scholarly journals Comparative Analyses of the Antiviral Activities of IgG and IgA Antibodies to Influenza A Virus M2 Protein

Viruses ◽  
2020 ◽  
Vol 12 (7) ◽  
pp. 780
Author(s):  
Kosuke Okuya ◽  
Nao Eguchi ◽  
Rashid Manzoor ◽  
Reiko Yoshida ◽  
Shinji Saito ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Envelope Protein ◽  
Influenza A ◽  
Viral Envelope ◽  
Progeny Virus ◽  
Gel Chromatography ◽  
M2 Protein ◽  
Igg Antibody ◽  
Iga Antibodies ◽  
Antiviral Activities

The influenza A virus (IAV) matrix-2 (M2) protein is an antigenically conserved viral envelope protein that plays an important role in virus budding together with another envelope protein, hemagglutinin (HA). An M2-specific mouse monoclonal IgG antibody, rM2ss23, which binds to the ectodomain of the M2 protein, has been shown to be a non-neutralizing antibody, but inhibits plaque formation of IAV strains. In this study, we generated chimeric rM2ss23 (ch-rM2ss23) IgG and IgA antibodies with the same variable region and compared their antiviral activities. Using gel chromatography, ch-rM2ss23 IgA were divided into three antibody subsets: monomeric IgA (m-IgA), dimeric IgA (d-IgA), and trimeric and tetrameric IgA (t/q-IgA). We found that t/q-IgA had a significantly higher capacity to reduce the plaque size of IAVs than IgG and m-IgA, most likely due to the decreased number of progeny virus particles produced from infected cells. Interestingly, HA-M2 colocalization was remarkably reduced on the infected cell surface in the presence of ch-rM2ss23 antibodies. These results indicate that anti-M2 polymeric IgA restricts IAV budding more efficiently than IgG and suggest a role of anti-M2 IgA in cross-protective immunity to IAVs.

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.

scholarly journals The Lack of an Inherent Membrane Targeting Signal Is Responsible for the Failure of the Matrix (M1) Protein of Influenza A Virus To Bud into Virus-Like Particles

2010 ◽  
Vol 84 (9) ◽  
pp. 4673-4681 ◽  
Author(s):  
Dan Wang ◽  
Aaron Harmon ◽  
Jing Jin ◽  
David H. Francis ◽  
Jane Christopher-Hennings ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Plasma Membrane ◽  
Influenza A Virus ◽  
Influenza A ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Membrane Targeting ◽  
Virus Like Particles ◽  
The Matrix ◽  
Targeting Signal

ABSTRACT The matrix protein (M1) of influenza A virus is generally viewed as a key orchestrator in the release of influenza virions from the plasma membrane during infection. In contrast to this model, recent studies have indicated that influenza virus requires expression of the envelope proteins for budding of intracellular M1 into virus particles. Here we explored the mechanisms that control M1 budding. Similarly to previous studies, we found that M1 by itself fails to form virus-like-particles (VLPs). We further demonstrated that M1, in the absence of other viral proteins, was preferentially targeted to the nucleus/perinuclear region rather than to the plasma membrane, where influenza virions bud. Remarkably, we showed that a 10-residue membrane targeting peptide from either the Fyn or Lck oncoprotein appended to M1 at the N terminus redirected M1 to the plasma membrane and allowed M1 particle budding without additional viral envelope proteins. To further identify a functional link between plasma membrane targeting and VLP formation, we took advantage of the fact that M1 can interact with M2, unless the cytoplasmic tail is absent. Notably, native M2 but not mutant M2 effectively targeted M1 to the plasma membrane and produced extracellular M1 VLPs. Our results suggest that influenza virus M1 may not possess an inherent membrane targeting signal. Thus, the lack of efficient plasma membrane targeting is responsible for the failure of M1 in budding. This study highlights the fact that interactions of M1 with viral envelope proteins are essential to direct M1 to the plasma membrane for influenza virus particle release.

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 Protective effect of low-concentration chlorine dioxide gas against influenza A virus infection

2008 ◽  
Vol 89 (1) ◽  
pp. 60-67 ◽  
Author(s):  
Norio Ogata ◽  
Takashi Shibata
Keyword(s):  
Influenza Virus ◽  
Virus Infection ◽  
Influenza A Virus ◽  
Chlorine Dioxide ◽  
Influenza A ◽  
Influenza Virus Infection ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Exposure Level ◽  
Low Concentration

Influenza virus infection is one of the major causes of human morbidity and mortality. Between humans, this virus spreads mostly via aerosols excreted from the respiratory system. Current means of prevention of influenza virus infection are not entirely satisfactory because of their limited efficacy. Safe and effective preventive measures against pandemic influenza are greatly needed. We demonstrate that infection of mice induced by aerosols of influenza A virus was prevented by chlorine dioxide (ClO2) gas at an extremely low concentration (below the long-term permissible exposure level to humans, namely 0.1 p.p.m.). Mice in semi-closed cages were exposed to aerosols of influenza A virus (1 LD50) and ClO2 gas (0.03 p.p.m.) simultaneously for 15 min. Three days after exposure, pulmonary virus titre (TCID50) was 102.6±1.5 in five mice treated with ClO2, whilst it was 106.7±0.2 in five mice that had not been treated (P=0.003). Cumulative mortality after 16 days was 0/10 mice treated with ClO2 and 7/10 mice that had not been treated (P=0.002). In in vitro experiments, ClO2 denatured viral envelope proteins (haemagglutinin and neuraminidase) that are indispensable for infectivity of the virus, and abolished infectivity. Taken together, we conclude that ClO2 gas is effective at preventing aerosol-induced influenza virus infection in mice by denaturing viral envelope proteins at a concentration well below the permissible exposure level to humans. ClO2 gas could therefore be useful as a preventive means against influenza in places of human activity without necessitating evacuation.

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
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