No high background was observed (OD450 ≤ 0.05). Panels of serum samples from 103 patients and 86 healthy blood donors were screened for anti-M. pneumoniae IgM, IgG and IgA antibodies using the corresponding Ani Labsystems EIA kits according to the manufacturer’s instructions. Statistical analysis All results were analysed with the Tanagra software 1.4.31 (http://chirouble.univ-lyon2.fr/~ricco/tanagra/fr/tanagra.html). The accuracy of the serological assays in discriminating disease cases from normal cases was evaluated by using ROC curve plots [44]. ROC plots were
calculated by expressing the relationship between the fraction “”correctly identified to be positive”" and the fraction “”falsely identified to be positive”" for every possible cut-off point selected to discriminate between the patients and the blood donors. The AUC is a measure of the assay efficiency
to discriminate the “”true positives”" from the “”true negatives”". The cut-off values BI 2536 cost for every in-house serological assay were determined for maximum efficiency of the test. A sample was considered positive if the antibody titre exceeded the defined cut-off value. Binary logistic regression analysis was performed before evaluating the performance of the antigen combination by ROC plots as described above. Sensitivity, specificity and 95% confidence intervals (95% CI) were calculated for rAtpD and rP1-C antigens, either alone or in combination. The calculation of cut-off Cobimetinib solubility dmso values and the interpretation of the results of the Ani Labsystems kits were performed GDC973 according to the manufacturer’s instructions. Acknowledgements We thank J. selleck inhibitor Raymond and J.L. Gaillard for providing M. pneumoniae-positive serum specimens from Cochin hospital (Paris) and Raymond Poincaré hospital (Garches), respectively. References 1. Gerstenecker B, Jacobs E: Topological mapping of the P1-adhesin of Mycoplasmapneumoniae with adherence-inhibiting monoclonal antibodies. J Gen Microbiol 1990, 136:471–476.PubMed
2. Svenstrup HF, Nielsen PK, Drasbek M, Birkelund S, Christiansen G: Adhesion and inhibition assay of Mycoplasma genitalium and M. pneumoniae by immunofluorescence microscopy. J Med Microbiol 2002, 51:361–373.PubMedCrossRef 3. Willby MJ, Balish MF, Ross SM, Lee KK, Jordan JL, Krause DC: HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae . J Bacteriol 2004, 186:8221–8228.PubMedCrossRef 4. Waldo RH, Krause DC: Synthesis, stability, and function of cytadhesin P1 and accessory protein B/C complex of Mycoplasma pneumoniae . J Bacteriol 2006, 188:569–575.PubMedCrossRef 5. Chaudhry R, Varshney AK, Malhotra P: Adhesion proteins of Mycoplasma pneumoniae. Front Biosci 2007, 12:690–699.PubMedCrossRef 6. Clyde WA Jr: Clinical overview of typical Mycoplasma pneumoniae infections. Clin Infect Dis 1993,17(Suppl 1):S32-S36.PubMed 7. Waites KB, Talkington : Mycoplasma pneumoniae and its role as a human pathogen.
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