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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adhesins, Bacterial / isolation & purification
-
Amino Acid Sequence
-
Bacterial Proteins / isolation & purification
-
Bacteriological Techniques
-
Blotting, Western
-
Carrier Proteins / isolation & purification
-
Catheters, Indwelling / microbiology
-
Coagulase / metabolism
-
Humans
-
Lithium Chloride
-
Molecular Sequence Data
-
Ornithine Carbamoyltransferase / chemistry*
-
Ornithine Carbamoyltransferase / isolation & purification*
-
Staphylococcal Infections / microbiology*
-
Staphylococcus epidermidis / enzymology*
-
Staphylococcus epidermidis / isolation & purification
Substances
-
Adhesins, Bacterial
-
Bacterial Proteins
-
Carrier Proteins
-
Coagulase
-
fibronectin-binding proteins, bacterial
-
Ornithine Carbamoyltransferase
-
Lithium Chloride