rdf:type |
|
lifeskim:mentions |
umls-concept:C0004611,
umls-concept:C0018154,
umls-concept:C0036536,
umls-concept:C0036537,
umls-concept:C0040715,
umls-concept:C0205245,
umls-concept:C0238953,
umls-concept:C0332307,
umls-concept:C0439185,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C1154262,
umls-concept:C1522702
|
pubmed:issue |
1
|
pubmed:dateCreated |
2001-2-22
|
pubmed:abstractText |
Type III secretion for injection of effector proteins into host cells has not been described for Gram-positive bacteria despite their importance in disease. Here, we describe an injection pathway for the Gram-positive pathogen Streptococcus pyogenes that utilizes streptolysin O (SLO), a cholesterol-dependent cytolysin. The data support a model in which an effector is translocated through the SLO pore by a polarized process. The effector, SPN (S. pyogenes NAD-glycohydrolase), is capable of producing the potent second messenger cyclic ADP-ribose, and SLO and SPN act synergistically to trigger cytotoxicity. These data provide a novel paradigm for the function of the cholesterol-dependent cytolysin family and its wide distribution suggests that cytolysin-mediated translocation (CMT) may be the equivalent of type III secretion for Gram-positive pathogens.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0092-8674
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
12
|
pubmed:volume |
104
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
143-52
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:11163247-Adenosine Diphosphate Ribose,
pubmed-meshheading:11163247-Bacterial Adhesion,
pubmed-meshheading:11163247-Bacterial Proteins,
pubmed-meshheading:11163247-Biological Transport,
pubmed-meshheading:11163247-Cell Line,
pubmed-meshheading:11163247-Cell Membrane,
pubmed-meshheading:11163247-Cyclic ADP-Ribose,
pubmed-meshheading:11163247-Cytoplasm,
pubmed-meshheading:11163247-Cytotoxins,
pubmed-meshheading:11163247-Humans,
pubmed-meshheading:11163247-Keratinocytes,
pubmed-meshheading:11163247-NAD+ Nucleosidase,
pubmed-meshheading:11163247-Protein Sorting Signals,
pubmed-meshheading:11163247-Second Messenger Systems,
pubmed-meshheading:11163247-Streptococcus pyogenes,
pubmed-meshheading:11163247-Streptolysins,
pubmed-meshheading:11163247-Virulence
|
pubmed:year |
2001
|
pubmed:articleTitle |
Cytolysin-mediated translocation (CMT): a functional equivalent of type III secretion in gram-positive bacteria.
|
pubmed:affiliation |
Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|