| pubmed-article:20123991 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20123991 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:20123991 | lifeskim:mentions | umls-concept:C0007582 | lld:lifeskim |
| pubmed-article:20123991 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:20123991 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:20123991 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:20123991 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:20123991 | pubmed:dateCreated | 2010-3-29 | lld:pubmed |
| pubmed-article:20123991 | pubmed:abstractText | Bacteria mostly live as multicellular communities, although they are unicellular organisms, yet the mechanisms that tie individual bacteria together are often poorly understood. The adhesin involved in diffuse adherence (AIDA-I) is an adhesin of diarrheagenic Escherichia coli strains. AIDA-I also mediates bacterial auto-aggregation and biofilm formation and thus could be important for the organization of communities of pathogens. Using purified protein and whole bacteria, we provide direct evidence that AIDA-I promotes auto-aggregation by interacting with itself. Using various biophysical and biochemical techniques, we observed a conformational change in the protein during AIDA-AIDA interactions, strengthening the notion that this is a highly specific interaction. The self-association of AIDA-I is of high affinity but can be modulated by sodium chloride. We observe that a bile salt, sodium deoxycholate, also prevents AIDA-I oligomerization and bacterial auto-aggregation. Thus, we propose that AIDA-I, and most likely other similar autotransporters such as antigen 43 (Ag43) and TibA, organize bacterial communities of pathogens through a self-recognition mechanism that is sensitive to the environment. This could permit bacteria to switch between multicellular and unicellular lifestyles to complete their infection. | lld:pubmed |
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| pubmed-article:20123991 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20123991 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20123991 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20123991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20123991 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20123991 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:20123991 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:20123991 | pubmed:author | pubmed-author:MourezMichael... | lld:pubmed |
| pubmed-article:20123991 | pubmed:author | pubmed-author:SiddiquiNadee... | lld:pubmed |
| pubmed-article:20123991 | pubmed:author | pubmed-author:CamposManuelM | lld:pubmed |
| pubmed-article:20123991 | pubmed:author | pubmed-author:HancockMark... | lld:pubmed |
| pubmed-article:20123991 | pubmed:author | pubmed-author:BerthiaumeFré... | lld:pubmed |
| pubmed-article:20123991 | pubmed:author | pubmed-author:GirardVictori... | lld:pubmed |
| pubmed-article:20123991 | pubmed:author | pubmed-author:CharbonneauMa... | lld:pubmed |
| pubmed-article:20123991 | pubmed:author | pubmed-author:CôtéJean-Phil... | lld:pubmed |
| pubmed-article:20123991 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20123991 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:20123991 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:20123991 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20123991 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20123991 | pubmed:pagination | 10616-26 | lld:pubmed |
| pubmed-article:20123991 | pubmed:dateRevised | 2011-7-27 | lld:pubmed |
| pubmed-article:20123991 | pubmed:meshHeading | pubmed-meshheading:20123991... | lld:pubmed |
| pubmed-article:20123991 | pubmed:meshHeading | pubmed-meshheading:20123991... | lld:pubmed |
| pubmed-article:20123991 | pubmed:meshHeading | pubmed-meshheading:20123991... | lld:pubmed |
| pubmed-article:20123991 | pubmed:meshHeading | pubmed-meshheading:20123991... | lld:pubmed |
| pubmed-article:20123991 | pubmed:meshHeading | pubmed-meshheading:20123991... | lld:pubmed |
| pubmed-article:20123991 | pubmed:meshHeading | pubmed-meshheading:20123991... | lld:pubmed |
| pubmed-article:20123991 | pubmed:meshHeading | pubmed-meshheading:20123991... | lld:pubmed |
| pubmed-article:20123991 | pubmed:meshHeading | pubmed-meshheading:20123991... | lld:pubmed |
| pubmed-article:20123991 | pubmed:meshHeading | pubmed-meshheading:20123991... | lld:pubmed |
| pubmed-article:20123991 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20123991 | pubmed:articleTitle | Conformation change in a self-recognizing autotransporter modulates bacterial cell-cell interaction. | lld:pubmed |
| pubmed-article:20123991 | pubmed:affiliation | Canada Research Chair on Bacterial Animal Diseases, Université de Montréal, Saint-Hyacinthe, Québec J2S 7C6, Canaada. | lld:pubmed |
| pubmed-article:20123991 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20123991 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20123991 | lld:pubmed |
