Recombinant IAV H3N2 (A/Brisbane/10/2007) Nucleoprotein [His]

Liquiritin is an anti-viral agent of H1N1 and H3N2 influenza A virus which was reported to inhibit H1N1 and H3N2 NA enzyme with IC(50)value of 82.3 and > 100 mu M, respectively. The ground state optimized geometry was carried out for Liquiritin molecule through DFT method. The experimental vibrational (FT-IR and FT-Raman) and electronic (UV-Vis) spectral information were analysed and compared with theoretical data. The MEP and Fukui functions were determined for Liquiritin to analyse the electrophilic and nucleophilic attack of the molecule. The NBO and HOMO-LUMO were concluded for Liquiritin to investigate the chemical reactivity and kinetic stability. The druglikeness and ADMET predictions were analysed for Liquiritin, and it confirms the Lipinski's rule of five. Liquiritin fits very well in the active site cavity of H1N1 and H3N2 NA enzyme with binding energies of - 6.36 and - 5.87 kcal mol(-1)and inhibition constants (21.76 and 49.98 ki UM micromol), respectively, through docking study. Consequently, the molecule reveals good biological behaviour in nature and it can act as a probable drug candidate for H1N1 and H3N2 viral influenza.

Rotavirus A (RVA) remains one of the most widespread causes of diarrheal disease and mortality in piglets despite decades of research and efforts to boost lactogenic immunity for passive protection. Genetic changes at B cell epitopes (BCEs) may be driving failure of lactogenic immunity, which relies on production of IgA antibodies to passively neutralize RVA within the piglet gut, yet little research has mapped epitopes to swine-specific strains of RVA. Here we describe a bioinformatic approach to predict BCEs on the VP7 outer capsid protein using sequence data alone. We first validated the approach using a previously published dataset of VP7-specific cross-neutralization titers, and found that amino acid changes at predicted BCEs on the VP7 protein allowed for accurate recapitulation of antigenic relationships among the strains. Applying the approach to a dataset of swine RVA sequences identified 9 of the 11 known BCEs previously mapped to swine strains, indicating that epitope prediction can identify sites that are known to drive neutralization escapein vitro. Additional genotype-specific BCEs were also predicted that may be the cause of antigenic differences among strains of RVA on farms and should be targeted for further confirmatory work. The results of this work lay the groundwork for high throughput, immunologically-relevant analysis of swine RVA sequence data, and provide potential sites that can be targeted with vaccines to reduce piglet mortality and support farm health.