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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2000-6-23
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pubmed:abstractText |
Streptococcus pyogenes secretes several proteins that influence host-pathogen interactions. A tissue-culture model was used to study the influence of the secreted cysteine protease streptococcal erythrogenic toxin B (SPE B) on the interaction between S. pyogenes strain NZ131 (serotype M49) and mammalian cells. Inactivation of the speB gene enhanced fibronectin-dependent uptake of the pathogen by Chinese hamster ovary (CHO-K1) cells compared to that in the isogenic wild-type strain. Preincubation of the NZ131 speB mutant with purified SPE B protease significantly inhibited fibronectin-dependent uptake by both CHO-K1 and CHO-pgs745 cells. The effect was attributed to an abrogation of fibronectin binding to the surface of the bacteria that did not involve either the M49 protein or the streptococcal fibronectin-binding protein SfbI. In contrast, pretreatment of the NZ131 speB mutant with SPE B did not influence sulfated polysaccharide-mediated uptake by CHO-pgs745 cells. The results indicate that the SPE B protease specifically alters bacterial cell surface proteins and thereby influences pathogen uptake.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-10048029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-10456887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-10456915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-10681429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-10753062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-1327968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-14334353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-1439793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-1936949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-1987034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-2198264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-2643059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-2843471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-388439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-7516997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-7689226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-7706813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-7730368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-7968627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-7991594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-8359893,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-8577996,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-9199429,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-9701828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-9746555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-9784580,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-9822827,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-9846743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816467-9864206
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Exotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SpeA protein, Streptococcus pyogenes,
http://linkedlifedata.com/resource/pubmed/chemical/erythrogenic toxin,
http://linkedlifedata.com/resource/pubmed/chemical/fibronectin-binding proteins...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0019-9567
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
68
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3226-32
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pubmed:dateRevised |
2010-10-19
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pubmed:meshHeading |
pubmed-meshheading:10816467-Adhesins, Bacterial,
pubmed-meshheading:10816467-Animals,
pubmed-meshheading:10816467-Bacterial Adhesion,
pubmed-meshheading:10816467-Bacterial Proteins,
pubmed-meshheading:10816467-CHO Cells,
pubmed-meshheading:10816467-Carrier Proteins,
pubmed-meshheading:10816467-Cricetinae,
pubmed-meshheading:10816467-Cysteine Endopeptidases,
pubmed-meshheading:10816467-Exotoxins,
pubmed-meshheading:10816467-Fibronectins,
pubmed-meshheading:10816467-Membrane Proteins,
pubmed-meshheading:10816467-Streptococcus pyogenes
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pubmed:year |
2000
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pubmed:articleTitle |
Streptococcal erythrogenic toxin B abrogates fibronectin-dependent internalization of Streptococcus pyogenes by cultured mammalian cells.
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pubmed:affiliation |
Laboratory of Human Bacterial Pathogenesis, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840, USA. mchaussee@nih.gov
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pubmed:publicationType |
Journal Article
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