Protein Localisation In Some Selected Pathogens: A Panacea for Potential Drug Development
DOI:
https://doi.org/10.63561/jhssr.v3i1.1142Keywords:
Protein, Molecular, Weight, Drugs, Bio-InformaticsAbstract
Protein localization in pathogens gives information about the virulence of the pathogens. This research is aimed at Z localization of microbial proteins of some selected pathogens using bioinformatics tools. Some isolated soil microbes were identified using conventional methods and 16s ribosomal RNA sequencing. These isolates were found to be homologous Pseudomonas aeruginosa, Bacillus subtilis, Serratia marcescens and Bacillus sphaericus (bacterial isolates) while Aspergillus terreus, Candidia tropicalis, Penicillium ruben, Yarrowia lipolytica and Metarrhizium anisopliae. SDS-PAGE was used to separate the proteins according to molecular weight. A. terreus and P. ruben expressed proteins homologous to typsin inhibitor molecular weight range. P. ruben and B. sphaericus expressed glycoprotein of 30kda. P. ruben and B. subtilis showed protein band homologues to the molecular weight of ribosomal protein S6 (32Kda). P. ruben, M. anisophiliae, Y. lipolytica, B. subtilis, B. sphaericus expressed spheroplast 40kda, peroxisomal thiolase 42kda, carbonic anhydrase 34.17 kda, ovalbumin 47.05kda and glutathione transferase 110kda respectively. All the isolates expresses cytochrome p450 116kda. Using bio-informatics tools, Candida tropicalis, Penicillium rubens, Yarrowia lipolytica and Metarrhizium anisopliae all expresses wall anchor proteins. Aspergillus terreus, Bacillus sphaericus and Serratia marcescens expresses integral membrane protein that spanned across the transmembrane helix, hence they are neither exported nor cytoplasmic protein. Bacillus substilis and Pseudomonas aeruginosa were both predicted to be exported proteins. The location of the various proteins could be related to the survival and virulence of the pathogens. Hence the knowledge of the protein nature could aid in the development of drugs to targets this localized proteins.
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