scholarly journals Role of the Influenza Virus M1 Protein in Nuclear Export of Viral Ribonucleoproteins

2000 ◽  
Vol 74 (4) ◽  
pp. 1781-1786 ◽  
Author(s):  
Matthew Bui ◽  
Elizabeth G. Wills ◽  
Ari Helenius ◽  
Gary R. Whittaker
Keyword(s):  
Influenza Virus ◽  
Nuclear Export ◽  
Matrix Protein ◽  
Semliki Forest Virus ◽  
Kinase Inhibitor ◽  
The Matrix ◽  
Matrix Protein M1 ◽  
Influenza Virus Replication ◽  
Additional Role

ABSTRACT The protein kinase inhibitor H7 blocks influenza virus replication, inhibits production of the matrix protein (M1), and leads to a retention of the viral ribonucleoproteins (vRNPs) in the nucleus at late times of infection (K. Martin and A. Helenius, Cell 67:117–130, 1991). We show here that production of assembled vRNPs occurs normally in H7-treated cells, and we have used H7 as a biochemical tool to trap vRNPs in the nucleus. When H7 was removed from the cells, vRNP export was specifically induced in a CHO cell line stably expressing recombinant M1. Similarly, fusion of cells expressing recombinant M1 from a Semliki Forest virus vector allowed nuclear export of vRNPs. However, export was not rescued when H7 was present in the cells, implying an additional role for phosphorylation in this process. The viral NS2 protein was undetectable in these systems. We conclude that influenza virus M1 is required to induce vRNP nuclear export but that cellular phosphorylation is an additional factor.

scholarly journals Influenza Virus M2 Ion Channel Protein Is Necessary for Filamentous Virion Formation

2010 ◽  
Vol 84 (10) ◽  
pp. 5078-5088 ◽  
Author(s):  
Jeremy S. Rossman ◽  
Xianghong Jing ◽  
George P. Leser ◽  
Victoria Balannik ◽  
Lawrence H. Pinto ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Influenza A ◽  
Matrix Protein ◽  
Influenza Virus Infection ◽  
Cytoplasmic Tail ◽  
Integral Membrane Protein ◽  
Filament Formation ◽  
The Matrix ◽  
Matrix Protein M1 ◽  
Raft Domains

ABSTRACT Influenza A virus buds from cells as spherical (∼100-nm diameter) and filamentous (∼100 nm × 2 to 20 μm) virions. Previous work has determined that the matrix protein (M1) confers the ability of the virus to form filaments; however, additional work has suggested that the influenza virus M2 integral membrane protein also plays a role in viral filament formation. In examining the role of the M2 protein in filament formation, we observed that the cytoplasmic tail of M2 contains several sites that are essential for filament formation. Additionally, whereas M2 is a nonraft protein, expression of other viral proteins in the context of influenza virus infection leads to the colocalization of M2 with sites of virus budding and lipid raft domains. We found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and we speculate that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.

scholarly journals Nucleus-targeting domain of the matrix protein (M1) of influenza virus.

1995 ◽  
Vol 69 (3) ◽  
pp. 1964-1970 ◽  
Author(s):  
Z Ye ◽  
D Robinson ◽  
R R Wagner
Keyword(s):  
Influenza Virus ◽  
Matrix Protein ◽  
The Matrix ◽  
Matrix Protein M1

scholarly journals Association of Influenza Virus Proteins with Membrane Rafts

2011 ◽  
Vol 2011 ◽  
pp. 1-14 ◽  
Author(s):  
Michael Veit ◽  
Bastian Thaa
Keyword(s):  
Influenza Virus ◽  
Matrix Protein ◽  
Protein Transport ◽  
Virus Assembly ◽  
Environmental Stability ◽  
Membrane Rafts ◽  
The Matrix ◽  
Matrix Protein M1 ◽  
Membrane Budding ◽  
Raft Domains

