Estimation of the evolutionary stability of the Influenza A virus: Prediction of variable regions in the domain structure of the M1 protein

2010 ◽  
Vol 65 (4) ◽  
pp. 221-223 ◽  
Author(s):  
M. A. Kuznetsova ◽  
U. A. Pekov ◽  
A. L. Ksenofontov ◽  
L. V. Kordyukova ◽  
V. L. Drutsa
Keyword(s):  
Domain Structure ◽  
Influenza A Virus ◽  
Influenza A ◽  
Evolutionary Stability ◽  
Variable Regions ◽  
M1 Protein

scholarly journals Cyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication

2009 ◽  
Vol 11 (5) ◽  
pp. 730-741 ◽  
Author(s):  
Xiaoling Liu ◽  
Lei Sun ◽  
Maorong Yu ◽  
Zengfu Wang ◽  
Chongfeng Xu ◽  
...  
Keyword(s):  
Viral Replication ◽  
Influenza A Virus ◽  
Influenza A ◽  
Early Stage ◽  
Cyclophilin A ◽  
M1 Protein

Matrix proteins of enveloped viruses: a case study of Influenza A virus M1 protein

2018 ◽  
Vol 37 (3) ◽  
pp. 671-690 ◽  
Author(s):  
Larisa V. Kordyukova ◽  
Eleonora V. Shtykova ◽  
Lyudmila A. Baratova ◽  
Dmitri I. Svergun ◽  
Oleg V. Batishchev
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Matrix Proteins ◽  
Enveloped Viruses ◽  
M1 Protein

scholarly journals Distinct Domains of the Influenza A Virus M2 Protein Cytoplasmic Tail Mediate Binding to the M1 Protein and Facilitate Infectious Virus Production

2006 ◽  
Vol 80 (16) ◽  
pp. 8178-8189 ◽  
Author(s):  
Matthew F. McCown ◽  
Andrew Pekosz
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Reverse Genetics ◽  
Infectious Virus ◽  
Virus Assembly ◽  
Virus Production ◽  
Cytoplasmic Tail ◽  
M2 Protein ◽  
Virus Particles ◽  
M1 Protein

ABSTRACT The cytoplasmic tail of the influenza A virus M2 protein is highly conserved among influenza A virus isolates. The cytoplasmic tail appears to be dispensable with respect to the ion channel activity associated with the protein but important for virus morphology and the production of infectious virus particles. Using reverse genetics and transcomplementation assays, we demonstrate that the M2 protein cytoplasmic tail is a crucial mediator of infectious virus production. Truncations of the M2 cytoplasmic tail result in a drastic decrease in infectious virus titers, a reduction in the amount of packaged viral RNA, a decrease in budding events, and a reduction in budding efficiency. The M1 protein binds to the M2 cytoplasmic tail, but the M1 binding site is distinct from the sequences that affect infectious virus particle formation. Influenza A virus strains A/Udorn/72 and A/WSN/33 differ in their requirements for M2 cytoplasmic tail sequences, and this requirement maps to the M1 protein. We conclude that the M2 protein is required for the formation of infectious virus particles, implicating the protein as important for influenza A virus assembly in addition to its well-documented role during virus entry and uncoating.

scholarly journals Functional and antigenic domains of the matrix (M1) protein of influenza A virus.

1987 ◽  
Vol 61 (2) ◽  
pp. 239-246 ◽  
Author(s):  
Z P Ye ◽  
R Pal ◽  
J W Fox ◽  
R R Wagner
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
M1 Protein ◽  
The Matrix ◽  
Antigenic Domains

scholarly journals Tyrosine 132 Phosphorylation of Influenza A Virus M1 Protein Is Crucial for Virus Replication by Controlling the Nuclear Import of M1

2013 ◽  
Vol 87 (11) ◽  
pp. 6182-6191 ◽  
Author(s):  
S. Wang ◽  
Z. Zhao ◽  
Y. Bi ◽  
L. Sun ◽  
X. Liu ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Virus Replication ◽  
Nuclear Import ◽  
Influenza A ◽  
M1 Protein

The In Situ Structural Characterization of the Influenza A Virus Matrix M1 Protein within a Virion

2009 ◽  
Vol 16 (11) ◽  
pp. 1407-1413 ◽  
Author(s):  
Alexander Shishkov ◽  
Elena Bogacheva ◽  
Alexey Dolgov ◽  
Alexey Chulichkov ◽  
Denis Knyazev ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Structural Characterization ◽  
Influenza A ◽  
M1 Protein

scholarly journals Influenza A virus M1 blocks the classical complement pathway through interacting with C1qA

2009 ◽  
Vol 90 (11) ◽  
pp. 2751-2758 ◽  
Author(s):  
Junjie Zhang ◽  
Gang Li ◽  
Xiaoling Liu ◽  
Zengfu Wang ◽  
Wenjun Liu ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Influenza A Virus ◽  
Influenza A ◽  
Critical Role ◽  
Complement Pathway ◽  
Virus Propagation ◽  
Classical Complement Pathway ◽  
M1 Protein ◽  
Classical Complement

The matrix (M1) protein of influenza A virus is a conserved multifunctional protein that plays essential roles in regulating the viral life cycle. This study demonstrated that M1 is able to interact with complement C1qA and plays an important inhibitory function in the classical complement pathway. The N-terminal domain of M1 protein was required for its binding to the globular region of C1qA. As a consequence, M1 blocked the interaction between C1qA and heat-aggregated IgG in vitro and inhibited haemolysis. It was shown that M1 protein prevented the complement-mediated neutralization of influenza virus in vitro. In addition, studies on mice indicated that the administration of M1 could promote a higher virus propagation rate in lung and shortened survival of mice infected with the virus. Taken together, these results suggest strongly that the M1 protein plays a critical role in protecting influenza virus from the host innate immune system.

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

Virus Genes ◽  
2014 ◽  
Vol 49 (1) ◽  
pp. 157-162 ◽  
Author(s):  
Qinfang Liu ◽  
Bhupinder Bawa ◽  
Jingjiao Ma ◽  
Feng Li ◽  
Wenjun Ma ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Crucial Role ◽  
Influenza A ◽  
Terminal Domain ◽  
M1 Protein
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