tetano
Editor, Senior Moderator
Virology. 2012 Aug 22. [Epub ahead of print]
Glycosylation of CM2 is important for efficient replication of influenza C virus.
Okuwa T, Muraki Y, Himeda T, Ohara Y.
Source
Department of Microbiology, Kanazawa Medical University School of Medicine, 1-1 Daigaku, Uchinada, Ishikawa 920-0293, Japan.
Abstract
CM2 is the second membrane protein of influenza C virus and possesses a conserved motif for N-glycosylation. To investigate the role(s) of CM2 glycosylation in the virus replication, we generated rN11A, a recombinant influenza C virus lacking the glycosylation site. The rN11A virus grew less efficiently than the wild-type (WT) virus, although the biochemical characteristics of the mutant CM2 were similar to those of authentic CM2. The amount of the genome (GFP-vRNA) in the CM2-N11A-virus-like particles (VLPs) was 13% of that found in WT-VLPs. The incoming GFP-vRNA was less efficiently transported to the nucleus in CM2-N11A-VLP-infected cells than WT-VLP-infected cells, leading to the reduced reporter gene expression in CM2-N11A-VLP-infected cells. Thus the glycosylation of CM2 is required for efficient replication of influenza C virus, and the obtained findings confirmed and extended the previous observation that CM2 is involved in the genome packaging and uncoating processes.
Copyright ? 2012 Elsevier Inc. All rights reserved.
PMID:
22921534
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22921534
Glycosylation of CM2 is important for efficient replication of influenza C virus.
Okuwa T, Muraki Y, Himeda T, Ohara Y.
Source
Department of Microbiology, Kanazawa Medical University School of Medicine, 1-1 Daigaku, Uchinada, Ishikawa 920-0293, Japan.
Abstract
CM2 is the second membrane protein of influenza C virus and possesses a conserved motif for N-glycosylation. To investigate the role(s) of CM2 glycosylation in the virus replication, we generated rN11A, a recombinant influenza C virus lacking the glycosylation site. The rN11A virus grew less efficiently than the wild-type (WT) virus, although the biochemical characteristics of the mutant CM2 were similar to those of authentic CM2. The amount of the genome (GFP-vRNA) in the CM2-N11A-virus-like particles (VLPs) was 13% of that found in WT-VLPs. The incoming GFP-vRNA was less efficiently transported to the nucleus in CM2-N11A-VLP-infected cells than WT-VLP-infected cells, leading to the reduced reporter gene expression in CM2-N11A-VLP-infected cells. Thus the glycosylation of CM2 is required for efficient replication of influenza C virus, and the obtained findings confirmed and extended the previous observation that CM2 is involved in the genome packaging and uncoating processes.
Copyright ? 2012 Elsevier Inc. All rights reserved.
PMID:
22921534
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22921534