Assembly and budding of influenza virus proceeds in the viral budozone, a domain in the plasma membrane with characteristics of cholesterol/sphingolipid-rich membrane rafts. The viral transmembrane glycoproteins hemagglutinin (HA) and neuraminidase (NA) are intrinsically targeted to these domains, while M2 is seemingly targeted to the edge of the budozone. Virus assembly is orchestrated by the matrix protein M1, binding to all viral components and the membrane. Budding progresses by protein- and lipid-mediated membrane bending and particle scission probably mediated by M2. Here, we summarize the experimental evidence for this model with emphasis on the raft-targeting features of HA, NA, and M2 and review the functional importance of raft domains for viral protein transport, assembly and budding, environmental stability, and membrane fusion.

scholarly journals Influenza Virus Hemagglutinin and Neuraminidase, but Not the Matrix Protein, Are Required for Assembly and Budding of Plasmid-Derived Virus-Like Particles

2007 ◽  
Vol 81 (13) ◽  
pp. 7111-7123 ◽  
Author(s):  
Benjamin J. Chen ◽  
George P. Leser ◽  
Eiji Morita ◽  
Robert A. Lamb
Keyword(s):  
Influenza Virus ◽  
Culture Medium ◽  
Matrix Protein ◽  
Culture Media ◽  
Protein Composition ◽  
Multivesicular Body ◽  
Viral Proteins ◽  
Dominant Negative ◽  
The Matrix ◽  
Overexpression System

ABSTRACT For influenza virus, we developed an efficient, noncytotoxic, plasmid-based virus-like particle (VLP) system to reflect authentic virus particles. This system was characterized biochemically by analysis of VLP protein composition, morphologically by electron microscopy, and functionally with a VLP infectivity assay. The VLP system was used to address the identity of the minimal set of viral proteins required for budding. Combinations of viral proteins were expressed in cells, and the polypeptide composition of the particles released into the culture media was analyzed. Contrary to previous findings in which matrix (M1) protein was considered to be the driving force of budding because M1 was found to be released copiously into the culture medium when M1 was expressed by using the vaccinia virus T7 RNA polymerase-driven overexpression system, in our noncytotoxic VLP system M1 was not released efficiently into the culture medium. Additionally, hemagglutinin (HA), when treated with exogenous neuraminidase (NA) or coexpressed with viral NA, could be released from cells independently of M1. Incorporation of M1 into VLPs required HA expression, although when M1 was omitted from VLPs, particles with morphologies similar to those of wild-type VLPs or viruses were observed. Furthermore, when HA and NA cytoplasmic tail mutants were included in the VLPs, M1 failed to be efficiently incorporated into VLPs, consistent with a model in which the glycoproteins control virus budding by sorting to lipid raft microdomains and recruiting the internal viral core components. VLP formation also occurred independently of the function of Vps4 in the multivesicular body pathway, as dominant-negative Vps4 proteins failed to inhibit influenza VLP budding.

scholarly journals Two amino acid residues in the matrix protein M1 contribute to the virulence difference of H5N1 avian influenza viruses in mice

Virology ◽  
2009 ◽  
Vol 384 (1) ◽  
pp. 28-32 ◽  
Author(s):  
Shufang Fan ◽  
Guohua Deng ◽  
Jiasheng Song ◽  
Guobin Tian ◽  
Yongbing Suo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Avian Influenza ◽  
Matrix Protein ◽  
Influenza Viruses ◽  
Amino Acid Residues ◽  
Avian Influenza Viruses ◽  
H5n1 Avian Influenza ◽  
The Matrix ◽  
Matrix Protein M1

scholarly journals Restriction of Viral Replication by Mutation of the Influenza Virus Matrix Protein

