The investigation of P1 gene in Mycoplasma pneumonia isolated from atypic pneumonia by molecular methods, determine IgG antibody and MIC to ciprofloxacin antibiotic

Abstract Objective Mycoplasma pneumoniae, which causes atypical pneumonia, is a well-established pathogen of the respiratory tract. This bacteria is intrinsically susceptible to fluoroquinolones. But Recently, drug-resistant forms of this bacteria have been reported. This study aims to determine the prevalence of this bacteria by ELISA and PCR and MIC to ciprofloxacin. Methods The clinical samples (blood and nasopharyngeal swab) were collected from 100 patients who were referred to selective hospitals in Tehran with respiratory complaints were enrolled in 2017.Nasopharyngeal swab sample collections were cultured on PPLO broth and PPLO agar. After culturing and DNA extraction, PCR was performed by specific P1 genes primers. Ciprofloxacin's MIC of Mycoplasma pneumonia isolated was determined by Micro-broth dilution method. Also, measure serum IgG antibody titers were measured by ELISA Mycoplasma pneumonia. Results In this study, out of 100 samples 12, bacteria were isolated on PPLO agar.Using specific primers,7 samples of Mycoplasma speciesism-specific were positive for the presence of M.pneumoniae. 2 Ciprofloxacin resistant isolates were evaluated. ELISA results show that the IgG titre antibody In 19 samples is existent. Also,5 samples are intermediate. IgG antibody titre average in the whole sample is 27/66 U/ml but it is in Positive samples by P1 PCR is 45/75 U/ml. Conclusions This study showed that PCR is a sensitive and reliable method for rapid detection of M. pneumoniae bacteria in respiratory infectious samples.but the results of this method are different from the ELISA method. also, It seems that the Resistance to ciprofloxacin is relatively common among M. pneumoniae.

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IgG antibody aggrevates the renal inflammation in an experimental model of IgA nephropathy in rats

Immunology Letters ◽

10.1016/s0165-2478(97)88110-2 ◽

1997 ◽

Vol 56 (1-3) ◽

pp. 315

Author(s):

M Van Dixhoorn

Keyword(s):

Iga Nephropathy ◽

Experimental Model ◽

Igg Antibody ◽

Renal Inflammation

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Partial Inhibition of Platelet Aggregation and Fibrinogen Binding by a Murine Monoclonal Antibody to GPIIIa: Requirement for Antibody Bivalency

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648991 ◽

1994 ◽

Vol 72 (06) ◽

pp. 964-972 ◽

Cited By ~ 16

Author(s):

Jeffery L Kutok ◽

Barry S Coller

Keyword(s):

Monoclonal Antibody ◽

Platelet Aggregation ◽

Murine Monoclonal Antibody ◽

Platelet Glycoprotein ◽

Igg Antibody ◽

Surface Receptors ◽

Partial Inhibition ◽

Fibrinogen Binding ◽

Igg Binding ◽

Agonist Concentration

SummaryWe produced a murine monoclonal antibody, 7H2, and localized its epitope to one or more small regions on platelet glycoprotein (GP) Ilia. 7H2-IgG and 7H2-F(ab’)2 completely inhibit platelet aggregation and fibrinogen binding at low agonist concentrations, but only partially inhibit aggregation and fibrinogen binding at high agonist concentrations; 7H2-Fab has no effect on aggregation or fibrinogen binding at any agonist concentration. 7H2-IgG binds to the entire platelet population as judged by flow cytometry. At near saturating concentrations, ∼40,000 7H2-IgG antibody molecules bind per platelet. In contrast, ∼80,000 7H2 Fab molecules bind per platelet, suggesting that 7H2-IgG binding is bivalent. 7H2 was unable to inhibit fibrinogen binding to purified, immobilized GPIIb/IIIa. These data indicate that the bivalent binding of 7H2 to GPIIIa is required for its partial inhibition of fibrinogen binding to platelets, perhaps through dimerization of GPIIb/IIIa surface receptors (or more complex GPIIb/IIIa redistribution triggered by 7H2 binding) resulting in limited accessibility of fibrinogen to its binding site(s).

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Physiological Effects of Nonimmune Platelet Associated Immunoglobulin G

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650123 ◽

1981 ◽

Vol 45 (01) ◽

pp. 027-033 ◽

Cited By ~ 10

Author(s):

K Sugiura ◽

M Steiner ◽

M Baldini

Keyword(s):

Shape Change ◽

Fluorescein Isothiocyanate ◽

Recovery Phase ◽

Human Platelets ◽

Serotonin Release ◽

Platelet Volume ◽

Igg Antibody ◽

Heterologous Antiserum ◽

Igg Binding ◽

Series Of Experiments

SummaryThe function of nonimmune IgG associated with platelets is unknown. In a series of experiments we have investigated this problem, relating amount of platelet-associated IgG (PAIgG) to platelet volume, serotonin release, adherence of platelets to monocytes and platelet senescence. Most of these studies were performed with human platelets. Platelets freed of preexisting PAIgG by incubation at 22° C were incubated with IgG in a series of concentrations ranging from 0.4 — 27.0 X10-6 M. The IgG preparations used were demonstrably free of aggregated forms of the protein. The amount of PAIgG bound to platelets was determined by the use of fluorescein isothiocyanate-conjugated anti-IgG antibody (F-anti-IgG antibody) which was quantified in a fluorospectrophotometer. Newly bound IgG was assayed similarly by the use of F-IgG. A dose-dependent increase in platelet volume was associated with the binding of nonimmune IgG by platelets. The process which leveled off at an IgG concentration of 1.2 —1.5 X10-5 M was almost fully reversible and was not due to platelet shape change or aggregation. Release of serotonin from IgG-treated platelets was relatively small but to the extent that it occurred was positively related to the IgG concentration to which platelets were exposed. Adherence to autologous monocytes studied quantitatively by the use of formaldehyde-fixed cells was also positively related to the amount of IgG on the platelets. Normal or IgG-defident serum had a potent inhibitory (noncompetitive) action on the binding of F-IgG and F-anti-human IgG antibody to human platelets. Cohorts of platelets prepared in rabbits during the recovery phase of immunological thrombocytopenia induced by injection of heterologous antiserum, showed an age-dependent increase of PAIgG and of IgG binding. These results suggest that PAIgG plays a role in the clearance of senescent platelets.

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