Influenza virus M2 extracellular domain (M2e) has been a target for developing cross-protective vaccines. However, the efficacy and immune correlates of M2e vaccination are poorly understood in the different host genetic backgrounds in comparison with influenza vaccines. We previously reported the cross-protective efficacy of virus-like particle (M2e5x VLP) vaccines containing heterologous tand...

Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccine antigens, and resistance to antivirals can appear rapidly and become entrenched in circulating ...

A Monte Carlo program is presented for the computation of the most general cross section for two-photon production in ee collisions at fixed twophoton invariant mass W . Functions implemented for the five γγ structure functions include three models of the total hadronic cross section and the lepton-pair production cross section. Prospects of a structure-function determination through a study of...

In the face of increasingly serious environmental pollution, health human lung tissues is also facing threats. Mogroside ⅡE (M2E) main metabolite sweetening agents mogrosides from anti-tussive Chinese herbal Siraitia Grosvenori. The study elucidated anti-inflammatory action and molecular mechanism M2E against acute injury (ALI). A lipopolysaccharide (LPS)-induced ALI model was establishe...

background: sequence variations in glycoproteins of influenza virus surface impel us to design new candidate vaccines yearly. ectodomain of influenza m2 protein is a surface and highly conserved protein. m2e in influenza vaccines may eliminate the need for changing vaccine formulation every year. objectives: in this study, a recombinant baculovirus containing m2e and cholera toxin subunit b fus...

We have developed an antagonist to suppressor of cytokine signaling 1 (SOCS1), pJAK2(1001-1013), which corresponds to the activation loop of the Janus kinase JAK2, which is the binding site for the kinase inhibitory region (KIR) of SOCS1. Internalized pJAK2(1001-1013) inhibits SOCS1 and SOCS3. SOCS1 has been shown to be an influenza virus-induced virulence factor that enhances infection of cell...