Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle

Wheelhouse, Nick M; Sait, Michelle; Aitchison, Kevin; Livingstone, Morag; Wright, Frank; McLean, Kevin; Inglis, Neil F; Smith, David G E; Longbottom, David

Abstract

BACKGROUND: Chlamydia possess a unique family of autotransporter proteins known as the Polymorphic membrane proteins (Pmps). While the total number of pmp genes varies between Chlamydia species, all encode a single pmpD gene. In both Chlamydia trachomatis (C. trachomatis) and C. pneumoniae, the PmpD protein is proteolytically cleaved on the cell surface. The current study was carried out to determine the cleavage patterns of the PmpD protein in the animal pathogen C. abortus (termed Pmp18D). METHODOLOGY/PRINCIPAL FINDINGS: Using antibodies directed against different regions of Pmp18D, proteomic techniques revealed that the mature protein was cleaved on the cell surface, resulting in a100 kDa N-terminal product and a 60 kDa carboxy-terminal protein. The N-terminal protein was further processed into 84, 76 and 73 kDa products. Clustering analysis resolved PmpD proteins into three distinct clades with C. abortus Pmp18D, being most similar to those originating from C. psittaci, C. felis and C. caviae. CONCLUSIONS/SIGNIFICANCE: This study indicates that C. abortus Pmp18D is proteolytically processed at the cell surface similar to the proteins of C. trachomatis and C. pneumoniae. However, patterns of cleavage are species-specific, with low sequence conservation of PmpD across the genus. The absence of conserved domains indicates that the function of the PmpD molecule in chlamydia remains to be elucidated.

Citation

Wheelhouse, N. M., Sait, M., Aitchison, K., Livingstone, M., Wright, F., McLean, K., …Longbottom, D. (2012). Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle. PLOS ONE, 7, Article e49190. https://doi.org/10.1371/journal.pone.0049190

• Journal Article Type: Article
• Acceptance Date: Oct 5, 2012
• Publication Date: Nov 8, 2012
• Deposit Date: Jul 21, 2016
• Publicly Available Date: Jan 30, 2020
• Journal: PLoS One
• Print ISSN: 1932-6203
• Electronic ISSN: 1932-6203
• Publisher: Public Library of Science
• Peer Reviewed: Peer Reviewed
• Volume: 7
• Article Number: e49190
• DOI: https://doi.org/10.1371/journal.pone.0049190
• Keywords: Chlamydia trachomatis, Chlamydia, Sequence motif analysis, Immunoprecipitation, Peptides, amino acid sequence, Chlamydophila pneumoniae, Matrix-assisted laser desorption ionization time-of-flight mass spectrometry, sis Chlamydophila pneumoniae Matri
• Public URL: http://researchrepository.napier.ac.uk/Output/304758
• Related Public URLs: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3493501/pdf/pone.0049190.pdf