ArticleJournal of bacteriology2004
OppA, the substrate-binding subunit of the oligopeptide permease, is the major Ecto-ATPase of Mycoplasma hominis.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
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- Mycoplasma bovis 5'-nucleotidase is a virulence factor conferring mammary fitness in bovine mastitis.PLoS pathogens · 2024Article
- Thymidine utilisation pathway is a novel phenotypic switch ofJournal of medical microbiology · 2022Article
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- Population Genomic Analysis ofMicroorganisms · 2020Article
- DNA Vaccines Against Mycoplasma Elicit Humoral Immune Responses in Ostriches.Frontiers in immunology · 2019Article
- Transcriptional Studies on aApplied and environmental microbiology · 2018Article
- Generation of Mycoplasma hominis gene-targeted mutants by targeting-induced local lesions in genomes (TILLING).BMC genomics · 2018Article
- Whole-Genome Characterization of Bacillus cereus Associated with Specific Disease Manifestations.Infection and immunity · 2018Article
- The Variable Internal Structure of the Mycoplasma penetrans Attachment Organelle Revealed by Biochemical and Microscopic Analyses: Implications for Attachment Organelle Mechanism and Evolution.Journal of bacteriology · 2017Article
- Changes in pathogenicity and immunogenicity of Mycoplasma mycoides subsp. mycoides strains revealed by comparative genomics analysis.Scientific reports · 2016Article
- The Mycoplasma gallisepticum virulence factor lipoprotein MslA is a novel polynucleotide binding protein.Infection and immunity · 2013Article
- Improved adhesive properties of recombinant bifidobacteria expressing the Bifidobacterium bifidum-specific lipoprotein BopA.Microbial cell factories · 2012Article
- In Mycoplasma hominis the OppA-mediated cytoadhesion depends on its ATPase activity.BMC microbiology · 2011Article
- The liposoluble proteome of Mycoplasma agalactiae: an insight into the minimal protein complement of a bacterial membrane.BMC microbiology · 2010Article
- Life on arginine for Mycoplasma hominis: clues from its minimal genome and comparison with other human urogenital mycoplasmas.PLoS genetics · 2009Article
- Possible effects of microbial ecto-nucleoside triphosphate diphosphohydrolases on host-pathogen interactions.Microbiology and molecular biology reviews : MMBR · 2008Review
- Differential expression of lipoprotein genes in Mycoplasma pneumoniae after contact with human lung epithelial cells, and under oxidative and acidic stress.BMC microbiology · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most ATPases, involved in energy-driven processes, act in the cytoplasm. However, external membrane-bound ATPases have also been described in parasites and eukaryotic cells. In Mycoplasma hominis, a bacterium lacking a cell wall, the surface-exposed substrate-binding protein OppA of an oligopeptide permease (Opp) contains an ATP binding P-loop structure in the C-terminal region. With ATP affinity chromatography and tryptic digestion in the presence or absence of ATP, the functionality of the Mg(2+)-dependent ATP binding site is demonstrated. In addition to ATP, ADP also could bind to OppA. The presence of an ATPase activity on the surface of M. hominis is indicated by the inactivation of ATP hydrolyzing activity of intact mycoplasma cells by the impermeable ATPase inhibitor 4',4'-diisothiocyanostilbene-2',2'-disulfonic acid and influenced by the ATP analog 5'-fluorosulfonyl-benzoyladenosine. Comparing equimolar amounts of OppA in intact mycoplasma cells and in the purified form indicated that more than 80% of the surface-localized ATPase activity is derived from OppA, implying that OppA is the main ATPase on the surface of mycoplasma cells. Together, these data present the first evidence that the cytoadhesive substrate binding protein OppA of the oligopeptide permease also functions as an ecto-ATPase in Mycoplasma hominis.
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