pneumophila

(10) 0 0 0 C. burnetii (10) 0 1 0 S. pneumoniae (8) 0 2 0 B. pertussis (8) 0 0 0 C. psittaci (1) 0 0 0 Discussion Respiratory disease due to M. pneumoniae can be assessed by serological methods, and of these the CFT and ELISA are most widely used. The conserved C-terminal region of the P1 GDC-0449 molecular weight adhesin (rP1-C) was recently confirmed as the main antigen for the immunodiagnosis of M. pneumoniae infections [13, 16]. This work reports the first immunoproteomic study for M. pneumoniae, leading to the identification of new antigenic proteins such as the ATP synthase beta subunit, enolase, the pyruvate dehydrogenase beta subunit (PDH-B) and Regorafenib fructose bisphosphate aldolase. Antibodies against the GroEl protein have previously

been reported in serum samples from patients with RTIs [24]. All of the antigens described in this study, except the enolase protein, were previously described as “”proteins of the Triton X-100 insoluble fraction of M. pneumoniae”" [25]. These proteins may be associated or bound to a cytoskeleton-like structure, which could provide the necessary framework to maintain and stabilize the shape of M. pneumoniae [26], to allow motility [27] and to allow the formation of an asymmetric cell. this website The correct assembly of this organelle is a prerequisite for the binding of M. pneumoniae to specific receptors on the host cell [28, 29]. Previous studies have demonstrated that the enolase and the PDH-B protein in addition to their major biosynthetic and metabolic roles in the cytoplasm, could be translocated to the surface to serve as plasminogen- and fibronectin-binding proteins, respectively, facilitating interactions between mycoplamas and the extracellular matrix [30, 31]. Thus, these data suggest a pivotal role for these proteins in the infection mechanism of M. pneumoniae. Serologic proteome analysis showed that the

AtpD and the P1 proteins were highly detected by serum samples from patients with RTIs and not from healthy blood donors. The other proteins identified were less able Erythromycin to discriminate between patients and controls as they were lightly antigenic to blood donors (confirmed with further ELISA studies, data not shown). Thus the AtpD and the rP1-C proteins were selected for further serological study focusing on comparisons of the performance of assays using these recombinant proteins with assays using adhesin P1-enriched total extracts such as the commercial Ani Labsystems kit. To this end, the atpD gene and the P1-C sequence were cloned, expressed in E. coli, and purified. The serological performance of the two recombinant proteins either alone or in combination (logistic regression analysis), and of the Ani Labsystems kit were further compared using a panel of 103 serum samples from M. pneumoniae-infected patients (54 children and 49 adults) and 86 serum samples from healthy blood donors.