Evaluation of anti-influenza efficiency of polyclonal IgG antibodies specific to the ectodomain of M2 protein of influenza A virus by passive immunization of mice

2011 ◽  
Vol 55 (3) ◽  
pp. 261-265 ◽  
Author(s):  
J. KIRÁLY ◽  
E. VAREČKOVÁ ◽  
V. MUCHA ◽  
F. KOSTOLANSKÝ
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Passive Immunization ◽  
Igg Antibodies ◽  
M2 Protein ◽  
Polyclonal Igg

scholarly journals EPR Spectroscopy of the C-terminal Domain of the M2 Protein from Influenza A Virus

2009 ◽  
Vol 96 (3) ◽  
pp. 432a
Author(s):  
Emily Brown ◽  
Phuong Nguyen ◽  
Kathleen P. Howard
Keyword(s):  
Influenza A Virus ◽  
Epr Spectroscopy ◽  
Influenza A ◽  
M2 Protein ◽  
Terminal Domain

Physicochemical study of the influenza A virus M2 protein and aluminum salt adjuvant interaction as a vaccine candidate model

2019 ◽  
Vol 14 (8) ◽  
pp. 523-536
Author(s):  
Maryam Saleh ◽  
Jamileh Nowroozi ◽  
Fatemeh Fotouhi ◽  
Behrokh Farahmand
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Structural Changes ◽  
Vaccine Candidate ◽  
Human Influenza ◽  
M2 Protein ◽  
Physicochemical Methods ◽  
Α Helix ◽  
High Level ◽  
Β Sheet

Aim: The present study evaluated the structural changes resulting from the interaction between a recombinant influenza A virus M2 protein and aluminum hydroxide adjuvant to investigate the antigen for further immunological studies. Materials & methods: Membrane protein II was produced from the H1N1 subtype of human influenza A virus. The interaction between M2 protein and alum inum hydroxide adjuvant was evaluated by physicochemical techniques including scanning electron microscope, UV-Vis spectra, Fourier-transform infrared spectroscopy and circular dichroism spectroscopy. Results: Physicochemical methods showed high-level protein adsorption and accessibility to the effective parts of the protein. Conclusion: It was concluded that M2 protein secondary structural perturbations, including the α-helix-to-β-sheet transition, enhanced its mechanical properties toward adsorption.

Direct Measurement of the Influenza A Virus M2 Protein Ion Channel Activity in Mammalian Cells

Virology ◽  
1994 ◽  
Vol 205 (1) ◽  
pp. 133-140 ◽  
Author(s):  
Chang Wang ◽  
Robert A. Lamb ◽  
Lawrence H. Pinto
Keyword(s):  
Ion Channel ◽  
Influenza A Virus ◽  
Direct Measurement ◽  
Mammalian Cells ◽  
Influenza A ◽  
Channel Activity ◽  
M2 Protein

scholarly journals Production of the M2 protein of influenza A virus in insect cells is enhanced in the presence of amantadine

1993 ◽  
Vol 74 (8) ◽  
pp. 1673-1677 ◽  
Author(s):  
R. A. Black ◽  
P. A. Rota ◽  
N. Gorodkova ◽  
A. Cramer ◽  
H.-D. Klenk ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Insect Cells ◽  
M2 Protein

scholarly journals Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR

2013 ◽  
Vol 22 (11) ◽  
pp. 1623-1638 ◽  
Author(s):  
Shu Yu Liao ◽  
Keith J. Fritzsching ◽  
Mei Hong
Keyword(s):  
Solid State ◽  
Conformational Analysis ◽  
Influenza A Virus ◽  
Solid State Nmr ◽  
Influenza A ◽  
Full Length ◽  
M2 Protein

scholarly journals Extending the Cytoplasmic Tail of the Influenza A Virus M2 Protein Leads to Reduced Virus Replication In Vivo but Not In Vitro

2007 ◽  
Vol 82 (2) ◽  
pp. 1059-1063 ◽  
Author(s):  
Wai-Hong Wu ◽  
Andrew Pekosz
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Mdck Cells ◽  
Cytoplasmic Tail ◽  
M2 Protein ◽  
Coding Region ◽  
Epitope Tag ◽  
Carboxy Terminal

ABSTRACT A carboxy-terminal epitope tag introduced into the coding region of the A/WSN/33 M2 protein resulted in a recombinant virus (rWSN M2myc) which replicated to titers similar to those of the parental virus (rWSN) in MDCK cells. The rWSN M2myc virus was attenuated in its ability to induce mortality and weight loss after the intranasal inoculation of BALB/c mice, indicating that the M2 cytoplasmic tail plays a role in virus virulence. Mice infected with rWSN M2myc were completely protected from subsequent challenge with rWSN, suggesting that epitope tagging of the M2 protein may be a useful way of attenuating influenza A virus strains.

scholarly journals Characterizations of four monoclonal antibodies against M2 protein ectodomain of influenza A virus

Virology ◽  
2009 ◽  
Vol 385 (1) ◽  
pp. 218-226 ◽  
Author(s):  
Tong-Ming Fu ◽  
Daniel C. Freed ◽  
Melanie S. Horton ◽  
Jiang Fan ◽  
Michael P. Citron ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Influenza A Virus ◽  
Influenza A ◽  
M2 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.

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