[Antigenic and immunogenic activity of virus-like particles based on rabbit hemorrhagic disease virus (Caliciviridae: ) genotypes GI1 and GI2 recombinant major capsid proteins].

Introduction: Rabbit hemorrhagic disease is an acute highly contagious infection associated with two genotypes of pathogenic Lagovirus. Antibodies to major capsid protein (Vp60) are protective. The aim of the work ‒ is an evaluation of antigenic and immunogenic activity of virus-like particles (VLPs) based on recombinant major capsid proteins of both genotypes of rabbit hemorrhagic disease virus (RHDV) (recVP60-GI1 and recVP60-GI2).

In silico simulations reveal that RYR distribution affects the dynamics of calcium release in cardiac myocytes.

The dyads of cardiac myocytes contain ryanodine receptors (RYRs) that generate calcium sparks upon activation. To test how geometric factors of RYR distribution contribute to the formation of calcium sparks, which cannot be addressed experimentally, we performed in silico simulations on a large set of models of calcium release sites (CRSs). Our models covered the observed range of RYR number, density, and spatial arrangement.

p-Dimethylaminobenzaldehyde-based chemosensor for on-site sensing of ammonia precursor in concrete.

A chemosensor for on-site sensing of ammonia precursor in concrete to avoid a problem of ammonia emission into the indoor space of concrete buildings was designed and implemented. It was found that aqueous extracts of concrete samples containing antifreeze additives and excreting ammonia were colored in the presence of p-dimethylaminobenzaldehyde. This phenomenon was used for the fast visual sensing of main ammonia precursor (urea) in concrete for the first time.

Stochastic and deterministic approaches to modelling calcium release in cardiac myocytes at different spatial arrangements of ryanodine receptors.

Calcium release sites (CRSs) play a key role in excitation-contraction coupling of cardiac myocytes. Recent studies based on electron tomography and super-resolution imaging revealed that CRSs are not completely filled with ryanodine receptors (RyRs) and that the spatial arrangement of RyRs is neither uniform nor static. In this work, we studied the effect of spatial arrangement of RyRs on RyR activation using simulations based on Monte Carlo (MC) and mean-field (MF) approaches.