ArticleBMC microbiology2010
Identification, expression and serological evaluation of the recombinant ATP synthase beta subunit of Mycoplasma pneumoniae.
Article in BMC microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Indirect ELISA developed to detect antibodies against Mycoplasma synoviae P50 protein via immunoproteomic screening.Applied microbiology and biotechnology · 2025Article
- Evaluation of the CARDS toxin and its fragment for the serodiagnosis of Mycoplasma pneumoniae infections.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2021Article
- Lipid moieties ofNPJ vaccines · 2020Article
- Pathogenic Analysis of the Bronchoalveolar Lavage Fluid Samples With Pediatric RefractoryFrontiers in cellular and infection microbiology · 2020Article
- Immunoproteomic identification of MbovP579, a promising diagnostic biomarker for serological detection of Mycoplasma bovis infection.Oncotarget · 2016Article
- Antibody Response to Mycoplasma pneumoniae: Protection of Host and Influence on Outbreaks?Frontiers in microbiology · 2016Review
- Evaluation of P1 adhesin epitopes for the serodiagnosis of Mycoplasma pneumoniae infections.FEMS microbiology letters · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMycoplasma pneumoniae is responsible for acute respiratory tract infections (RTIs) common in children and young adults. As M. pneumoniae is innately resistant to beta-lactams antibiotics usually given as the first-line treatment for RTIs, specific and early diagnosis is important in order to select the right treatment. Serology is the most used diagnostic method for M. pneumoniae infections.
resultsIn this study, we identified the M. pneumoniae ATP synthase beta subunit (AtpD) by serologic proteome analysis and evaluated its usefulness in the development of a serological assay. We successfully expressed and purified recombinant AtpD (rAtpD) protein, which was recognised by serum samples from M. pneumoniae-infected patient in immunoblots. The performance of the recombinant protein rAtpD was studied using a panel of serum samples from 103 infected patients and 86 healthy blood donors in an in-house IgM, IgA and IgG enzyme-linked immunosorbent assay (ELISA). The results of this assay were then compared with those of an in-house ELISA with a recombinant C-terminal fragment of the P1 adhesin (rP1-C) and of the commercial Ani Labsystems ELISA kit using an adhesin P1-enriched whole-cell extract. Performances of the rAtpD and rP1-C antigen combination were further assessed by binary logistic regression analysis. We showed that combination of rAtpD and rP1-C discriminated maximally between the patients infected with M. pneumoniae (children and adults) and the healthy subjects for the IgM class, performing better than the single recombinant antigens or the commercial whole-cell extract.
conclusionThese results suggest that AtpD can be used as an antigen for the immunodiagnosis of early and acute M. pneumoniae infection in association with adhesin P1, providing an excellent starting point for the development of point-of-care diagnostic assays.
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