tetano
Editor, Senior Moderator
J Virol. 2014 Apr 16. [Epub ahead of print]
Characterization of The Nucleocytoplasmic Shuttle of The Matrix Protein of Influenza B Virus.
Cao S1, Jiang J, Li J, Li Y, Yang L, Wang S, Yan J, Gao GF, Liu W.
Author information
Abstract
Influenza B virus is an enveloped negative-strand RNA virus, that contributes considerably to annual influenza illnesses in human. The matrix protein of influenza B virus (BM1) acts as a cytoplasmic-nuclear shuttling protein during the early and late stages of infection. The mechanism of this intracellular transport of BM1 was revealed through the identification of two leucine-rich CRM1-dependent nuclear export signals (NESs) (3-14aa and 124-133aa), one bipartite nuclear localization signal (NLS) (76-94aa), and two phosphorylation sites (80T and 84S) in BM1. The biological function of the NLS and NES regions were determined through the observation of the intracellular distribution of EGFP-tagged signal peptides, and WT, NES-mutant and NLS-mutant EGFP-BM1. Furthermore, the NLS phosphorylation sites 80T and 84S, were found to be required for the nuclear accumulation of EGFP-NLS and for the efficient binding of EGFP-BM1 to human importin-α 1. Moreover, all of these regions/sites were required for the generation of viable influenza B virus in a 12-plasmid virus rescue system.
IMPORTANCE:
This study expands our understanding of the life cycle of influenza B virus by defining defines/presents the dynamic mechanism of the nucleocytoplasmic shuttle of BM1, and could provide a scientific basis for the development of anti-viral medication.
PMID:
24741102
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24741102
Characterization of The Nucleocytoplasmic Shuttle of The Matrix Protein of Influenza B Virus.
Cao S1, Jiang J, Li J, Li Y, Yang L, Wang S, Yan J, Gao GF, Liu W.
Author information
Abstract
Influenza B virus is an enveloped negative-strand RNA virus, that contributes considerably to annual influenza illnesses in human. The matrix protein of influenza B virus (BM1) acts as a cytoplasmic-nuclear shuttling protein during the early and late stages of infection. The mechanism of this intracellular transport of BM1 was revealed through the identification of two leucine-rich CRM1-dependent nuclear export signals (NESs) (3-14aa and 124-133aa), one bipartite nuclear localization signal (NLS) (76-94aa), and two phosphorylation sites (80T and 84S) in BM1. The biological function of the NLS and NES regions were determined through the observation of the intracellular distribution of EGFP-tagged signal peptides, and WT, NES-mutant and NLS-mutant EGFP-BM1. Furthermore, the NLS phosphorylation sites 80T and 84S, were found to be required for the nuclear accumulation of EGFP-NLS and for the efficient binding of EGFP-BM1 to human importin-α 1. Moreover, all of these regions/sites were required for the generation of viable influenza B virus in a 12-plasmid virus rescue system.
IMPORTANCE:
This study expands our understanding of the life cycle of influenza B virus by defining defines/presents the dynamic mechanism of the nucleocytoplasmic shuttle of BM1, and could provide a scientific basis for the development of anti-viral medication.
PMID:
24741102
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24741102