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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2006-9-21
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pubmed:abstractText |
Various bacterial pathogens secrete toxins, which are not only responsible for fatal pathogenesis of disease, but also facilitate evasion of host defences. One of the best-known bacterial toxin groups is the mono-ADP-ribosyltransferase family. In the present study, we demonstrate that human neutrophil alpha-defensins are potent inhibitors of the bacterial enzymes, particularly against DT (diphtheria toxin) and ETA (Pseudomonas exotoxin A). HNP1 (human neutrophil protein 1) inhibited DT- or ETA-mediated ADP-ribosylation of eEF2 (eukaryotic elongation factor 2) and protected HeLa cells against DT- or ETA-induced cell death. Kinetic analysis revealed that inhibition of DT and ETA by HNP1 was competitive with respect to eEF2 and uncompetitive against NAD+ substrates. Our results reveal that toxin neutralization represents a novel biological function of HNPs in host defence.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-11319814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-11595641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-11890553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-12060767,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-12072367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-12393692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-12530476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-14733615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-14976550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-15213400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-15330253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-15772169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-15802128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-16107839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-16406634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-221485,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-4056036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-447682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-5545092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-5545093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-7827036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-7968608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-8476558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-8878030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-8920207,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16817779-9841866
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1470-8728
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
399
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
225-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16817779-Adenosine Diphosphate Ribose,
pubmed-meshheading:16817779-Animals,
pubmed-meshheading:16817779-Cell Death,
pubmed-meshheading:16817779-Corynebacterium diphtheriae,
pubmed-meshheading:16817779-Diphtheria Toxin,
pubmed-meshheading:16817779-Exotoxins,
pubmed-meshheading:16817779-HeLa Cells,
pubmed-meshheading:16817779-Humans,
pubmed-meshheading:16817779-Kinetics,
pubmed-meshheading:16817779-Mice,
pubmed-meshheading:16817779-NAD,
pubmed-meshheading:16817779-Peptide Elongation Factor 2,
pubmed-meshheading:16817779-Protein Binding,
pubmed-meshheading:16817779-Substrate Specificity,
pubmed-meshheading:16817779-Thermodynamics,
pubmed-meshheading:16817779-alpha-Defensins
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pubmed:year |
2006
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pubmed:articleTitle |
Human alpha-defensins neutralize toxins of the mono-ADP-ribosyltransferase family.
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pubmed:affiliation |
Department of Immunology, Max Planck Institute for Infection Biology, Schumannstrasse 21-22, D-10117 Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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