Peptide M, an 18-amino acid fragment from position 303 to position 320 of retinal S-antigen, produces experimental autoimmune uveitis (EAU), similar to that produced by native S-antigen, in several vertebrate species including nonhuman primates. It was observed that 12 of the 39 (30.7%) patients with uveitis, 1 of the 29 (3.4%) patients with systemic connective tissue disorders (CTD) without eye involvement, 2 of the 7 (5.8%) patients of CTD with uveitis, 1 of the 17 (5.8%) patients with diabetic retinopathy, and none of the 19 normal healthy controls showed a significant lymphoproliferative response to peptide M (stimulation index of 3 or more). Yeast histone H3 peptide gave a positive response in 1 (2.5%), 2 (6.8%), 1 (14.2%), 2 (11.7%), and 2 (10.5%) individuals, respectively, in the different groups studied. In a few cases a positive response to yeast histone H3 peptide was observed without significant stimulation to peptide M. These findings indicate that peptide M could also be an immunogenic epitope of S-antigen in humans and be aetiopathologically related to uveitis in a subset of patients with this disease. However, unlike experimental animals, the responses to peptide M and yeast histone H3 were nonconcordant, necessitating further studies.

Chandipura vesiculovirus (CHPV) is a rapidly emerging pathogen responsible for causing acute encephalitis. Due to its widespread occurrence in Asian and African countries, this has become a global threat, and there is an urgent need to design an effective and non-allergenic vaccine against this pathogen. The conventional method of vaccine design involves large proteins or whole organism which leads to unnecessary antigenic load with increased chances of allergenic reactions. In addition, the process is also very time consuming and labour intensive. These limitations can be overcome by peptide-based vaccines comprising of short immunogenic peptide fragments that can elicit highly targeted immune responses, avoiding the chances of allergenic reactions, in a relatively shorter time span. The multi-epitope vaccine constructed using CTL, HTL and IFN-γ epitopes was able to elicit specific immune responses when exposed to the pathogen, in-silico. Not only that, Molecular Docking and Molecular Dynamics Simulation studies confirmed a stable interaction of the vaccine with the immune receptors. Several physicochemical analyses of the designed vaccine candidate confirmed it to be highly immunogenic and non-allergic. The computer-aided analysis performed in this study suggests that the designed multi-epitope vaccine can elicit specific immune responses and can be a potential candidate against CHPV.

Chandipura vesiculovirus (CHPV) is a rapidly emerging pathogen responsible for causing acute encephalitis. Due to its widespread occurrence in Asian and African countries, this has become a global threat, and there is an urgent need to design an effective and nonallergenic vaccine against this pathogen. The present study aimed to develop a multi‐epitope vaccine using an immunoinformatics approach. The conventional method of vaccine design involves large proteins or whole organism which leads to unnecessary antigenic load with increased chances of allergenic reactions. In addition, the process is also very time‐consuming and labor‐intensive. These limitations can be overcome by peptide‐based vaccines comprising short immunogenic peptide fragments that can elicit highly targeted immune responses, avoiding the chances of allergenic reactions, in a relatively shorter time span. The multi‐epitope vaccine constructed using CTL, HTL, and IFN‐γ epitopes was able to elicit specific immune responses when exposed to the pathogen, in silico. Not only that, molecular docking and molecular dynamics simulation studies confirmed a stable interaction of the vaccine with the immune receptors. Several physicochemical analyses of the designed vaccine candidate confirmed it to be highly immunogenic and nonallergic. The computer‐aided analysis performed in this study suggests that the designed multi‐epitope vaccine can elicit specific immune responses and can be a potential candidate against CHPV.

A facile and highly efficient metal‐free approach has been unfolded for the synthesis of novel dihydrothiochromeno[4,3‐c]pyrazoles using elemental sulfur as a powerful sulfurating reagent. This method includes sp2 C−H functionalization followed by sp2 C−NO2 group displacement using elemental sulfur as an odourless sulfur source activated by DABCO in DMSO. Using the developed synthetic strategy, a library of 29 novel dihydrothiochromeno[4,3‐c]pyrazoles, incorporating two pharmacologically important scaffolds has been synthesized in 52–76% yield with a broad substrate scope. A sensible mechanistic proposal has been projected based on control experiments.