IAV M2e Specific Neutra™ Antibody Products

Creative Biolabs’ IAV M2e antibody is a valuable tool for researchers investigating the influenza A virus. It offers solutions for key applications, delivering specific and reliable results. Our solutions deliver the tools and expertise necessary to overcome the obstacles in rabies virus research.

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Introduction of IAV M2e

The influenza A virus M2 proton channel serves as a multifunctional scaffold critical for viral pathogenesis, operating through three discrete mechanisms. First, its tetrameric pore facilitates coordinated ion flux during uncoating: early endosomal pH (6.5-6.0) triggers proton conductance that disrupts M1-vRNP binding, while subsequent potassium influx at pH 5.4-6.0 dissolves ribonucleoprotein complex cohesion. This pH-regulated priming enables HA-mediated membrane fusion and nuclear-directed vRNP release.

Fig. 1 The structure of matrix protein 2 (M2).^1,3

Secondly, M2 is necessary for assembling and budding new viruses. The distal end of M2's cytoplasmic portion interacts with M1, which facilitates virion assembly. The proximal, cytoplasmic, amphipathic α-helix of M2 governs the budding process. Within the plasma membrane of infected cells, M2 accumulates at the edges of lipid rafts containing HA and neuraminidase, altering membrane curvature. This eventually severs newly formed virions. Finally, M2 affects various host cell functions. In myeloid cells, the ion channel function may activate inflammasomes, while a conserved LC3 interaction motif near the carboxyl terminus of its cytoplasmic region may interfere with autophagy The functional counterpart of M2 in influenza B virus is termed BM2. Similar to M2, BM2 can transport protons across the membrane and interact with influenza B virus's M1. The sequences of M2 and BM2 differ significantly.

The ectodomain of the influenza A virus matrix protein 2 (M2e) is a promising candidate for a universal vaccine against influenza A. Numerous experiments conducted on mice have shown that M2e-based vaccines can effectively provide protection against various influenza A virus challenges, but there is limited research on their efficacy in natural hosts.

Antibodies against IAV M2e

The influenza A virus M2 proton channel serves as a multifunctional scaffold critical for viral pathogenesis, operating through three discrete mechanisms. First, its tetrameric pore facilitates coordinated ion flux during uncoating: early endosomal pH (6.5-6.0) triggers proton conductance that disrupts M1-vRNP binding, while subsequent potassium influx at pH 5.4-6.0 dissolves ribonucleoprotein complex cohesion. This pH-regulated priming enables HA-mediated membrane fusion and nuclear-directed vRNP release. Second, M2 orchestrates virion morphogenesis through membrane-proximal interactions. The C-terminal domain engages M1 for capsid scaffolding, while its amphipathic helix induces raft microdomain curvature through cholesterol-dependent oligomerization, ultimately catalyzing bud scission via SNARE-like membrane remodeling. Third, M2 subverts host defenses—channel-mediated NLRP3 inflammasome priming in dendritic cells contrasts with its LC3-interacting region (LIR motif)-mediated autophagy blockade through ATG5 sequestration.

Fig. 2 Mechanism of protection of M2e–specific immunoglobulin G.^1,3

The influenza A virus M2 ectodomain (M2e) is a broadly protective vaccine candidate for influenza A. Numerous experimental studies in mice have shown that M2e-based vaccines can effectively protect against any influenza A virus challenge, but limited research has been conducted in natural hosts. M2e immunity is primarily mediated by IgG, and early clinical trials have demonstrated the vaccine's safety.

Published Data

Fig. 3 M2e-specific VHHs and their binding specificities.^2,3

A new strategy to combat influenza A virus, centered on a designed single-domain antibody (VHH) structure, was created. This construct selectively draws innate immune cells to where the virus is multiplying. The protective agent comprises two VHHs. One VHH exhibits nanomolar affinity for the conserved ectodomain of influenza A's matrix protein 2 (M2e). A second VHH, chosen for its specific binding to mouse Fcγ receptor IV (FcγRIV), is genetically linked to the M2e-specific VHH. This results in a bispecific VHH-based structure that can be effectively produced in Pichia pastoris. This single-domain antibody agent specifically triggers mouse FcγRIV when exposed to cells expressing M2 or infected with influenza A virus. Research indicates that humanized, formatted, M2e-specific VHHs could represent a novel therapeutic avenue for addressing influenza A virus infection.

Why Choose Us?

Creative Biolabs is a trusted provider of high-quality antibodies, including those targeting IAV M2e. We offer several key advantages:

• Specificity and Sensitivity: Our IAV M2e antibodies are generated using carefully designed antigens and undergo rigorous screening to ensure exceptional specificity and sensitivity, minimizing off-target binding and maximizing signal-to-noise ratios.
• Customization Options: We offer a range of antibody formats and modifications to meet your specific research needs, including different isotypes, conjugates (e.g., HRP, FITC), and purification levels.
• Expert Support: Our team of experienced scientists provides comprehensive technical support, assisting you with experimental design, antibody selection, and troubleshooting.
• Reliable Performance: Creative Biolabs antibodies are manufactured under strict quality control standards, ensuring consistent performance and reproducibility in your experiments.
• Published Data: Creative Biolabs products are frequently cited in peer-reviewed publications, demonstrating their reliability and effectiveness in scientific research.

For more information about Creative Biolabs' IAV M2e antibodies and services, please contact us.

REFERENCES

1. Saelens, Xavier. "The role of matrix protein 2 ectodomain in the development of universal influenza vaccines." The Journal of infectious diseases 219.Supplement_1 (2019): S68-S74.
2. De Vlieger, Dorien, et al. "Selective engagement of FcγRIV by a m2e-specific single domain antibody construct protects against influenza A virus infection." Frontiers in Immunology 10 (2019): 2920.
3. Distributed under Open Access license CC BY 4.0, without modification.