Regulation of Host Immune Responses against Influenza A Virus Infection by Mitogen-Activated Protein Kinases (MAPKs)

Influenza is a major respiratory viral illness caused by infection of influenza A virus (IAV), which still persists in various global seasonal epidemics every year. the host immune response is a key factor that determines the severity of influenza infection, present an attractive target for the development of new therapies for the treatment.

Among the double track signal transduction that regulates the activation of the host immune response and function in response to infection IAV, the mitogen-activated protein kinase (MAPK) pathway that wicks important signaling, downstream receptors pattern recognition (PRRS), activated by IAVs that regulate various processes cell in the immune cells of both the innate and adaptive immunity.

In addition, aberrant activation of MAPK overexuberant underlying the production of inflammatory mediators, promoting the development of a “cytokine storm”, the characteristics of severe respiratory viral diseases. Therefore, explanation of MAPK regulatory role in the immune response to IAVs not only important for understanding the pathogenesis of severe influenza, but it is also important to develop a MAPK-dependent therapies for the treatment of respiratory viral diseases. In this review, we will summarize the current understanding of the function of MAPK in both the innate and adaptive immune responses to IAVs and discuss their contribution to the cytokine storm caused by the highly pathogenic influenza virus.


Trimeric soluble recombinant influenza A virus hemagglutinins (HA) and tetrameric neuraminidases (NA) has proven to be an excellent tool to decipher biological properties. Receptor binding and cleavage of sialic acid by a recombinant protein correlated satisfactory compared with the whole virus. Expression of HA and NA can be achieved in many different laboratories host.

For the study of immunology and receptor interactions, however, insect and mammalian cell expressed proteins are preferred because of the presence of N-linked glycosylation and disulfide bond formation. Because the expression of mammalian cells is widely applied, yield enhancement expression is an important goal. Here we report that the use of codon-optimized genes and fusion sfGFP, HA expression results can be improved

Regulation of Host Immune Responses against Influenza A Virus Infection by Mitogen-Activated Protein Kinases (MAPKs)
Regulation of Host Immune Responses against Influenza A Virus Infection by Mitogen-Activated Protein Kinases (MAPKs)

Comparative Analysis of Antiviral Activity of IgG and IgA antibodies to Influenza A Virus M2 Protein

The influenza A virus (IAV) matrix-2 (M2) protein is a viral envelope proteins conserved antigens that plays an important role in virus starters together with other envelope proteins, hemagglutinin (HA). M2-specific mouse monoclonal antibody IgG, rM2ss23, which binds to the ectodomain of the M2 protein, has been shown to be non-neutralizing antibodies, but inhibits plaque formation IAV strains.

In this study, we produce rM2ss23 chimeric (ch-rM2ss23) IgG and IgA antibodies with the same variable region and compared their antiviral activity. Using gel chromatography, ch-rM2ss23 IgA is divided into three subsets of antibodies: IgA monomer (m-IgA), dimeric IgA (d-IgA), and trimeric and tetrameric IgA (t / q-IgA).

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Hemoglobin Assay Kit

abx298879-100Assays 100 Assays
EUR 488.00
  • Shipped within 5-10 working days.

Copper Assay Kit

abx298883-100Assays 100 Assays
EUR 425.00
  • Shipped within 5-10 working days.

Proteasome Assay Kit

55R-1341 100 assays
EUR 654.00
Description: Assay Kit for detection of Proteasome in the research laboratory

Calpain Assay Kit

55R-1342 100 assays
EUR 779.00
Description: Assay Kit for detection of Calpain in the research laboratory

Glutathione Assay Kit

55R-1343 100 assays
EUR 654.00
Description: Assay Kit for detection of Glutathione in the research laboratory

Glutathione Assay Kit

55R-1354 100 assays
EUR 895.00
Description: Assay Kit for detection of Glutathione activity in the research laboratory

HDAC Assay Kit

55R-1371 100 assays
EUR 673.00
Description: Assay Kit for detection of HDAC in the research laboratory

HDAC Assay Kit

55R-1372 100 assays
EUR 673.00
Description: Assay Kit for detection of HDAC in the research laboratory

HAT Assay Kit

55R-1373 100 assays
EUR 740.00
Description: Assay Kit for detection of HAT in the research laboratory

SOD Assay Kit

55R-1374 100 assays
EUR 602.00
Description: Assay Kit for detection of SOD in the research laboratory

HDAC3 Assay Kit

55R-1377 100 assays
EUR 693.00
Description: Assay Kit for detection of HDAC3 in the research laboratory

HDAC8 Assay Kit

55R-1379 100 assays
EUR 689.00
Description: Assay Kit for detection of HDAC8 in the research laboratory

ATP Assay Kit

55R-1380 100 assays
EUR 809.00
Description: Assay Kit for detection of ATP in the research laboratory

ADP Assay Kit

55R-1381 100 assays
EUR 809.00
Description: Assay Kit for detection of ADP in the research laboratory

FAD Assay Kit

55R-1382 100 assays
EUR 732.00
Description: Assay Kit for detection of FAD in the research laboratory

PEP Assay Kit

55R-1384 100 assays
EUR 876.00
Description: Assay Kit for detection of PEP in the research laboratory

Ammonia Assay Kit

55R-1388 100 assays
EUR 740.00
Description: Assay Kit for detection of Ammonia in the research laboratory

cAMP Assay Kit

55R-1389 100 assays
EUR 706.00
Description: Assay Kit for detection of cAMP activity in the research laboratory

cGMP Assay Kit

55R-1390 100 assays
EUR 706.00
Description: Assay Kit for detection of cGMP activity in the research laboratory

Urea Assay Kit

55R-1391 100 assays
EUR 740.00
Description: Assay Kit for detection of Urea in the research laboratory

Calcium Assay Kit

55R-1392 250 assays
EUR 586.00
Description: Assay Kit for detection of Calcium activity in the research laboratory

Magnesium Assay Kit

55R-1393 100 assays
EUR 654.00
Description: Assay Kit for detection of Magnesium in the research laboratory

We found that t / q-IgA have significantly higher capacity to reduce plaque size of IAVs of m-IgG and IgA, most likely caused by a decrease in the number of offspring produced virus particles from infected cells. Interestingly, HA-M2 colocalization was greatly reduced on the surface of infected cells with antibodies ch-rM2ss23. These results indicate that the polymeric IgA anti-M2 Limit beginner IAV more efficient than IgG and suggested the role of anti-M2 IgA cross-protective immunity IAVs.