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Applied and Environmental Microbiology, February 2003, p. 1051-1058, Vol. 69, No. 2
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.2.1051-1058.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Bacteriocin Detection from Whole Bacteria by Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry

Thomas Hindré, Sandrine Didelot, Jean-Paul Le Pennec, Dominique Haras, Alain Dufour,* and Karine Vallée-Réhel

Laboratoire de Biologie et Chimie Moléculaires, EA 2594, Université de Bretagne Sud, 56321 Lorient, France

Received 31 July 2002/ Accepted 4 November 2002

Class I bacteriocins (lantibiotics) and class II bacteriocins are antimicrobial peptides secreted by gram-positive bacteria. Using two lantibiotics, lacticin 481 and nisin, and the class II bacteriocin coagulin, we showed that bacteriocins can be detected without any purification from whole producer bacteria grown on plates by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS). When we compared the results of MALDI-TOF-MS performed with samples of whole cells and with samples of crude supernatants of liquid cultures, the former samples led to more efficient bacteriocin detection and required less handling. Nisin and lacticin 481 were both detected from a mixture of their producer strains, but such a mixture can yield additional signals. We used this method to determine the masses of two lacticin 481 variants, which confirmed at the peptide level the effect of mutations in the corresponding structural gene.

* Corresponding author. Mailing address: LBCM, Université de Bretagne Sud, BP 573, 56017 Vannes cedex, France. Phone: (33) 2-97-01-71-25. Fax: (33) 2-97-01-70-71. E-mail: alain.dufour{at}univ-ubs.fr.

Applied and Environmental Microbiology, February 2003, p. 1051-1058, Vol. 69, No. 2
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.2.1051-1058.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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