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Characterization of Bacillus anthracis proteases through protein-protein interaction: an in silico study of anthrax pathogenicity
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  • Journal title : TANG [HUMANITAS MEDICINE]
  • Volume 4, Issue 1,  2014, pp.6.1-6.12
  • Publisher : Association of Humanitas Medicine
  • DOI : 10.5667/tang.2013.0031
 Title & Authors
Characterization of Bacillus anthracis proteases through protein-protein interaction: an in silico study of anthrax pathogenicity
Banerjee, Amrita; Pal, Shilpee; Paul, Tanmay; Mondal, Keshab Chandra; Pati, Bikash Ranjan; Sen, Arnab; Mohapatra, Pradeep Kumar Das;
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Anthrax is the deadly disease for human being caused by Bacillus anthracis. Instantaneous research work on the mode of infection of the organism revealed that different proteases are involved in different steps of pathogenesis. Present study reports the in silico characterization and the detection of pathogenic proteases involved in anthrax infection through protein-protein interaction. A total of 13 acid, 9 neutral, and 1 alkaline protease of Bacillus anthracis were selected for analysing the physicochemical parameter, the protein superfamily and family search, multiple sequence alignment, phylogenetic tree construction, protein-protein interactions and motif finding. Among the 13 acid proteases, 10 were found as extracellular enzymes that interact with immune inhibitor A (InhA) and help the organism to cross the blood brain barrier during the process of infection. Multiple sequence alignment of above acid proteases revealed the position 368, 489, and 498-contained 100% conserved amino acids which could be used to deactivate the protease. Among the groups analyzed, only acid protease were found to interact with InhA, which indicated that metalloproteases of acid protease group have the capability to develop pathogenesis during B. anthracis infection. Deactivation of conserved amino acid position of germination protease can stop the sporulation and germination of B anthracis cell. The detailed interaction study of neutral and alkaline proteases could also be helpful to design the interaction network for the better understanding of anthrax disease.
Anthrax;Bacillus anthracis;protease;superfamily and family;phylogenetic tree;motif;protein-protein interaction;
 Cited by
Baillie L. The development of new vaccines against Bacillus anthracis. J Appl Microbiol. 2001;91:609-613. crossref(new window)

Banerjee A, Jana A, Pati BR, Mondal KC, Das Mohapatra PK. Characterization of tannase protein sequences of bacteria and fungi: an in silico study. Protein J. 2012;31:306-327. crossref(new window)

Chertow JH. Bacillus anthracis protease regulates bacterial adhesion. ProQuest Dissertations and Theses of George Mason University. 2011.

Dubey AK, Yadav S, Kumar M, Singh VK, Sarangi BK, Yadav D. In silico characterization of pectate lyase protein sequences from different source organisms. Enzyme Res. 2010;2010:1-11.

Guruprasad K, Reddy BVB, Pandit MW. Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Eng. 1990;4:155-161. crossref(new window)

Huson DH, Richter DC, Rausch C, Dezulian T, Franz M, Rupp R. Dendroscope: An interactive viewer for large phylogenetic trees. BMC Bioinform. 2007;8:460-464. crossref(new window)

John WE, Teresa GA. Serum protease cleavage of Bacillus anthracis protective antigen. J Biol Chem. 2010;285:8130-8137. crossref(new window)

Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982;157:105-132. crossref(new window)

Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, William HM, Valentin F, Wallace IM, Wilm A, Lopez R, Thompson JD, Gibson TJ, Higgins DG. Clustal W and clustal X version 2.0. Bioinformatics. 2007;23:2947-2948. crossref(new window)

Morya VK, Yadav S, Kim EK, Yadav D. In silico characterization of alkaline proteases from different species of Aspergillus. Appl Biochem Biotechnol. 2012;166:243-257. crossref(new window)

Mukherjee DV, Tonry JH, Kim KS, Ramarao N, Popova TG, Bailey C, Mail SP, Chung MC. Bacillus anthracis protease inha increases blood-brain barrier permeability and contributes to cerebral hemorrhages. PLoS ONE. 2011;6:1-11.

Pflughoeft KJ. The Immune Inhibitor A1 Protease of Bacillus anthracis. Dissertations and theses of graduate School of Biomedical Sciences in the University of Texas. 2010.

Pflughoeft KJ, Swick MC, Engler DA, Yeo HJ, Koehler TM. Modulation of the Bacillus anthracis secretome by the immune inhibitor a1 protease. J Bacteriol. 2014;196:424-435. crossref(new window)

Pomerantsev AP, Pomerantseva OM, Moayeri M, Fattah R, Tallant C, Leppla SH. A Bacillus anthracis strain deleted for six proteases serves as an effective host for production of recombinant proteins. Protein Expr Purif. 2011;80:80-90. crossref(new window)

Rogers S, Wells R, Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science.1986;234:364-368. crossref(new window)

Russell BH, Vasan R, Keene DR, Xu Y. Bacillus anthracis internalization by human fibroblasts and epithelial cells. Cell Microbiol. 2007;9:1262-1274. crossref(new window)

Sheppard MR, Vinay K, Abbas AK, Nelson F. Robbins Basic Pathology. 8th ed. (Philadelphia, USA: Saunders), pp. 1-122, 2007.

Shrivastava S, Shukla P, Poddar R. In silico studies for evaluating conservation homology among family 11 xylanases from Thermomyces lanuginosus. JASES. 2007;2:70-76.

Tonry JH, McNichol BA, Ramarao N, Chertow DS, Kim KS, Stibitz S, Schneewind O, Kashanchi F, Bailey CL, Popov S, Chung MC. Bacillus anthracis protease InhA regulates BslA-mediated adhesion in human endothelial cells. Cell Microbiol. 2012;14:1219-1230. crossref(new window)

Tuimala J. A primer to phylogenetic analysis using the PHYLIP package. Cladistics. 1989; 5:164-166.