title: Growth inhibition of Mycobacterium smegmatis by mycobacteriophage-derived enzymes.
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.
authors.affiliation: 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.
authors.forename: Navdeep
authors.initials: N
authors.lastname: Grover
authors.affiliation: 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.
authors.forename: Elena E
authors.initials: EE
authors.lastname: Paskaleva
authors.affiliation: 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.
authors.forename: Krunal K
authors.initials: KK
authors.lastname: Mehta
authors.affiliation: 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.
authors.forename: Jonathan S
authors.initials: JS
authors.lastname: Dordick
authors.affiliation: 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.
authors.forename: Ravi S
authors.initials: RS
authors.lastname: Kane
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000494:pharmacology; D001435:Bacteriophages / Q000201:enzymology*; D002473:Cell Wall / Q000187:drug effects; D004305:Dose-Response Relationship, Drug; D004357:Drug Synergism; D010450:Endopeptidases / Q000494:pharmacology*; D004950:Esterases / Q000494:pharmacology*; D005685:Galactans / Q000378:metabolism; D006868:Hydrolysis; D008969:Molecular Sequence Data; D020102:Mycobacterium smegmatis / Q000187:drug effects* / Q000254:growth & development; D011994:Recombinant Proteins / Q000494:pharmacology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013501:Surface-Active Agents / Q000494:pharmacology
chemical_list: D001426:Bacterial Proteins; D005685:Galactans; D011994:Recombinant Proteins; D013501:Surface-Active Agents; C549865:mycolylarabinogalactan; D004950:Esterases; D010450:Endopeptidases; C001143:endolysin
keywords: Bactericidal; LysB; Mycobacteriophage; Mycobacterium smegmatis; Phage derived lysins; Tuberculosis