Growth inhibition of Mycobacterium smegmatis by mycobacteriophage-derived enzymes

Navdeep Grover; Elena E Paskaleva; Krunal K Mehta; Jonathan S Dordick; Ravi S Kane

doi:10.1016/j.enzmictec.2014.04.018

Growth inhibition of Mycobacterium smegmatis by mycobacteriophage-derived enzymes

Enzyme Microb Technol. 2014 Sep:63:1-6. doi: 10.1016/j.enzmictec.2014.04.018. Epub 2014 May 9.

Authors

Navdeep Grover¹, Elena E Paskaleva¹, Krunal K Mehta¹, Jonathan S Dordick², Ravi S Kane³

Affiliations

¹ Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY, USA; Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, USA.
² Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY, USA; Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, USA; Department of Materials Science and Engineering, Rensselaer Polytechnic Institute, Troy, NY, USA; Department of Biology, Rensselaer Polytechnic Institute, Troy, NY, USA; Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY, USA. Electronic address: dordick@rpi.edu.
³ Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY, USA; Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, USA. Electronic address: kaner@rpi.edu.

PMID: 25039052
DOI: 10.1016/j.enzmictec.2014.04.018

Abstract

We report the ability of mycobacteriophage-derived endolysins to inhibit the growth of Mycobacterium smegmatis. We expressed and purified LysB from mycobacteriophage Bxz2 and compared its activity with that of a previously reported LysB from mycobacteriophage Ms6. The esterase activity of Bxz2 LysB with pNP esters was 10-fold higher than that of the previously reported LysB but its lipolytic activity was significantly lower. The presence of surfactant - Tween 80 or Triton X-100 - significantly increased the activity of LysB. Characterization of LysB-treated M. smegmatis cells and LysB-treated purified cell wall by mass spectroscopy confirmed the hydrolytic activity of the enzyme. Both enzymes were equally effective in inhibiting the growth of M. smegmatis, demonstrating their potential as bacteriostatic agents.

Keywords: Bactericidal; LysB; Mycobacteriophage; Mycobacterium smegmatis; Phage derived lysins; Tuberculosis.

Publication types

Comparative Study

MeSH terms

Amino Acid Sequence
Bacterial Proteins / pharmacology
Bacteriophages / enzymology*
Cell Wall / drug effects
Dose-Response Relationship, Drug
Drug Synergism
Endopeptidases / pharmacology*
Esterases / pharmacology*
Galactans / metabolism
Hydrolysis
Molecular Sequence Data
Mycobacterium smegmatis / drug effects*
Mycobacterium smegmatis / growth & development
Recombinant Proteins / pharmacology
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
Surface-Active Agents / pharmacology

Substances

Bacterial Proteins
Galactans
Recombinant Proteins
Surface-Active Agents
mycolylarabinogalactan
Esterases
Endopeptidases
endolysin