Identification of influenza virus inhibitors which disrupt of viral polymerase protein-protein interactions

被引:27
|
作者
Chase, Geoffrey [1 ]
Wunderlich, Kerstin [1 ]
Reuther, Peter [1 ]
Schwemmle, Martin [1 ]
机构
[1] Univ Freiburg Klinikum, Dept Virol, Freiburg, Germany
关键词
Influenza; Polymerase; Antiviral; ELISA; A VIRUS; STRUCTURAL BASIS; RNA-POLYMERASE; SMALL-MOLECULE; COMPLEX; REPLICATION; PEPTIDE;
D O I
10.1016/j.ymeth.2011.08.007
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Due to their ability to rapidly mutate, influenza viruses quickly develop resistance against many antiviral substances, leading to an urgent need for new compounds. The trimeric viral polymerase complex, a major target for the development of new inhibitors, must be assembled from the PB1, PB2, and PA subunits for successful infection. Here, we describe ELISA-based assays which allow the identification of peptides which impair polymerase complex formation. Since the protein-protein interaction domains of the viral polymerase are highly conserved, these inhibitors are also predicted to be active against a broad range of influenza strains. Using this method, identification of small molecules and lead compounds against influenza A and B viruses should be feasible. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码:188 / 191
页数:4
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