Staff View: New insights into the mode of action of the lantibiotic salivaricin B

New insights into the mode of action of the lantibiotic salivaricin B

Salivaricin B is a 25 amino acid polycyclic peptide belonging to the type AII lantibiotics and first shown to be produced by Streptococcus salivarius. In this study we describe the bactericidal mode of action of salivaricin B against susceptible Gram-positive bacteria. The killing action of salivari...

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Main Authors:	Barbour, A., Tagg, J., Abou-Zied, O.K., Philip, K.
Format:	Article
Published:	Nature Publishing Group 2016
Subjects:	Q Science (General) QH Natural history
Online Access:	http://eprints.um.edu.my/18465/ https://doi.org/10.1038/srep31749
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id	my.um.eprints.18465
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spelling	my.um.eprints.184652017-12-07T02:11:48Z http://eprints.um.edu.my/18465/ New insights into the mode of action of the lantibiotic salivaricin B Barbour, A. Tagg, J. Abou-Zied, O.K. Philip, K. Q Science (General) QH Natural history Salivaricin B is a 25 amino acid polycyclic peptide belonging to the type AII lantibiotics and first shown to be produced by Streptococcus salivarius. In this study we describe the bactericidal mode of action of salivaricin B against susceptible Gram-positive bacteria. The killing action of salivaricin B required micro-molar concentrations of lantibiotic whereas the prototype lantibiotic nisin A was shown to be potent at nano-molar levels. Unlike nisin A, salivaricin B did not induce pore formation or dissipate the membrane potential in susceptible cells. This was established by measuring the fluorescence of the tryptophan residue at position 17 when salivaricin B interacted with bacterial membrane vesicles. The absence of a fluorescence blue shift indicates a failure of salivaricin B to penetrate the membranes. On the other hand, salivaricin B interfered with cell wall biosynthesis, as shown by the accumulation of the final soluble cell wall precursor UDP-MurNAc-pentapeptide which is the backbone of the bacterial peptidoglycan. Transmission electron microscopy of salivaricin B-treated cells showed a reduction in cell wall thickness together with signs of aberrant septum formation in the absence of visible changes to cytoplasmic membrane integrity. Nature Publishing Group 2016 Article PeerReviewed Barbour, A. and Tagg, J. and Abou-Zied, O.K. and Philip, K. (2016) New insights into the mode of action of the lantibiotic salivaricin B. Scientific Reports, 6. p. 31749. ISSN 2045-2322 https://doi.org/10.1038/srep31749 doi:10.1038/srep31749
institution	Universiti Malaya
building	UM Library
collection	Institutional Repository
continent	Asia
country	Malaysia
content_provider	Universiti Malaya
content_source	UM Research Repository
url_provider	http://eprints.um.edu.my/
topic	Q Science (General) QH Natural history
spellingShingle	Q Science (General) QH Natural history Barbour, A. Tagg, J. Abou-Zied, O.K. Philip, K. New insights into the mode of action of the lantibiotic salivaricin B
description	Salivaricin B is a 25 amino acid polycyclic peptide belonging to the type AII lantibiotics and first shown to be produced by Streptococcus salivarius. In this study we describe the bactericidal mode of action of salivaricin B against susceptible Gram-positive bacteria. The killing action of salivaricin B required micro-molar concentrations of lantibiotic whereas the prototype lantibiotic nisin A was shown to be potent at nano-molar levels. Unlike nisin A, salivaricin B did not induce pore formation or dissipate the membrane potential in susceptible cells. This was established by measuring the fluorescence of the tryptophan residue at position 17 when salivaricin B interacted with bacterial membrane vesicles. The absence of a fluorescence blue shift indicates a failure of salivaricin B to penetrate the membranes. On the other hand, salivaricin B interfered with cell wall biosynthesis, as shown by the accumulation of the final soluble cell wall precursor UDP-MurNAc-pentapeptide which is the backbone of the bacterial peptidoglycan. Transmission electron microscopy of salivaricin B-treated cells showed a reduction in cell wall thickness together with signs of aberrant septum formation in the absence of visible changes to cytoplasmic membrane integrity.
format	Article
author	Barbour, A. Tagg, J. Abou-Zied, O.K. Philip, K.
author_facet	Barbour, A. Tagg, J. Abou-Zied, O.K. Philip, K.
author_sort	Barbour, A.
title	New insights into the mode of action of the lantibiotic salivaricin B
title_short	New insights into the mode of action of the lantibiotic salivaricin B
title_full	New insights into the mode of action of the lantibiotic salivaricin B
title_fullStr	New insights into the mode of action of the lantibiotic salivaricin B
title_full_unstemmed	New insights into the mode of action of the lantibiotic salivaricin B
title_sort	new insights into the mode of action of the lantibiotic salivaricin b
publisher	Nature Publishing Group
publishDate	2016
url	http://eprints.um.edu.my/18465/ https://doi.org/10.1038/srep31749
_version_	1643690712862031872
score	13.211869

New insights into the mode of action of the lantibiotic salivaricin B

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