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A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin ?1 protein.

ABSTRACT: The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin ?1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin ?1 and is localized in the nucleus, suggesting that the NLS located at residues 101-105 is not the only NLS within M1 recombinant protein containing 1-160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin ?1, but M1/60-252 domains cannot bind importin ?1. Further mapping showed that the deletion of residues 1-20 impaired the interaction between N terminus of M1 and importin ?1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin ?1 and for nuclear localization.

SUBMITTER: Liu Q

PROVIDER: S-EPMC4111955 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein.

Liu Qinfang Q Bawa Bhupinder B Ma Jingjiao J Li Feng F Ma Wenjun W Richt Jürgen A JA

Virus genes 20140418 1

The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstra ...[more]

PMID: 24743939

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Project description:The influenza A(H1N1)pdm09 virus caused the first influenza pandemic of the 21st century. In this study, we wanted to decipher the role of conserved basic residues of the viral M1 matrix protein in virus assembly and release. M1 plays many roles in the influenza virus replication cycle. Specifically, it participates in viral particle assembly, can associate with the viral ribonucleoprotein complexes and can bind to the cell plasma membrane and/or the cytoplasmic tail of viral transmembrane proteins. M1 contains an N-terminal domain of 164 amino acids with two basic domains: the nuclear localization signal on helix 6 and an arginine triplet (R76/77/78) on helix 5. To investigate the role of these two M1 basic domains in influenza A(H1N1)pdm09 virus molecular assembly, we analyzed M1 attachment to membranes, virus-like particle (VLP) production and virus infectivity. In vitro, M1 binding to large unilamellar vesicles (LUVs), which contain negatively charged lipids, decreased significantly when the M1 R76/77/78 motif was mutated. In cells, M1 alone was mainly observed in the nucleus (47%) and in the cytosol (42%). Conversely, when co-expressed with the viral proteins NS1/NEP and M2, M1 was relocated to the cell membranes (55%), as shown by subcellular fractionation experiments. This minimal system allowed the production of M1 containing-VLPs. However, M1 with mutations in the arginine triplet accumulated in intracellular clusters and its incorporation in VLPs was strongly diminished. M2 over-expression was essential for M1 membrane localization and VLP production, whereas the viral trans-membrane proteins HA and NA seemed dispensable. These results suggest that the M1 arginine triplet participates in M1 interaction with membranes. This R76/77/78 motif is essential for M1 incorporation in virus particles and the importance of this motif was confirmed by reverse genetic demonstrating that its mutation is lethal for the virus. These results highlight the molecular mechanism of M1-membrane interaction during the formation of influenza A(H1N1)pdm09 virus particles which is essential for infectivity.

Dataset Information

A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin ?1 protein.

Publications

A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein.

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