| pubmed-article:18411296 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18411296 | lifeskim:mentions | umls-concept:C0026941 | lld:lifeskim |
| pubmed-article:18411296 | lifeskim:mentions | umls-concept:C0016055 | lld:lifeskim |
| pubmed-article:18411296 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:18411296 | lifeskim:mentions | umls-concept:C0030933 | lld:lifeskim |
| pubmed-article:18411296 | lifeskim:mentions | umls-concept:C0596260 | lld:lifeskim |
| pubmed-article:18411296 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:18411296 | pubmed:dateCreated | 2008-6-20 | lld:pubmed |
| pubmed-article:18411296 | pubmed:abstractText | Mycoplasma pneumoniae is a bacterial pathogen of the human respiratory tract that causes a wide range of airway diseases as well as extrapulmonary symptoms. It possesses a distinct, differentiated terminal structure, termed the attachment organelle, that mediates adherence to the host respiratory epithelium. Previously, we reported that surface-associated M. pneumoniae elongation factor Tu (EF-Tu, also called MPN665) serves as a fibronectin (Fn)-binding protein, facilitating interactions between mycoplasmas and extracellular matrix. In the present study, we determined that binding of M. pneumoniae EF-Tu to Fn is primarily mediated by the EF-Tu carboxyl region. A 179-amino-acid region spanning the carboxyl terminus (designated EC; amino acids 192 to 394) binds Fn in a dose-dependent manner. Further analysis of carboxyl constructs (ED3 and ED4) and their deletion truncations (ED3.1, ED3.2, and ED4.1) revealed that the carboxyl region possessed two distinct sites with different Fn-binding efficiencies. Immunogold electron microscopy using antibodies raised against recombinant ED3 and ED4 demonstrated the surface accessibility of the EF-Tu carboxyl region. Competitive binding assays using intact radiolabeled mycoplasmas and purified recombinant ED3 and ED4 proteins, along with antibody blocking assays, reinforced the role of the surface-exposed EF-Tu carboxyl region in Fn binding. Alkali and high-salt treatment of mycoplasma membranes and Triton X-114-partitioned mycoplasma fractions confirmed the stable association of EF-Tu within the mycoplasma membrane. These observations highlight the unique, multifaceted, and unpredictable role of the classically defined cytoplasmic protein EF-Tu relative to cellular function, compartmentalization, and topography. | lld:pubmed |
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| pubmed-article:18411296 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18411296 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18411296 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18411296 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:18411296 | pubmed:issn | 1098-5522 | lld:pubmed |
| pubmed-article:18411296 | pubmed:author | pubmed-author:KannanT RTR | lld:pubmed |
| pubmed-article:18411296 | pubmed:author | pubmed-author:BasemanJoel... | lld:pubmed |
| pubmed-article:18411296 | pubmed:author | pubmed-author:Balasubramani... | lld:pubmed |
| pubmed-article:18411296 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18411296 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:18411296 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18411296 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18411296 | pubmed:pagination | 3116-23 | lld:pubmed |
| pubmed-article:18411296 | pubmed:dateRevised | 2010-9-22 | lld:pubmed |
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