All subtypes of the Pmp adhesin family are implicated in chlamydial virulence and show species-specific function
Article first published online: 1 JUL 2014
© 2014 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 3, Issue 4, pages 544–556, August 2014
How to Cite
MicrobiologyOpen 2014; 3(4): 544–556
- Issue published online: 14 AUG 2014
- Article first published online: 1 JUL 2014
- Manuscript Accepted: 15 MAY 2014
- Manuscript Revised: 30 APR 2014
- Manuscript Received: 23 DEC 2013
- Deutsche Forschungsgemeinschaft
- Federal Ministry for Education and Research
- Chlamydia pneumoniae ;
- Chlamydia trachomatis ;
- Pmp protein family;
The bacterial pathogens Chlamydia trachomatis and C. pneumoniae are obligate intracellular parasites, cause a number of serious diseases, and can infect various cell types in humans. Chlamydial infections are probably initiated by binding of the bacterial outer membrane protein OmcB to host cell glycosaminoglycans (GAGs). Here, we show that all nine members of the polymorphic membrane protein (Pmp) family of C. trachomatis mediate adhesion to human epithelial and endothelial cells. Importantly, exposure of infectious particles to soluble recombinant Pmps blocks subsequent infection, thus implicating an important function of the entire protein family in the infection process. Analogous experiments with pairs of recombinant Pmps or a combination of Pmp and OmcB revealed that all Pmps probably act in an adhesion pathway that is distinct from the OmcB-GAG pathway. Finally, we provide evidence that the Pmps of C. trachomatis and C. pneumoniae exhibit species and tissue specificity. These findings argue for the involvement of C. trachomatis Pmps in the initial phase of infection and suggest that they may interact with a receptor other than the epidermal growth factor receptor recently identified for their counterparts in C. pneumoniae.