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

Author:

Hussain Muzaffar1,Peters Georg1,Chhatwal Gursharan S.2,Herrmann Mathias1

Affiliation:

1. Institute of Medical Microbiology, University Hospital of Münster, Münster,1 and

2. Department of Microbial Pathogenesis, Gesellschaft für Biotechnologische Forschung, Braunschweig,2Germany

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference22 articles.

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5. Characterization of Tn917 insertion mutants of Staphylococcus epidermidis affected in biofilm formation

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