Skip to main content
SpringerLink
Log in

Sequence Analysis and Comparative Bioinformatics Study of Camelysin Gene (calY) Isolated from Bacillus thuringiensis

  • Original Article
  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

Bacillus strains have been widely used for the production of fibrinolytic enzymes having role in the treatment of cardiovascular disorders. Purification and overproduction of such enzymes has increased their usage in medical fields including metalloproteinases with the ability to degrade extracellular matrix (ECM). Camelysin, a neutral metalloproteinase has been isolated from different species of bacteria like Bacillus cereus, Bacillus anthracis, and Bacillus thuringiensis with fibrinolytic, collagenolytic and actin degradation activity. This project successfully demonstrated the presence of 734-bp coding DNA sequence (CDS) encoding a 20.72331 kDa camelysin gene in local strain of Bacillus thuringiensis containing a signal peptide with cleavage site between residues 19 and 20. The sequence was submitted to GenBank (KT023597) and the sequence showed high homology with the camelysin protein of closely related Bacillus species. The alignment of related proteins through ClustalW displayed difference of four amino acids (“Q” replaced by “P” at position 169 and at position 182–184, “NQE” replaced by “HLK”) in the isolated protein. Comparison including structural and functional analysis of camelysin sequences isolated from different Bacillus species was carried out using different bioinformatics tools and software. The information would help in better understanding the properties of camelysin protein and its role in pathogenicity and clinical treatments.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2

Similar content being viewed by others

References

  • Ageno W, Gallus AS, Wittkowsky A, Crowther M, Hylek EM, Palareti G (2012) Oral anticoagulant therapy. Antithrombotic therapy and prevention of thrombosis, 9th ed: American College of Chest Physicians Evidence-based clinical practice guidelines. Chest 141(2):e44S–e88S

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Bauer MA, Derbyshire MK, Gonzales NR, Lu S, Chitsaz F, Geer LY, Geer RC, He J, Gwadz M, Hurwitz DI, Lanczycki CJ (2014) CDD: NCBI’s conserved domain database. Nucleic Acids Res 43:D222–D226

    Article  Google Scholar 

  • Chakrabarti I (2010) A minireview: matrix metalloproteases-an invasive arm of nematode parasites. In: 22nd National Congress of Parasitology. Department of zoology, University of Kalyani, Kalyani, pp 98–101

  • Dubey R, Kumar J, Agrawala D, Char T, Pusp P (2011) Isolation, production, purification, assay and characterization of fibrinolytic enzymes (Nattokinase, Streptokinase and Urokinase) from bacterial sources. Afr J Biotech 10(8):1408–1420

    CAS  Google Scholar 

  • Fricke B, Buchmann T, Friebe S (1995) Unusual chromatographic behaviour and one-step purification of a novel membrane proteinase from Bacillus cereus. J Chromatogr A 715(2):247–258

    Article  CAS  PubMed  Google Scholar 

  • Fricke B, DroMler K, Willhardt I, Schierhorn A, Menge S, Rücknagel P (2001) The cell envelope-bound metalloprotease (camelysin) from Bacillus cereus is a possible pathogenic factor. Biochem Biophys Acta 1537(2):132–146

    CAS  PubMed  Google Scholar 

  • Ganguly K, Sharma AV, Reiter RJ, Swarnakar S (2010) Melatonin promotes angiogenesis during protection and healing of indomethacin-induced gastric ulcer: role of matrix metalloproteinase-2. J Pineal Res 49(2):130–140

    CAS  PubMed  Google Scholar 

  • Grass G, Schierhorn A, Sorkau E, Muller H, Rucknagel P, Nies DH, Fricke B (2004) Camelysin is a novel surface metalloproteinase from Bacillus cereus. J Infect Immun 72(1):219–228

    Article  CAS  Google Scholar 

  • Hadler-Olsen E, Winberg JO, Uhlin-Hansen L (2013) Matrix metalloproteinases in cancer: their value as diagnostic and prognostic markers and therapeutic targets. Tumor Biol 34(4):2041–2051

    Article  CAS  Google Scholar 

  • Kotb E (2013) Activity assessment of microbial fibrinolytic enzymes. Appl Microbiol Biotechnol 97(15):6647–6665

    Article  CAS  PubMed  Google Scholar 

  • Mushtaq Z, Jamil A (2012) Isolation of a fibrinolytic enzyme BKII gene from local isolate of Bacillus. J Chem Biochem Sci 2:94–100

    Google Scholar 

  • Myers AR (2005) Cloning, expression, and sequence analysis of camelysin, a zinc metalloprotease from Bacillus anthracis and B. cereus. Graduate Theses and Dissertations. University of South Florida Scholar Commons, Tampa

  • Nisnevitch M, Sigawi S, Cahan R, Nitzan Y (2010) Isolation, characterization and biological role of camelysin from Bacillus thuringiensis subsp. Israelensis. Curr Microbiol 61(3):176–183

    Article  CAS  PubMed  Google Scholar 

  • Okafor ON, Gorog DA (2015) Endogenous fibrinolysis an important mediator of thrombus formation and cardiovascular risk. J Am Coll Cardiol 65(16):1683–1699

    Article  CAS  PubMed  Google Scholar 

  • Petersen B, Petersen TN, Andersen P, Nielsen M, Lundegaard C (2009) A generic method for assignment of reliability scores applied to solvent accessibility predictions. BMC Struct Biol 9(1):51

    Article  PubMed  PubMed Central  Google Scholar 

  • Wilson K (1987) Preparation of genomic DNA from bacteria. In: Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds) Current protocols in molecular biology. John Wiley & Sons, New York, pp 2.4.1–2.4.5

    Google Scholar 

Download references

Author information

Author notes

  1. Fateha Irshad and Zahid Mushtaq contributed equally to this work.

Authors and Affiliations

  1. Bioactive Molecules Research Lab, Department of Biochemistry, University of Agriculture, Faisalabad, Pakistan

    Fateha Irshad, Zahid Mushtaq & Shakeel Akhtar

Authors
  1. Fateha Irshad
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Zahid Mushtaq
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Shakeel Akhtar
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Zahid Mushtaq.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Irshad, F., Mushtaq, Z. & Akhtar, S. Sequence Analysis and Comparative Bioinformatics Study of Camelysin Gene (calY) Isolated from Bacillus thuringiensis . Biochem Genet 56, 103–115 (2018). https://doi.org/10.1007/s10528-017-9833-6

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10528-017-9833-6

Keywords

Search

Navigation