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Infection and Immunity, December 1999, p. 6688-6690, Vol. 67, No. 12
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

A Lithium Chloride-Extracted, Broad-Spectrum-Adhesive 42-Kilodalton Protein of Staphylococcus epidermidis Is Ornithine Carbamoyltransferase

Muzaffar Hussain,1 Georg Peters,1 Gursharan S. Chhatwal,2 and Mathias Herrmann1,*

Institute of Medical Microbiology, University Hospital of Münster, Münster,1 and Department of Microbial Pathogenesis, Gesellschaft für Biotechnologische Forschung, Braunschweig,2 Germany

Received 24 May 1999/Returned for modification 22 July 1999/Accepted 14 September 1999

To identify novel putative staphylococcal adhesins, lithium chloride extraction (an established method for selective surface molecule solubilization) was employed. N-terminal sequencing and functional assays identified a 42-kDa fibronectin-binding protein from Staphylococcus epidermidis as ornithine carbamoyltransferase (OCTase). However, OCTase was not recognizable extracellularly, and this fact together with the fact that LiCl induced DNA release and a decrease in viability suggests that LiCl extraction may not be the method of choice for selective surface molecule extraction from staphylococci.

* Corresponding author. Mailing address: Institute of Medical Microbiology, University Hospital, Domagkstr. 10, 48129 Münster, Germany. Phone: 49-251-835 5357. Fax: 49-251-835 5350. E-mail: mathias.herrmann{at}uni-muenster.de.

Infection and Immunity, December 1999, p. 6688-6690, Vol. 67, No. 12
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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