2002 ◽  
Vol 76 (24) ◽  
pp. 13055-13061 ◽  
Author(s):  
Teresa Liu ◽  
Zhiping Ye
Keyword(s):  
Influenza Virus ◽  
Amino Acid ◽  
Viral Replication ◽  
Zinc Finger ◽  
Nuclear Export ◽  
Matrix Protein ◽  
Reverse Genetics ◽  
Rna Binding ◽  
Viral Assembly ◽  
Zinc Finger Motif

ABSTRACT The matrix protein (M1) of influenza virus plays an essential role in viral assembly and has a variety of functions, including association with influenza virus ribonucleoprotein (RNP). Our previous studies show that the association of M1 with viral RNA and nucleoprotein not only promotes formation of helical RNP but also is required for export of RNP from the nucleus during viral replication. The RNA-binding domains of M1 have been mapped to two independent regions: a zinc finger motif at amino acid positions 148 to 162 and a series of basic amino acids (RKLKR) at amino acid positions 101 to 105, which is also involved in RNP-binding activity. To further understand the role of the RNP-binding domain of M1 in viral assembly and replication, mutations in the coding sequences of RKLKR and the zinc finger motif of M1 were constructed using a PCR technique and introduced into wild-type influenza virus by reverse genetics. Altering the zinc finger motif of M1 only slightly affected viral growth. Substitution of Arg with Ser at position 101 or 105 of RKLKR did not have a major impact on nuclear export of RNP or viral replication. In contrast, deletion of RKLKR or substitution of Lys with Asn at position 102 or 104 of RKLKR resulted in a lethal mutation. These results indicate that the RKLKR domain of M1 protein plays an important role in viral replication.

scholarly journals Intravirion cohesion of matrix protein M1 with ribonucleocapsid is a prerequisite of influenza virus infectivity

Virology ◽  
2016 ◽  
Vol 492 ◽  
pp. 187-196 ◽  
Author(s):  
O.P. Zhirnov ◽  
A.A. Manykin ◽  
J.S. Rossman ◽  
H.D. Klenk
Keyword(s):  
Influenza Virus ◽  
Matrix Protein ◽  
Virus Infectivity ◽  
Matrix Protein M1

scholarly journals Quantification of avian influenza virus in tissues of mute swans using TaqMan real time qRT-PCR

2009 ◽  
Vol 54 (No. 9) ◽  
pp. 435-443 ◽  
Author(s):  
K. Rosenbergova ◽  
P. Lany ◽  
Z. Pospisil ◽  
O. Kubicek ◽  
V. Celer ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Avian Influenza ◽  
Avian Influenza Virus ◽  
Matrix Protein ◽  
Protein Gene ◽  
Vero Cells ◽  
Taqman Probe ◽  
Virus Rna ◽  
The Matrix ◽  
Mute Swans

This study reports on the first quantification of avian influenza virus in the organs of mute swans that died during the epizootic of avian influenza (H5N1) between January and April 2006 in the Czech Republic. The quantitative real-time Reverse Transcriptase PCR (qRT-PCR) assay based on a TaqMan probe was developed for a rapid detection and quantification of avian influenza virus RNA in clinical samples collected from mute swans. Conserved regions in the matrix protein gene of avian influenza virus served as targets for the primers and TaqMan probe design. A recombinant plasmid containing the matrix protein gene amplicon was constructed for a quantitative assay of copy numbers of the target gene. Quantification of avian influenza virus RNA was accomplished using a standard curve generated from ten-fold serial dilutions of recombinant plasmid DNA in the range of 10<sup>2</sup> to 10<sup>8</sup> copies/µl. Avian influenza virus A/Cygnus olor/Brno-cz/2006 was adapted to grow in VERO cells. In the same passage of cell cultivation, the concentration of viral RNA was determined to be 1.01 × 10<sup>7</sup> copies/ml and TCID<sub>50</sub> was 10<sup>4.2</sup>/ml. From these values the ratio of one RNA copy to 0.00157 virion capable of VERO cells infection was calculated. This ratio was used to estimate the virus concentrations in the tissues of dead mute swans.

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