The population of catfish,
Clarias batrachus
has substantially diminished in various countries and studies show that another related species
Clarias gariepinus
is replacing it. The better adaptability and survivability of
C. gariepinus
over
C. batrachus
could be attributed to the metabolic differences between these two species, which is primarily regulated by mitochondrial activities. To understand the reasons behind this phenomenon, we performed
in silico
analyses to decipher the differences between the proteins encoded by the mitochondrial genome of these two related species. Our analysis revealed that out of thirteen, twelve proteins encoded by the mitochondrial genome of these two species have substantial variations between them. We characterised these variations by analysing their effect on secondary structure, intrinsic disorder predisposition, and functional impact on protein and stability parameters. Our data show that most of the parameters are changing between these two closely related species. Altogether, we demonstrate the molecular insights into the mitochondrial genome-encoded proteins of these two species and predict their effect on protein function and stability that might be helping
C. gariepinus
to gain survivability better than the
C. batrachus
.
The SARS-CoV-2 is rapidly evolving and new mutations are being reported from different parts of the world. In this study, we investigated the variations occurring in the nucleocapsid phosphoprotein (N-protein) of SARS-CoV-2 from India. We used several in silico prediction tools to characterise N-protein including IEDB webserver for B cell epitope prediction, Vaxijen 2.0 and AllergenFP v.1.0 for antigenicity and allergenicity prediction of epitopes, CLUSTAL Omega for mutation identification and PONDR webserver for disorder prediction, PROVEAN score for protein function and iMutantsuite for protein stability prediction. Our results show that 81 mutations have occurred in this protein among Indian SARS-CoV-2 isolates. Subsequently, we characterized the N-protein epitopes to identify seven most promising peptides. We mapped these mutations with seven N-protein epitopes to identify the loss of antigenicity in two of them, suggesting that the mutations occurring in the SARS-CoV-2 genome contribute to the alteration in the properties of epitopes. Altogether, our data strongly indicates that N-protein is gaining several mutations in its B cell epitope regions that might alter protein function.
The on-going coronavirus disease-19 (COVID-19) pandemic caused by SARS-CoV-2 has infected hundreds of millions of people and killed more than two million people worldwide. Currently, there are no effective drugs available for treating SARS-CoV-2 infections; however, vaccines are now being administered worldwide to control this virus. In this study, we have studied SARS-CoV-2 helicase, Nsp13, which is critical for viral replication. We compared the Nsp13 sequences reported from India with the first reported sequence from Wuhan province, China to identify and characterize the mutations occurring in this protein. To correlate the functional impact of these mutations, we characterised the most prominent B cell and T cell epitopes contributed by Nsp13. Our data revealed twenty-one epitopes, which exhibited high antigenicity, stability and interactions with MHC class-I and class-II molecules. Subsequently, the physiochemical properties of these epitopes were also analysed. Furthermore, several of these Nsp13 epitopes harbour mutations, which were further characterised by secondary structure and per-residue disorderness, stability and dynamicity predictions. Altogether, we report the candidate epitopes of Nsp13 that may help the scientific community to understand the evolution of SARS-CoV-2 variants and their probable implications.
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