Type-2 diabetes mellitus (T2DM) is often linked with hyperglycemia, disturbed lipid profiles, inflammation, and gut dysbiosis. Omega-3 fatty acid supplementation has a vital role in the management of T2DM. As a result, a better understanding of the potential role of omega-3 fatty acids in the development and progression of T2DM by influencing the intestinal microflora will help to improve the therapeutic intervention for T2DM and related complications. Focusing on the molecular mechanisms and signaling pathways induced by omega-3 fatty acids, this paper attempts to comprehensively review and discuss the putative associations between omega-3 fatty acids, gut dysbiosis, and the pathophysiology of T2DM and its related comorbidities. In addition, we contemplate the importance of gut microbiota in T2DM prevention and treatment and ponder the role of omega-3 fatty acids in T2DM by positively modulating gut microbiota, which may lead to discovery of novel targets and therapeutic strategies thereby paving way for further comprehensive, mechanistic, and clinical studies.

From infancy through to old age, the microbiome plays an important role in modulating the host-immune system. As we age, our immune system and our gut microbiota change significantly in composition and function, which is linked to an increased vulnerability to infectious diseases and a decrease in vaccine responses. Our microbiome remains largely stable throughout adulthood; however, aging causes a major shift in the composition and function of the gut microbiome, as well as a decrease in diversity. Considering the critical role of the gut microbiome in the host-immune system, it is important to address, prevent, and ameliorate age-related dysbiosis, which could be an effective strategy for preventing/restoring functional deficits in immune responses as we grow older. Several factors, such as the host’s genetics and nutritional state, along with the gut microbiome, can influence vaccine efficacy or reaction. Emerging evidence suggests that the microbiome could be a significant determinant of vaccine immunity. Physiological mechanisms such as senescence, or the steady loss of cellular functions, which affect the aging process and vaccination responses, have yet to be comprehended. Recent studies on several COVID-19 vaccines worldwide have provided a considerable amount of data to support the hypothesis that aging plays a crucial role in modulating COVID-19 vaccination efficacy across different populations.

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Salmonella Typhimurium (ST) is the zoonotic pathogenic Gram-negative bacteria to causes infectious disease in humans as well as in animals. It causes gastrointestinal illness and fever called salmonellosis, which is foodborne diarrheal and leading cause of millions of deaths worldwide. Salmonella enterica serovar Typhimurium (S. Typhimurium) during its pathogenesis takeaway the actin cytoskeleton of their host cells and this is the crucial step of its infection cycle. Cyclophilin A, a type of peptidyl-prolyl isomerase that's encoded by the ppiA gene in ST, plays pleiotropic roles in maintaining bacterial physiology. In this research, the proteomic characterization of the peptidyl-prolyl cis-trans isomerase-A (Cyclophilin A) from Salmonella Typhimurium is reported. Cyclophilin A (CypA) protein from Salmonella Typhimurium proved to be a highly conserved protein sequence and highly homologous compared to other organisms. This protein was expressed in Escherichia coli and then puri ed in a recombinant form protein exhibited a characteristic PPIases activity (V max = 0.8752 ± 0.13892 µmoles/ min, K m = 0.9315 ± 0.5670 µM) in comparison to control. Also, in this study the mass spectrometry analysis of Cyp A proteinpeptide showed the highest sequence similarity with the cyclophilin protein of Salmonella. PPIases proteins enzyme data suggest that Ppi-A has roles in the protein folding that may be contributing to the virulence of Salmonella by isomerization of protein outline. These results suggest an active and vital role of this protein in protein folding along with regulation in Salmonella Typhimurium.

Salmonella Typhimurium (ST) is the zoonotic pathogenic Gram-negative bacteria to causes infectious disease in humans as well as in animals. It causes gastrointestinal illness and fever called salmonellosis, which is foodborne diarrheal and leading cause of millions of deaths worldwide. Salmonella enterica serovar Typhimurium (S. Typhimurium) during its pathogenesis takeaway the actin cytoskeleton of their host cells and this is the crucial step of its infection cycle. Cyclophilin A, a type of peptidyl-prolyl isomerase that’s encoded by the ppiA gene in ST, plays pleiotropic roles in maintaining bacterial physiology. In this research, the proteomic characterization of the peptidyl-prolyl cis-trans isomerase- A (Cyclophilin A) from Salmonella Typhimurium is reported. Cyclophilin A (CypA) protein from Salmonella Typhimurium proved to be a highly conserved protein sequence and highly homologous compared to other organisms. This protein was expressed in Escherichia coli and then purified in a recombinant form protein exhibited a characteristic PPIases activity (Vmax = 0.8752 ± 0.13892 µmoles/ min, Km = 0.9315 ± 0.5670 µM) in comparison to control. Also, in this study the mass spectrometry analysis of Cyp A protein-peptide showed the highest sequence similarity with the cyclophilin protein of Salmonella. PPIases proteins enzyme data suggest that Ppi-A has roles in the protein folding that may be contributing to the virulence of Salmonella by isomerization of protein outline. These results suggest an active and vital role of this protein in protein folding along with regulation in Salmonella Typhimurium.