| pubmed-article:16547033 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16547033 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:16547033 | lifeskim:mentions | umls-concept:C0038172 | lld:lifeskim |
| pubmed-article:16547033 | lifeskim:mentions | umls-concept:C0007623 | lld:lifeskim |
| pubmed-article:16547033 | lifeskim:mentions | umls-concept:C1622204 | lld:lifeskim |
| pubmed-article:16547033 | lifeskim:mentions | umls-concept:C0030958 | lld:lifeskim |
| pubmed-article:16547033 | lifeskim:mentions | umls-concept:C0024370 | lld:lifeskim |
| pubmed-article:16547033 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:16547033 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:16547033 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:16547033 | pubmed:dateCreated | 2006-3-20 | lld:pubmed |
| pubmed-article:16547033 | pubmed:abstractText | Staphylococcus simulans bv. staphylolyticus secretes lysostaphin, a bacteriocin that cleaves pentaglycine cross bridges in the cell wall of Staphylococcus aureus. The C-terminal cell wall-targeting domain (CWT) of lysostaphin is required for selective binding of this bacteriocin to S. aureus cells; however, the molecular target for this was unknown. We used purified green fluorescent protein fused to CWT (GFP-CWT) to reveal species-specific association of the reporter with staphylococci. GFP-CWT bound S. aureus cells as well as purified peptidoglycan sacculi. The addition of cross-linked murein, disaccharides linked to interconnected wall peptides, blocked GFP-CWT binding to staphylococci, whereas murein monomers or lysostaphin-solubilized cell wall fragments did not. S. aureus strain Newman variants lacking the capacity for synthesizing polysaccharide capsule (capFO), poly-N-acetylglucosamine (icaAC), lipoprotein (lgt), cell wall-anchored proteins (srtA), or the glycolipid anchor of lipoteichoic acid (ypfP) bound GFP-CWT similar to wild-type staphylococci. A tagO mutant strain, defective in the synthesis of polyribitol wall teichoic acid attached to the cell wall envelope, displayed increased GFP-CWT binding. In contrast, a femAB mutation, reducing both the amount and the length of peptidoglycan cross-linking (monoglycine cross bridges), showed a dramatic reduction in GFP-CWT binding. Thus, the CWT domain of lysostaphin directs the bacteriocin to cross-linked peptidoglycan, which also serves as the substrate for its glycyl-glycine endopeptidase domain. | lld:pubmed |
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| pubmed-article:16547033 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16547033 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16547033 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16547033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16547033 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16547033 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:16547033 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:16547033 | pubmed:author | pubmed-author:SchneewindOla... | lld:pubmed |
| pubmed-article:16547033 | pubmed:author | pubmed-author:GründlingAnge... | lld:pubmed |
| pubmed-article:16547033 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16547033 | pubmed:volume | 188 | lld:pubmed |
| pubmed-article:16547033 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16547033 | pubmed:authorsComplete | Y | lld:pubmed |
