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International Conference on

Recent Trends in Environmental Sustainability

ESCON22/ETERM/29
In Silico analysis of exotoxic bacterial proteases for identification of potential
therapeutic targets

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Nimra Noreen , Muhammad Idrees *, Zeenat Haq , Jehangir Khan , M. Fahad Khan
1 Department of Biosciences, University of Wah
Correspondence: idreesalvi@gmail.com
Abstract
Protease is an enzyme that can hydrolyze peptides and proteins. Proteases or peptidases are the
proteolytic enzymes which cleave the proteins into smaller fragments. Bacterial proteases play
a key role in different biological processes, life cycles of several pathogens, cell viability, stress
response and in the pathology of several syndromes like irritable bowel syndrome. Bacterial
proteases degrade many proteins involved in innate immunity which are specific in their mode
of action. Secreted bacterial proteases, for example exfoliative toxin, can also act as exotoxins
which are virulent factors and play important role in pathogenesis. Our study was aimed at
identification of potential therapeutic targets in “exotoxic bacterial proteases” for various
applications including treatment of infectious diseases and identification of new drug targets.
For this purpose, Pseudomonas aeruginosa MN1 elastase (ACC: DQ153386) with highest
enzymatic activity 82350 U/mg was selected out of 25 exotoxic bacterial proteases with the
help of literature review. Amino acid sequences (FASTA format) were retrieved from online
databases and analyzed with the help of online bioinformatic tools for phylogenetic analysis,
sequence comparisons, identification of conserved regions, motifs and domains. Several
conserved regions, functional motifs and domains including NNQKI (N=G, A, R, S), NNQKT
(N= G, A, R, S) and NIGVS (N=G, A, R, S) were identified which will be helpful for
therapeutic applications in biotechnology.

Keywords: Bacteria; Protease; Therapeutic; Motifs; Domains; Conserved

Department of Environmental Sciences, COMSATS University Islamabad, Vehari Campus

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