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Infection and Immunity, November 2002, p. 6121-6128, Vol. 70, No. 11
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.11.6121-6128.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Genetic Analysis and Functional Characterization of the Streptococcus pneumoniae vic Operon

Christian Wagner,1,{dagger} Antoine de Saizieu,1,{ddagger} Hans-Joachim Schönfeld,1 Markus Kamber,1,§ Roland Lange,1,|| Charles J. Thompson,2 and Malcolm G. Page1*

F. Hoffmann-La Roche Ltd., 4070 Basel,1 Division of Microbiology, Biozentrum, University of Basel, 4056 Basel, Switzerland2

Received 15 January 2002/ Returned for modification 21 March 2002/ Accepted 29 May 2002

The vic two-component signal transduction system of Streptococcus pneumoniae is essential for growth. The vic operon comprises three genes encoding the following: VicR, a response regulator of the OmpR family; VicK, its cognate histidine kinase; and VicX, a putative protein sharing 55% identity to the predicted product (YycJ) of an open reading frame in the Bacillus subtilis genome. We show that not only is vic essential for viability but it also influences virulence and competence. A putative transcriptional start site for the vic operon was mapped 16 bp upstream of the ATG codon of vicR. Only one transcript of 2.9 kb, encoding all three genes, was detected by Northern blot analysis. VicK, an atypical PAS domain-containing histidine kinase, can be autophosphorylated in vitro, and VicR functions in vitro as a phospho-acceptor protein. (PAS is an acronym formed from the names of the proteins in which the domains were first recognized: the Drosophila period clock protein [PER], vertebrate aryl hydrocarbon receptor nuclear translocator [ARNT], and Drosophila single-minded protein [SIM].) PAS domains are commonly involved in sensing intracellular signals such as redox potential, which suggests that the signal for vic might also originate in the cytoplasm. Growth rate, competence, and virulence were monitored in strains with mutations in the vic operon. Overexpression of the histidine kinase, VicK, resulted in decreased virulence, whereas the transformability of a null mutant decreased by 3 orders of magnitude.

* Corresponding author. Present address: Basilea Pharmaceutica Ltd., P.O. Box 3255, 4002 Basel, Switzerland. Phone: 41-61-688-3813. Fax: 41-61-688-2377. E-mail: malcolm.page{at}basileapharma.com.

Editor: E. I. Tuomanen

{dagger} Present address: Abbott Laboratories, Global Pharmaceutical R&D, Abbott Park, IL 60064-6217.

{ddagger} Present address: Roche Vitamins AG, Kaiseraugst, Switzerland.

§ Present address: Basilea Pharmaceutica Ltd., 4002 Basel, Switzerland.

|| Present address: Morphochem AG, 4058 Basel, Switzerland.

Infection and Immunity, November 2002, p. 6121-6128, Vol. 70, No. 11
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.11.6121-6128.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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