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Journal of Bacteriology, March 2006, p. 1744-1749, Vol. 188, No. 5
0021-9193/06/$08.00+0     doi:10.1128/JB.188.5.1744-1749.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

A Hydrophobic Patch in the Competence-Stimulating Peptide, a Pneumococcal Competence Pheromone, Is Essential for Specificity and Biological Activity

Ola Johnsborg,1 Per Eugen Kristiansen,2 Trinelise Blomqvist,1 and Leiv Sigve Håvarstein1*

Department of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences, Ås,1 Department of Molecular Biosciences, University of Oslo, Oslo, Norway2

Received 14 September 2005/ Accepted 31 October 2005

Induction of competence for natural genetic transformation in Streptococcus pneumoniae depends on pheromone-mediated cell-cell communication and a signaling pathway consisting of the competence-stimulating peptide (CSP), its membrane-embedded histidine kinase receptor ComD, and the cognate response regulator ComE. Extensive screening of pneumococcal isolates has revealed that two major CSP variants, CSP1 and CSP2, are found in members of this species. Even though the primary structures of CSP1 and CSP2 are about 50% identical, they are highly specific for their respective receptors, ComD1 and ComD2. In the present work, we have investigated the structural basis of this specificity by determining the three-dimensional structure of CSP1 from nuclear magnetic resonance data and comparing the agonist activity of a number of CSP1/CSP2 hybrid peptides toward the ComD1 and ComD2 receptors. Our results show that upon exposure to membrane-mimicking environments, the 17-amino-acid CSP1 pheromone adopts an amphiphilic {alpha}-helical configuration stretching from residue 6 to residue 12. Furthermore, the pattern of agonist activity displayed by the various hybrid peptides revealed that hydrophobic amino acids, some of which are situated on the nonpolar side of the {alpha}-helix, strongly contribute to CSP specificity. Together, these data indicate that the identified {alpha}-helix is an important structural feature of CSP1 which is essential for effective receptor recognition under natural conditions.

* Corresponding author. Mailing address: Department of Chemistry, Biotechnology, and Food Science, Biotechnology Building, Norwegian University of Life Sciences, P.O. Box 5003, N-1432 Ås, Norway. Phone: (47) 64965883. Fax: (47) 64965901. E-mail: sigve.havarstein{at}umb.no.

Journal of Bacteriology, March 2006, p. 1744-1749, Vol. 188, No. 5
0021-9193/06/$08.00+0     doi:10.1128/JB.188.5.1744-1749.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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