numerous helpful discussions and advice.
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Channel blockers
- Influenza
- M2 channel
- Viral resistance
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