ArticleInfection and immunity2009
Amino acid changes in elongation factor Tu of Mycoplasma pneumoniae and Mycoplasma genitalium influence fibronectin binding.
Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
- Review
- The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis.Frontiers in microbiology · 2019Review
- High quality draft genome sequence ofStandards in genomic sciences · 2018Article
- Elongation factor Tu is a multifunctional and processed moonlighting protein.Scientific reports · 2017Article
- Article
- Comparative genomic analysis of seven Mycoplasma hyosynoviae strains.MicrobiologyOpen · 2015Article
- The identification of six novel proteins with fibronectin or collagen type I binding activity from Streptococcus suis serotype 2.Journal of microbiology (Seoul, Korea) · 2014Article
- Proteomic and genomic analysis reveals novelEuPA open proteomics · 2014Article
- Description of a novel adhesin of Mycobacterium avium subsp. paratuberculosis.BioMed research international · 2014Article
- Factors influencing the cell adhesion and invasion capacity of Mycoplasma gallisepticum.Acta veterinaria Scandinavica · 2013Article
- Identification and characterization of sulfated carbohydrate-binding protein from Lactobacillus reuteri.PloS one · 2013Article
- Immunoproteomics: the key to discovery of new vaccine antigens against bacterial respiratory infections.Current protein & peptide science · 2012Review
- Methionine sulfoxide reductase A (MsrA) deficient Mycoplasma genitalium shows decreased interactions with host cells.PloS one · 2012Article
- Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease.Infection and immunity · 2011Review
- Immunospecific responses to bacterial elongation factor Tu during Burkholderia infection and immunization.PloS one · 2010Article
- Mycoplasma pneumoniae Mpn133 is a cytotoxic nuclease with a glutamic acid-, lysine- and serine-rich region essential for binding and internalization but not enzymatic activity.Cellular microbiology · 2010Article
- Molecular cloning, expression, and characterization of a Ca2+-dependent, membrane-associated nuclease of Mycoplasma genitalium.Journal of bacteriology · 2010Article
- Entry of Spiroplasma citri into Circulifer haematoceps cells involves interaction between spiroplasma phosphoglycerate kinase and leafhopper actin.Applied and environmental microbiology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mycoplasma pneumoniae and Mycoplasma genitalium are closely related organisms that cause distinct clinical manifestations and possess different tissue predilections despite their high degree of genome homology. We reported earlier that surface-localized M. pneumoniae elongation factor Tu (EF-Tu(Mp)) mediates binding to the extracellular matrix component fibronectin (Fn) through the carboxyl region of EF-Tu. In this study, we demonstrate that surface-associated M. genitalium EF-Tu (EF-Tu(Mg)), in spite of sharing 96% identity with EF-Tu(Mp), does not bind Fn. We utilized this finding to identify the essential amino acids of EF-Tu(Mp) that mediate Fn interactions by generating modified recombinant EF-Tu proteins with amino acid changes corresponding to those of EF-Tu(Mg). Amino acid changes in serine 343, proline 345, and threonine 357 were sufficient to significantly reduce the Fn binding of EF-Tu(Mp). Synthetic peptides corresponding to this region of EF-Tu(Mp) (EF-Tu(Mp) 340-358) blocked both recombinant EF-Tu(Mp) and radiolabeled M. pneumoniae cell binding to Fn. In contrast, EF-Tu(Mg) 340-358 peptides exhibited minimal blocking activity, reinforcing the specificity of EF-Tu-Fn interactions as mediators of microbial colonization and tissue tropism.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.