ArticleBMC infectious diseases2010
Identification of an N-terminal 27 kDa fragment of Mycoplasma pneumoniae P116 protein as specific immunogen in M. pneumoniae infections.
Article in BMC infectious diseases, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 22 citations in OpenAlex.
- Clinical utility of the targeted next-generation sequencing for detection of Mycoplasma pneumoniae and antimicrobial resistance genes for adults.BMC infectious diseases · 2026Article
- Immune dysregulation inFrontiers in immunology · 2026Review
- Therapeutic Efficacy of an Anti-P116-661 Polyclonal Antibody AgainstPathogens (Basel, Switzerland) · 2025Article
- Detection of human IgG antibodies againstJournal of clinical microbiology · 2025Article
- Case Report: PositiveFrontiers in pediatrics · 2025Article
- Exploring the pathogenetic mechanisms ofExperimental and therapeutic medicine · 2024Review
- Reviewing advancement inFrontiers in microbiology · 2024Review
- Galacto-Oligosaccharides as an Anti-Infective and Anti-Microbial Agent for Macrolide-Resistant and -SensitivePathogens (Basel, Switzerland) · 2023Article
- A novel inactivated whole-cell Pseudomonas aeruginosa vaccine that acts through the cGAS-STING pathway.Signal transduction and targeted therapy · 2021Article
- Development and clinical evaluation of a rapid antibody lateral flow assay for the diagnosis of SARS-CoV-2 infection.BMC infectious diseases · 2021Article
- 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
- Review
- Antibody Response to Mycoplasma pneumoniae: Protection of Host and Influence on Outbreaks?Frontiers in microbiology · 2016Review
- Delineation of immunodominant and cytadherence segment(s) of Mycoplasma pneumoniae P1 gene.BMC microbiology · 2014Article
- Evaluation of P1 adhesin epitopes for the serodiagnosis of Mycoplasma pneumoniae infections.FEMS microbiology letters · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMycoplasma pneumoniae is an important cause of respiratory tract infection and is increasingly being associated with other diseases such as asthma and extra-pulmonary complications. Considerable cross-reactivity is known to exist between the whole cell antigens used in the commercial serological testing assays. Identification of specific antigens is important to eliminate the risk of cross-reactions among different related organisms. Adherence of M. pneumoniae to human epithelial cells is mediated through a well defined apical organelle to which a number of proteins such as P1, P30, P116 and HMW1-3 have been localized, and are being investigated for adhesion, gliding and immunodiagnostic purposes.
methodsA 609 bp fragment P116(N-27), corresponding to the N-terminal region of M. pneumoniae P116 gene was cloned and expressed. A C-terminal fragment P1(C-40), of P1 protein of M. pneumoniae was also expressed. Three IgM ELISA assays based on P116(N-27), P1(C-40) and (P116 (N-27) + P1(C-40)) proteins were optimized and a detailed analysis comparing the reactivity of these proteins with a commercial kit was carried out. Comparative statistical analysis of these assays was performed with the SPSS version 15.0.
resultsThe expressed P116(N-27) protein was well recognized by the patient sera and was immunogenic in rabbit. P1(C-40) of M. pneumoniae was also immunogenic in rabbit. In comparison to the reference kit, which is reported to be 100% sensitive and 75% specific, ELISA assay based on purified P116(N-27), P1(C-40) and (P116(N-27) + P1(C-40)) proteins showed 90.3%, 87.1% and 96.8% sensitivity and 87.0%, 87.1% and 90.3% specificity respectively. The p value for all the three assays was found to be < 0.001, and there was a good correlation and association between them.
conclusionThis study shows that an N-terminal fragment of P116 protein holds a promise for serodiagnosis of M. pneumoniae infection. The IgM ELISA assays based on the recombinant proteins seem to be suitable for the use in serodiagnosis of acute M. pneumoniae infections. The use of short recombinant fragments of P116 and P1 proteins as specific antigens may eliminate the risk of cross-reactions and help to develop a specific and sensitive immunodiagnostic assay for M. pneumoniae detection.
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