Insilico Analyses of Heat Shock Protein (HSP 70) Variation In Asian Buffaloes

Abstract

Heat shock proteins (HSPs) are a class of molecular chaperones that prevent the aggregation of non-specific proteins and assist cellular proteins in regaining their native structure to preserve cellular homeostasis. The genomic and proteomic characteristics of HSP70 from six Asian buffaloes (Murrah, Diara, Iraqi, Kalahandi, Paralakhemund, and Banni) were analyzed using the NCBI database, clustal omega database for multiple sequence alignment, SWISS modeling, and phylogenetics analysis tools. The bioinformatics analysis revealed that the HSP70 gene in buffalo is located on chromosome 2 and contains two exons linked by one intron. In silico Expasy translate tool analysis revealed that HSP70 encodes 641 amino acids with molecular weights varying between 70.28-70.43 kDa. The data revealed that Iraqi buffalo HSP70 protein has 25 amino acid residues, while diara seven variable and banni three variable amino acid were detected respectively. The study concludes that the HSP70 was successfully identified and characterized in six Asian buffaloes. The Iraqi buffaloes have a polymorphism in amino acid variables and are different in the phylogeny tree; it may correlate with the distribution of buffaloes in different climatic and geographical conditions.