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Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle
Nick M Wheelhouse1, Michelle Sait, Kevin Aitchison
1Moredun Research Institute, Edinburgh, Midlothian, United Kingdom. nick.wheelhouse@moredun.ac.uk
Plos One
|November 13, 2012
Summary
The PmpD protein in Chlamydia abortus (Pmp18D) is cleaved on the cell surface, similar to other Chlamydia species. However, cleavage patterns are species-specific, and the PmpD function remains unknown.
Area of Science:
- Microbiology
- Protein biochemistry
- Chlamydia research
Background:
- Chlamydia species utilize a unique family of autotransporter proteins called Polymorphic Membrane Proteins (Pmps).
- All Chlamydia species encode a single pmpD gene, and PmpD is known to be proteolytically cleaved on the cell surface in C. trachomatis and C. pneumoniae.
Purpose of the Study:
- To investigate the cleavage patterns of the PmpD protein in the animal pathogen Chlamydia abortus, referred to as Pmp18D.
Main Methods:
- Proteomic techniques utilizing region-specific antibodies against Pmp18D.
- Clustering analysis of PmpD proteins.
Main Results:
- Pmp18D undergoes cell surface cleavage, yielding a 100 kDa N-terminal product and a 60 kDa C-terminal protein.
- The N-terminal product is further processed into 84, 76, and 73 kDa fragments.
- Chlamydia abortus Pmp18D clusters with PmpD proteins from C. psittaci, C. felis, and C. caviae.
Conclusions:
- C. abortus Pmp18D exhibits cell surface proteolytic processing analogous to C. trachomatis and C. pneumoniae PmpD.
- Cleavage patterns of PmpD are species-specific, with limited sequence conservation across the Chlamydia genus.
- The functional significance of PmpD in Chlamydia remains undetermined due to the absence of conserved domains.
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