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Applied and Environmental Microbiology, November 2005, p. 6501-6507, Vol. 71, No. 11
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.11.6501-6507.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Isolation and Partial Characterization of Antagonistic Peptides Produced by Paenibacillus sp. Strain B2 Isolated from the Sorghum Mycorrhizosphere

S. Selim,1 J. Negrel,1 C. Govaerts,2 S. Gianinazzi,1 and D. van Tuinen1*

UMR INRA 1088/CNRS 5184/Université de Bourgogne, Plante-Microbe-Environnement CMSE-INRA, 17 rue Sully, BP 86510, 21065 Dijon Cedex, France,1 Katholieke Universiteit Leuven, Faculteit Farmaceutische Wetenschappen, Laboratorium voor Farmaceutische Chemie en Analyse van Geneesmiddelen, Van Evenstraat 4, B-3000 Leuven, Belgium2

Received 1 December 2004/ Accepted 6 June 2005

Paenibacillus sp. strain B2, isolated from the mycorrhizosphere of sorghum colonized by Glomus mosseae, produces an antagonistic factor. This factor has a broad spectrum of activity against gram-positive and gram-negative bacteria and also against fungi. The antagonistic factor was isolated from the bacterial culture medium and purified by cation-exchange, reverse-phase, and size exclusion chromatography. The purified factor could be separated into three active compounds following characterization by amino acid analysis and by combined reverse-phase chromatography and mass spectrometry (liquid chromatography-mass spectrometry and mass spectrometry-mass spectrometry). The first compound had the same retention time as polymyxin B1, whereas the two other compounds were more hydrophobic. The molecular masses of the latter compounds are 1,184.7 and 1,202.7 Da, respectively, and their structure is similar to that of polymyxin B1, with a cyclic heptapeptide moiety attached to a tripeptide side chain and a fatty acyl residue. They both contain threonine, phenylalanine, leucine, and 2,4-diaminobutyric acid residues. The peptide with a molecular mass of 1,184.7 contains a 2,3-didehydrobutyrine residue with a molecular mass of 101 Da replacing a threonine at the A2 position of the polymyxin side chain. This modification could explain the broader range of antagonistic activity of this peptide compared to that of polymyxin B.

* Corresponding author. Mailing address: UMR INRA 1088/CNRS 5184/Université de Bourgogne, Plante-Microbe-Environnement CMSE-INRA, 17 rue Sully, BP 86510, 21065 Dijon Cedex, France. Phone: 33-3 8069 3248. Fax: 33-3 8069 3753. E-mail: tuinen{at}epoisses.inra.fr.

Applied and Environmental Microbiology, November 2005, p. 6501-6507, Vol. 71, No. 11
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.11.6501-6507.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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