|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0015264,
umls-concept:C0018270,
umls-concept:C0023861,
umls-concept:C0152060,
umls-concept:C0178719,
umls-concept:C0205154,
umls-concept:C0205314,
umls-concept:C0441712,
umls-concept:C0679622,
umls-concept:C1306235,
umls-concept:C2587213
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
2006-1-20
|
|
pubmed:abstractText |
Deciphering how Listeria monocytogenes exploits the host cell machinery to invade mammalian cells is a key issue in understanding the pathogenesis of this food-borne pathogen, which can cause diseases ranging from gastroenteritis to meningitis and abortion. In this study, we show that the lysosomal aspartyl-protease cathepsin-D (Ctsd) is of considerable importance for nonoxidative listericidal defense mechanisms. We observed enhanced susceptibility to L. monocytogenes infection of fibroblasts and bone-marrow macrophages and increased intraphagosomal viability of bacteria in fibroblasts isolated from Ctsd-deficient mice compared with wild type. These findings are further supported by prolonged survival of L. monocytogenes in Ctsd-deficient mice after infection. Transient transfection of Ctsd in wild-type cells was sufficient to revert these wild-type phagosomes back to microbicidal compartments. Based on infection experiments with mutant bacteria, in vitro degradation, and immunoprecipitation experiments, we suggest that a major target of cathepsin D is the main virulence factor listeriolysin O.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
AIM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0022-1767
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
1
|
|
pubmed:volume |
176
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1321-5
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:16424157-Animals,
pubmed-meshheading:16424157-Bacterial Toxins,
pubmed-meshheading:16424157-Cathepsin D,
pubmed-meshheading:16424157-Cells, Cultured,
pubmed-meshheading:16424157-Fibroblasts,
pubmed-meshheading:16424157-Heat-Shock Proteins,
pubmed-meshheading:16424157-Hemolysin Proteins,
pubmed-meshheading:16424157-Immunity, Innate,
pubmed-meshheading:16424157-Intracellular Fluid,
pubmed-meshheading:16424157-Listeria monocytogenes,
pubmed-meshheading:16424157-Listeriosis,
pubmed-meshheading:16424157-Macrophages,
pubmed-meshheading:16424157-Mice,
pubmed-meshheading:16424157-Mice, Inbred Strains,
pubmed-meshheading:16424157-Mice, Knockout,
pubmed-meshheading:16424157-Oxidation-Reduction,
pubmed-meshheading:16424157-Phagosomes,
pubmed-meshheading:16424157-Virulence Factors,
pubmed-meshheading:16424157-rab5 GTP-Binding Proteins
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
Cutting edge: a novel nonoxidative phagosomal mechanism exerted by cathepsin-D controls Listeria monocytogenes intracellular growth.
|
|
pubmed:affiliation |
Servicio de Inmunología, Hospital Universitario Marqués de Valdecilla, Servicio Cántabro de Salud, Santander, Spain.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
