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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2005-11-21
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pubmed:abstractText |
Type III cytotoxins contribute to the ability of bacterial pathogens to subvert the host innate immune system. ExoS (453 amino acids) is a bifunctional type III cytotoxin produced by Pseudomonas aeruginosa. Residues 96 to 232 comprise a Rho GTPase activating protein domain, while residues 233 to 453 comprise a 14-3-3-dependent ADP-ribosyltransferase domain. An N-terminal domain (termed the membrane localization domain [MLD]) targets ExoS to the Golgi-endoplasmic reticulum (Golgi-ER) of mammalian cells. This study identifies an amino acid motif that is responsible for the membrane binding properties of the MLD. Deletion mapping showed that the MLD included a symmetrical leucine-rich motif within residues 51 to 77 of ExoS. The terminal dileucines and internal leucines and an isoleucine within the MLD, but not charged or other hydrophobic residues, targeted a reporter protein to the Golgi-ER region of HeLa cells. Mutations of the leucines within the MLD did not affect type III secretion or translocation into HeLa cells but limited the ability of ExoS to ADP-ribosylate Ras GTPases. Mutations of charged residues within the MLD did not affect type III secretion, delivery into HeLa cells, or the ability of ExoS to ADP-ribosylate Ras GTPases. The organization of the leucines within the MLD of ExoS is different from that of previously described leucine-rich motifs but is present in several other bacterial proteins. This implies a role for intracellular targeting in the efficient targeting of mammalian cells by type III cytotoxins.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-10496922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-10502464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-10593930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-10825282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-10844661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-10931325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-10931345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-10940022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-11060011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-11111915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-11402339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-11748202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-11821389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-12132999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-12453223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-12626518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-14597627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-1535555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-1599416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-1937783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-1937815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-417030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-6405475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-7816143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-8418052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-8621406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-9045820,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-9069263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-9171345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-9184219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-9427393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-9651318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-9767584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-9767593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16299285-9988481
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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 |
Dec
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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 |
73
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7938-45
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16299285-ADP Ribose Transferases,
pubmed-meshheading:16299285-ADP-Ribosylation Factors,
pubmed-meshheading:16299285-Amino Acid Motifs,
pubmed-meshheading:16299285-Amino Acid Sequence,
pubmed-meshheading:16299285-Amino Acid Substitution,
pubmed-meshheading:16299285-Bacterial Toxins,
pubmed-meshheading:16299285-Cell Membrane,
pubmed-meshheading:16299285-Cytotoxins,
pubmed-meshheading:16299285-HeLa Cells,
pubmed-meshheading:16299285-Humans,
pubmed-meshheading:16299285-Leucine,
pubmed-meshheading:16299285-Molecular Sequence Data,
pubmed-meshheading:16299285-Mutation,
pubmed-meshheading:16299285-Protein Transport,
pubmed-meshheading:16299285-Pseudomonas aeruginosa,
pubmed-meshheading:16299285-Sequence Deletion,
pubmed-meshheading:16299285-ras Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
A leucine-rich motif targets Pseudomonas aeruginosa ExoS within mammalian cells.
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pubmed:affiliation |
Medical College of Wisconsin, Microbiology and Molecular Genetics, 8701 Watertown Plank Rd., Milwaukee, WI 53226, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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