SalmonellaTyphimurium is an important pathogen having a broad host range. In human population it causes mostly gastroenteritis but there are reports in which it was found to be responsible to cause several lethal diseases like endocarditis and meningitis. Poultry products are the major sources of this organism in India as these are consumed at various stages of cooking. The available vaccines have their own limitations such as short-term immunity. Outer membrane proteins have shown some promising potential, so in the present study Omp C ofSalmonellaTyphimurium was cloned and sequenced to explore the possibility of development of r-DNA vaccine againstSalmonellaTyphimurium for poultry. The sequence of Omp C was studied for antigenic indexing, epitope mapping, and MHC mapping using various bioinformatic tools. The ORF analysis revealed a complete coding region of approximately 1000 bp. Five major and 13 minor B-cell epitopes were identified having an antigenic index of 1.7. The sequences also showed major histocompatibility complex (MHC) class I and class II binding region indicating a potential of eliciting cell-mediated immune response. The findings indicate that Omp C may be proven as promising candidate for development of r-DNA vaccine againstSalmonellaTyphimurium.

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Aim:Sheep milk-born bioactive peptides have been found to exhibit various physiological activities. The present work was designed with the aim to evaluate the effect of boiling on antidiabetic property of peptides derived from sheep milk caseinate on hydrolysis with three different proteases.Materials and Methods:In this investigation, casein prepared from raw and boiled sheep milk was hydrolyzed by three commercially available proteases (trypsin, pepsin, and chymotrypsin). These hydrolysates collected at different hydrolysis times (60, 120, 160, and 240 min) were assayed for their antidiabetic activity.Results:Among the three different enzyme hydrolysates, casein treated with chymotrypsin shows the highest antidiabetic activity among other enzymes. While the antidiabetic effect of raw milk-derived casein hydrolysates always exceeds than effect shown by boiled milk casein hydrolysates.Conclusion:The result obtained hence shows that the effect of boiling on the properties of bioactive peptides released during different enzyme digestion depends largely on the enzymatic formulation used and treatment conditions. Chymotrypsin treatment of raw casein yields peptides with maximum antidiabetic activity as compared to pepsin and trypsin. Moreover, the peptides produced after enzymatic treatment of boiled casein show reduced antidiabetic properties. Therefore, enzymatically treated raw milk casein hydrolysates may be used as effective nutritional supplements for diabetic patients, as it causes a significant inhibition of α-amylase activity.

Salmonellosis is one of the major global health concerns leading to millions of deaths annually. The present vaccines not being up to the mark necessitate the need for the development of new generation vaccines. Outer membrane proteins (Omps) of several Gram negative bacteria have been investigated and found to be immunogenic and protective. The present study explores the potential of a major porin protein (OmpC) of Salmonella Typhimurium, as a vaccine candidate. The OmpC 3D structure and its potential to bind effectively with antibodies and generate humoral response was investigated using in silico docking, and expressed in a heterogeneous Escherichia coli M15 host strain. The rOmpC was purified and its immunopotential was evaluated in vitro by western blotting and in vivo in three weeks old chicks. The recombinant OmpC produced a significant humoral response and in vaccinated birds 100% survival rate was observed along with delay in the shedding of organism in droppings. These findings indicate that the rOmpC vaccination prevents mortality in chicken and lowers fecal shedding in droppings.

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