Prof. Dr. B. Henrich

Main Research

Characterisation of membrane proteins of Mycoplasma hominis, a facultative pathogen colonising the human uro-genital tract, identified some of them as multi-functional: 

OppA, the substrate-binding domain of the oligopeptide permease, was shown to act as a cytoadhesin and is the main ectoATPase, which has an apoptotic effect on HeLa cells. The focus of our research is now targeted at the mapping of the functional peptide regions (peptide binding, phosphorylation sites and cytoadhesion), generation of respective OppA mutants and characterisation of their patho-physiological effects on eucaryotic cells.

Having determined that the mycoplasma protein P80, a predominantly surface-localised membrane protein with cyto-adhesive and secretory properties, interacts with HinT, a cytoplasmic nucleotidyl hydrolase, we are now interested in the identification of further HinT-interaction partners in the Mollicutes.

To improve the diagnosis of human pathogens that are difficult to culture we have established and evaluated an in-house TaqMan-qPCRs for the simultaneous detection of Mycoplasma, Ureaplasma and Chlamydia  spp. and the differentiation of lymphogranumloma venereum associated serovars L1, L2 and L3 of C. trachomatis. To date we are optimizing the rDNA-based qPCR detection of pro- and lower eucaryotes in primary sterile samples (e.g. blood, liquor or biopsy).

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