Conserved cysteine and histidine residues in the putative zinc finger motif of the influenza A virus M1 protein are not critical for influenza virus replication.
Conserved cysteine and histidine residues in the putative zinc finger motif of the influenza A virus M1 protein are not critical for influenza virus replication.
复制标题
甲型流感病毒 M1 蛋白的假定锌指基序中的保守半胱氨酸和组氨酸残基对于流感病毒复制并不重要。
DOI：
10.1099/vir.0.19389-0
复制
发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Nayak,DebiP
中科院分区：
文献类型：
--
作者：
Hui,EricKa-Wai;Ralston,Katherine;Judd,AmritK;Nayak,DebiP
The influenza virus matrix protein (M1) possesses a cysteine and histidine (CCHH) motif in the helix 9 (H9) and adjacent region (148CATCEQIADSQHRSH162). The CCHH motif has been proposed as a putative zinc finger motif and zinc-binding activity has been implicated in virus uncoating as well as transcription inhibition and mRNA regulation. The function of the CCHH motif in the influenza virus life cycle was investigated by site-directed mutagenesis (alanine replacement) and by rescuing mutant viruses by reverse genetics. Mutant viruses containing an alanine replacement of the cysteine and histidine residues, either individually or in combination, were seen to exhibit wt phenotype in multiple virus growth cycles and plaque morphology. In addition, synthetic peptides containing the putative zinc finger motif did not inhibit virus replication in MDCK cells. However, mutation of Ala155in H9 was lethal for rescuing infectious virus. These data show that the CCHH motif does not provide a critical function in the influenza virus life cycle in cell culture and that the zinc-binding function may not be involved in virus biology. However, the lethal phenotype of the Ala155mutation shows that the H9 region of M1 provides some other critical function(s) in virus replication.
