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Infection and Immunity, October 2002, p. 5706-5714, Vol. 70, No. 10
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.10.5706-5714.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Divergently Transcribed Streptococcus parasanguis Virulence-Associated fimA Operon Encoding an Mn2+-Responsive Metal Transporter and pepO Encoding a Zinc Metallopeptidase Are Not Coordinately Regulated

Joyce Oetjen, Paula Fives-Taylor,* and Eunice H. Froeliger

Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, Vermont 05405

Received 13 February 2002/ Returned for modification 28 May 2002/ Accepted 22 July 2002

The study of how bacteria respond to and obtain divalent metal ions provides insight into the regulation of virulence factors in the host environment. Regulation of metal permease operons in gram-positive bacteria may involve the binding of metal-responsive repressors to palindromic domains in their control regions. The Streptococcus parasanguis fimA operon, which encodes an ATP-binding cassette (ABC) transporter system with sequence homology to the LraI family of metal transporters, possesses a palindromic regulatory region with high homology to that of the Streptococcus gordonii ScaR binding domain. Mapping of the promoter and regulatory regions of fimA and the divergently transcribed pepO gene, which encodes a zinc metalloendopeptidase, indicated that their promoter and regulatory elements overlap. fimA had one transcriptional start site, whereas pepO had three. Analysis of truncated versions of the pepO promoter suggested that all three transcriptional start sites are functional. Analysis of promoter activity under various environmental conditions indicated that the fimA operon promoter and the pepO promoter are not coordinately regulated. The fimA operon is responsive to changes in Mn2+ concentration, but the pepO promoter is not. A S. parasanguis fimA mutant showed a growth deficiency under conditions of limiting Mn2+. This deficiency was not alleviated by compensation with either Mg2+ or Fe3+. Wild-type S. parasanguis could take up Mn2+ and Fe3+, while the fimA mutant showed a marked reduction in this ability. These data suggested that FimA is a component of a metal transporter system capable of transporting both Mn2+ and Fe3+. FimA expression itself was shown to be responsive to Mn2+ concentration, but not to availability of Fe3+ or Mg2+.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, University of Vermont, 116 Stafford Hall, Burlington, VT 05405. Phone: (802) 656-1121. Fax: (802) 656-8749. E-mail: pfivesta{at}zoo.uvm.edu.

Editor: E. I. Tuomanen

Infection and Immunity, October 2002, p. 5706-5714, Vol. 70, No. 10
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.10.5706-5714.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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