|
Basic Characteristics of Mutations
|
|
Mutation Site
|
S31N |
|
Mutation Site Sentence
|
Discovery of novel dual inhibitors of the wild-type and the most prevalent drug-resistant mutant, S31N, of the M2 proton channel from influenza A virus. |
|
Mutation Level
|
Amino acid level |
|
Mutation Type
|
Nonsynonymous substitution |
|
Gene/Protein/Region
|
M2 |
|
Standardized Encoding Gene
|
M
|
|
Genotype/Subtype
|
H1N1;H5N1 |
|
Viral Reference
|
-
|
|
Functional Impact and Mechanisms
|
|
Disease
|
Influenza A
|
|
Immune
|
- |
|
Target Gene
|
-
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
|
Treatment
|
4-(adamantan-1-ylaminomethyl)-benzene-1;3-diol |
|
Location
|
- |
|
Literature Information
|
|
PMID
|
23437766
|
|
Title
|
Discovery of novel dual inhibitors of the wild-type and the most prevalent drug-resistant mutant, S31N, of the M2 proton channel from influenza A virus
|
|
Author
|
Wang J,Ma C,Wang J,Jo H,Canturk B,Fiorin G,Pinto LH,Lamb RA,Klein ML,DeGrado WF
|
|
Journal
|
Journal of medicinal chemistry
|
|
Journal Info
|
2013 Apr 11;56(7):2804-12
|
|
Abstract
|
Anti-influenza drugs, amantadine and rimantadine, targeting the M2 channel from influenza A virus are no longer effective because of widespread drug resistance. S31N is the predominant and amantadine-resistant M2 mutant, present in almost all of the circulating influenza A strains as well as in the pandemic 2009 H1N1 and the highly pathogenic H5N1 flu strains. Thus, there is an urgent need to develop second-generation M2 inhibitors targeting the S31N mutant. However, the S31N mutant presents a huge challenge to drug discovery, and it has been considered undruggable for several decades. Using structural information, classical medicinal chemistry approaches, and M2-specific biological testing, we discovered benzyl-substituted amantadine derivatives with activity against both S31N and WT, among which 4-(adamantan-1-ylaminomethyl)-benzene-1,3-diol (44) is the most potent dual inhibitor. These inhibitors demonstrate that S31N is a druggable target and provide a new starting point to design novel M2 inhibitors that address the problem of drug-resistant influenza A infections.
|
|
Sequence Data
|
-
|
|
|