tetano
Editor, Senior Moderator
Virology. 2014 Jun;458-459:33-42. doi: 10.1016/j.virol.2014.04.012. Epub 2014 May 5.
The R35 residue of the influenza A virus NS1 protein has minimal effects on nuclear localization but alters virus replication through disrupting protein dimerization.
Lalime EN1, Pekosz A2.
Author information
Abstract
The influenza A virus NS1 protein has a nuclear localization sequence (NLS) in the amino terminal region. This NLS overlaps sequences that are important for RNA binding as well as protein dimerization. To assess the significance of the NS1 NLS on influenza virus replication, the NLS amino acids were individually mutated to alanines and recombinant viruses encoding these mutations were rescued. Viruses containing NS1 proteins with mutations at R37, R38 and K41 displayed minimal changes in replication or NS1 protein nuclear localization. Recombinant viruses encoding NS1 R35A were not recovered but viruses containing second site mutations at position D39 in addition to the R35A mutation were isolated. The mutations at position 39 were shown to partially restore NS1 protein dimerization but had minimal effects on nuclear localization. These data indicate that the amino acids in the NS1 NLS region play a more important role in protein dimerization compared to nuclear localization.
Copyright ? 2014 Elsevier Inc. All rights reserved.
KEYWORDS:
Dimer; Influenza; NS1; Nuclear localization; RNA binding
PMID:
24928037
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24928037
The R35 residue of the influenza A virus NS1 protein has minimal effects on nuclear localization but alters virus replication through disrupting protein dimerization.
Lalime EN1, Pekosz A2.
Author information
Abstract
The influenza A virus NS1 protein has a nuclear localization sequence (NLS) in the amino terminal region. This NLS overlaps sequences that are important for RNA binding as well as protein dimerization. To assess the significance of the NS1 NLS on influenza virus replication, the NLS amino acids were individually mutated to alanines and recombinant viruses encoding these mutations were rescued. Viruses containing NS1 proteins with mutations at R37, R38 and K41 displayed minimal changes in replication or NS1 protein nuclear localization. Recombinant viruses encoding NS1 R35A were not recovered but viruses containing second site mutations at position D39 in addition to the R35A mutation were isolated. The mutations at position 39 were shown to partially restore NS1 protein dimerization but had minimal effects on nuclear localization. These data indicate that the amino acids in the NS1 NLS region play a more important role in protein dimerization compared to nuclear localization.
Copyright ? 2014 Elsevier Inc. All rights reserved.
KEYWORDS:
Dimer; Influenza; NS1; Nuclear localization; RNA binding
PMID:
24928037
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24928037