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. 2011 Jun 10:11:233.
doi: 10.1186/1471-2407-11-233.

Detection of antibodies directed at M. hyorhinis p37 in the serum of men with newly diagnosed prostate cancer

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Detection of antibodies directed at M. hyorhinis p37 in the serum of men with newly diagnosed prostate cancer

Cydney Urbanek et al. BMC Cancer. .

Abstract

Background: Recent epidemiologic, genetic, and molecular studies suggest infection and inflammation initiate certain cancers, including cancers of the prostate. Over the past several years, our group has been studying how mycoplasmas could possibly initiate and propagate cancers of the prostate. Specifically, Mycoplasma hyorhinis encoded protein p37 was found to promote invasion of prostate cancer cells and cause changes in growth, morphology and gene expression of these cells to a more aggressive phenotype. Moreover, we found that chronic exposure of benign human prostate cells to M. hyorhinis resulted in significant phenotypic and karyotypic changes that ultimately resulted in the malignant transformation of the benign cells. In this study, we set out to investigate another potential link between mycoplasma and human prostate cancer.

Methods: We report the incidence of men with prostate cancer and benign prostatic hyperplasia (BPH) being seropositive for M. hyorhinis. Antibodies to M. hyorhinis were surveyed by a novel indirect enzyme-linked immunosorbent assay (ELISA) in serum samples collected from men presenting to an outpatient Urology clinic for BPH (N = 105) or prostate cancer (N = 114) from 2006-2009.

Results: A seropositive rate of 36% in men with BPH and 52% in men with prostate cancer was reported, thus leading us to speculate a possible connection between M. hyorhinis exposure with prostate cancer.

Conclusions: These results further support a potential exacerbating role for mycoplasma in the development of prostate cancer.

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Figures

Figure 1
Figure 1
Purification of recombinant M. hyorhinis p37 protein by affinity chromotography. M. hyorhinis p37 (MH38-113) was expressed in E. coli and purified as described previously [16]. Sonicated cell lysate of E. coli was applied to a cobalt affinity column, and the bound protein was eluted with 150 mM imidazole. A total of 25 μg eluate was electrophoresed in a 12% SDS-PAGE gel, and stained with Coomassie blue. M, Prestained BenchMark Protein ladder (kDa); 1, purified recombinant protein. The arrow indicates the position of the recombinant protein.
Figure 2
Figure 2
Box plots of O.D. value detecting M hyorhinis serum antibodies. The distributions of O. D. values are presented in a box plot.
Figure 3
Figure 3
Detection limits of novel indirect ELISA for M. hyorhinis serum antibodies. Varying concentrations of M. hyorhinis antibodies were added to our indirect ELISA to illustrate the range of detection.

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