Abstract
Mycoplasma hominis has been implicated in many inflammatory conditions of the human urogenital tract in particular amniotic infections that lead to fetal and neonatal disease and pre-term labor. The mechanisms responsible are poorly defined. Biochemical and immunological methods were used to extract, purify, and characterize an inflammatory component present in M.hominis. We isolated and purified to homogeneity a 40-kDa bioactive lipoprotein from M.hominis that was a potent TLR2-dependent, CD14-independent activator of the human THP-1 macrophage cell line. Homology searches of the N-terminal sequence revealed that 22 of the first 23 residues were identical to those seen for the phase-variable M.hominis p50 adhesin. The truncated P50t lipoprotein importantly retained its adhesive properties for human macrophages. The unique adhesin/macrophage activator may play a key role in M.hominis infections by triggering an inflammatory cytokine cascade.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
