Dropping anchor: Attachment of peptidylarginine deiminase via A-LPS to secreted outer membrane vesicles of Porphyromonas gingivalisGabarrini, G., Heida, R., van Ieperen, N., Curtis, M. A., van Winkelhoff, A. J. & van Dijl, J. M., 12-Jun-2018, In : Scientific Reports. 8, 1, 9 p., 8949.
Research output: Contribution to journal › Article › Academic › peer-review
The periodontal pathogen Porphyromonas gingivalis has been invoked in the autoimmune disease rheumatoid arthritis (RA). This association relates to the peptidylarginine deiminase of P. gingivalis (PPAD), an enzyme capable of citrullinating human proteins and potentially contributing to loss of tolerance to citrullinated proteins in RA. PPAD is both retained in the outer membrane (OM) of P. gingivalis cells and secreted into the extracellular milieu, where it is detected in a soluble form and in association with outer membrane vesicles (OMVs). Recent studies showed that certain P. gingivalis proteins are retained in the OM through modification with an A-type lipopolysaccharide (A-LPS). Here, we investigated the possible involvement of A-LPS modification in the association of PPAD to the OM and OMVs. The results indicate that the OM-and OMV-associated PPAD is A-LPS-modified. The modified PPAD species is of low abundance in particular clinical isolates of P. gingivalis, which is not due to defects in the overall synthesis of A-LPS-modified proteins but, rather, to particular traits of the respective PPAD proteins. Lastly, we show that OMV association protects the A-LPS-modified PPAD from proteolytic degradation. Altogether, our observations show that A-LPS modification contributes to OM(V) sorting and 'protective secretion' of PPAD.
|Number of pages||9|
|Publication status||Published - 12-Jun-2018|
- RHEUMATOID-ARTHRITIS, PERIODONTAL-DISEASE, GLIDING MOTILITY, IX SECRETION, PROTEINS, SYSTEM, VIRULENCE, BACTERIAL, POLYSACCHARIDE, IDENTIFICATION