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Infect Immun, August 1998, p. 3767-3774, Vol. 66, No. 8
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Molecular Cloning of a 32-Kilodalton Lipoprotein Component of a Novel Iron-Regulated Staphylococcus epidermidis ABC Transporter

Alan Cockayne,1 2 3 * Philip J. Hill,1 2 3 dagger Nick B. L. Powell,1 2 Keith Bishop,1 2 Cate Sims,1 3 and Paul Williams1 2 3

Institute of Infections and Immunity,1 School of Clinical Laboratory Sciences,2 and School of Pharmaceutical Sciences,3 University of Nottingham, Nottingham NG7 2UH, United Kingdom

Received 11 February 1998/Returned for modification 7 March 1998/Accepted 4 May 1998

Our previous studies identified two iron-regulated cytoplasmic membrane proteins of 32 and 36 kDa expressed by both Staphylococcus epidermidis and Staphylococcus aureus. In this study we show by Triton X-114 phase partitioning and tritiated palmitic acid labelling that these proteins are lipoproteins which are anchored into the cytoplasmic membrane by their lipid-modified N termini. In common with those of some other gram-positive bacteria, these highly immunogenic lipoproteins were released from the bacterial cell into the culture supernatants, with release being promoted by growth of the bacteria under iron-restricted conditions. Immunoelectron microscopy with a monospecific rabbit antiserum to the 32-kDa S. epidermidis lipoprotein showed that the majority of the antigen was distributed throughout the staphylococcal cell wall. Only minor quantities were detected in the cytoplasmic membrane, and exposure of the lipoprotein on the bacterial surface was minimal. A monoclonal antibody raised to the 32-kDa lipoprotein of S. aureus was used in immunoblotting studies to investigate the conservation of this antigen among a variety of staphylococci. The monoclonal antibody reacted with polypeptides of 32 kDa in S. epidermidis and S. aureus and of 40 kDa in Staphylococcus hominis. No reactivity was detected with Staphylococcus lugdunensis, Staphylococcus cohni, or Staphylococcus haemolyticus. The gene encoding the 32-kDa lipoprotein from S. epidermidis has been isolated from a Lambda Zap II genomic DNA library and found to be a component of an iron-regulated operon encoding a novel ABC-type transporter. The operon contains three genes, designated sitA, -B, and -C, encoding an ATPase, a cytoplasmic membrane protein, and the 32-kDa lipoprotein, respectively. SitC shows significant homology both with a number of bacterial adhesins, including FimA of Streptococcus parasanguis and ScaA of Streptococcus gordonii, and with lipoproteins of a recently described family of ABC transporters with proven or putative metal ion transport functions. Although the solute specificity of this novel transporter has not yet been determined, we speculate that it may be involved in either siderophore- or transferrin-mediated iron uptake in S. epidermidis.

* Corresponding author. Mailing address: Institute of Infections and Immunity, University Hospital, Queen's Medical Centre, Nottingham NG7 2UH, United Kingdom. Phone: 0115 9249924, ext. 42445. Fax: 0115 970 9923. E-mail: mrzac{at}mrn1.nottingham.ac.uk.

dagger Present address: Department of Applied Biochemistry and Food Science, School of Biology, Sutton Bonington Campus, University of Nottingham, Leicestershire LE12 5RD, United Kingdom.

Infect Immun, August 1998, p. 3767-3774, Vol. 66, No. 8
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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