STUDY OF FEATURES OF THE EFFECT OF CATIONIC ANTIMICROBIAL PEPTIDE NISIN ON LISTERIA MONOCYTOGENES BACTERIA BY USING ATOMIC-FORCE MICROSCOPY
- Authors: Valyshev A.V1, Vasilchenko A.S1
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Affiliations:
- Research Institute of Cellular and Intracellular Symbiosis, Orenburg, Russia
- Issue: Vol 90, No 5 (2013)
- Pages: 8-13
- Section: Articles
- Submitted: 09.06.2023
- Published: 15.10.2013
- URL: https://microbiol.crie.ru/jour/article/view/13826
- ID: 13826
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Abstract
Aim. Characteristic of morpho-functional reaction of Listeria monocytogenes bacterial cells to the effect of cationic peptide nisin. Materials and methods. Culture of L. monocytogenes 88-BK bacterial cells was grown in the presence of nisin (experiment) and without it (control). The samples obtained were studied by atomic-force microscopy method in contact mode by using scanning probe of SMM-2000 microscope. Study of elastic properties of bacterial cells was carried out by using AFM in force spectroscopy mode. Results. Microorganisms grown in the presence of sub-inhibitory concentrations of antibiotic were characterized by changes in cell morphology and mechanical properties that were recorded by using AFM as changes in size parameters of bacteria, visualized local lesions of surface with the increase of its roughness as well as decrease of mechanical durability of the cell wall. Conclusion. Use of atomic-force microscopy allows to detail mechanisms of biological activity of cationic peptide nisin on gram-positive bacteria, evaluate specter of changes of cell morphological and mechanical parameters that took place and were analyzed in the conditions close to native.
About the authors
A. V Valyshev
Research Institute of Cellular and Intracellular Symbiosis, Orenburg, Russia
A. S Vasilchenko
Research Institute of Cellular and Intracellular Symbiosis, Orenburg, Russia
References
- Bolshakova A.V., Kiselyova O.I., Filonov A.S. et al. Comparative studies of bacteria with an atomic force microscopy operating in different modes. Ultramicroscopy. 2001, 86 (1-2): 121-128.
- Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 2005, 3 (3): 238-250.
- Cheigh C.I., Pyun YR. Nisin biosynthesis and its properties. Biotechnol. Lett. 2005, 27 (21): 16411648.
- Dorobantu L.S., Gray M.R. Application of atomic force microscopy in bacterial research. Scanning. 2010, 32 (2): 74-96.
- Hancock R.E., Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 1998, 16 (2): 82-88.
- Hasper H.E., Kramer N.E., Smith J.L. et al. An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science. 2006, 313 (5793): 1636-1637.
- Hertz H. Uber die Beruhrung fester elastischer Koroper (On the contact of elastic solids). Journal fur die reine und angewandte Mathematik. 1881, 92: 156-171.
- Hurst A. Nisin. Adv. Appl. Microbiol. 1981, 27: 85-123.
- Jenssen H., Hamill P., Hancock R.E. Peptide antimicrobial agents. Clin. Microbiol. Rev. 2006, 19 (3): 491-511.
- Kaur G., Malik R.K., Mishra S.K. et al. Nisin and class IIa bacteriocin resistance among Listeria and other foodborne pathogens and spoilage bacteria. Microb. Drug. Resist. 2011, 17 (2): 197205.
- Mangoni M.L., Papo N., Barra D. et al. Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli. Biochem. J. 2004, 380 (Pt 3): 859-865.
- Meincken M., Holroyd D.L., Rautenbach M. Atomic force microscopy study of the effect of antimicrobial peptides on the cell envelope of Escherichia coli. Antimicrob. Agents Chemother. 2005, 49 (10): 4085-4092.
- Tong Z., Zhou L., Li J. et al. In vitro evaluation of the antibacterial activities of MTAD in combination with nisin against Enterococcus faecalis. J. Endod. 2011, 37 (8): 1116-1120.
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