No abstract

Riemerella anatipestifer(RA) is a gram-negative bacterium that is susceptible to poultry such as domestic ducks and geese. Young birds have a high mortality rate after infection. The resistance caused by the abuse of antibiotics is also getting worse. Since there are 25 serotypes of RA, and the cross-immunization between serotypes is weak, it is necessary to find a vaccine that has cross-immunization against multiple serotypes of RA. In this article, the bioinformatics analysis of RA Proin protein was conducted, and it was speculated that it has the potential of a subunit vaccine. The protein was recombinantly expressed and purified, and immunized with Cherry Valley Duck. The results show that the serum antibodies of the Porin protein immunized group were positive at 1:24300 for the porin protein and RA strains CH1. The serum could improve the killing effect of complement and phagocytic cells on RA. After the challenge, the survival rate of Cherry Valley Duck can be increased by 80%.

Second generation non-nucleoside reverse transcriptase inhibitors (NNRTIs) etravirine and rilpivirine are essential components in the highly active antiretroviral therapy for the treatment of patients infected with human immunodeficiency virus type 1 (HIV-1). They are highly potent drugs against wild-type viruses and have exhibited excellent antiviral activities against some NNRTIs-resistant HIV-1 variants. In order to understand the underlying mechanism behind their robust resistance profile in comparison with the first generation NNRTIs nevirapine and efavirenz, it is necessary to quantitatively analyze their binding pockets in the wild-type HIV-1 reverse transcriptase (RT) and various HIV-1 RT mutants at the molecular level. Therefore, a high-level ab initio quantum chemical analysis was performed to decipher the molecular determinants for recognition of etravirine and rilpivirine by the wild-type RT and some RT mutants (K103N, K103N/Y181C, and K103N/L100I) of clinically important virus strains. Pair wise intermolecular interaction analysis determined the contribution of individual intermolecular interactions to the binding affinities between the second generation NNRTIs (etravirine or rilpivirine) and several variants of RTs, including the wild-type RT, and clinically relevant K103N, K103N/Y181C, and K103N/L100I mutant RTs. This quantitative analysis led to the identification of drug-protein interactions that persist despite mutations as well as to the evaluation of stabilization energy losses upon mutations. The results of this study enhanced our understanding of the molecular level mechanisms by which the second generation NNRTI drugs maintain their strong binding to mutant RTs. It is hoped that findings of this work would have a direct impact on designing new NNRTIs that are even more resilient to mutations in future.