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Proteomic analysis of the outer membrane of Protochlamydia amoebophila elementary bodies

Lookup NU author(s): Dr Eva Heinz

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Abstract

Chlamydiae are obligate intracellular bacteria, comprising some of the most important bacterial pathogens of animals and humans. During their unique developmental cycle they have to attach to and enter their eukaryotic host cells, a process mediated by proteins in the chlamydial outer membrane. So far the only experimental data for chlamydial outer membrane proteins are available from members of the Chlamydiaceae, a family comprising exclusively human and animal pathogens. To get further insights into the evolution of the protein composition of the chlamydial outer membrane and into host-dependent differences, we performed an extensive experimental analysis of outer membrane fractions of Protochlamydia amoebophila elementary bodies, which constitute the infectious form of this non-pathogenic member of the Chlamydiae that thrives as a symbiont in Acanthamoeba spp. We used 1-D and 2-DE in combination with MALDI-TOF, MALDI-TOF/TOF and nanoLC-ESI-MS/MS, and compared our experimental results with a previously published in silico analysis of chlamydial outer membrane proteins. This resulted in the identification of 38 proteins supported by both studies and therefore very likely to be located in the P. amoebophila outer membrane. The obtained experimental data provide the first comprehensive overview of outer membrane proteins of a chlamydial organism outside the Chlamydiaceae. They reveal both fundamental differences and convergent evolution between pathogenic and symbiotic chlamydiae.

Publication metadata

Author(s): Heinz E, Pichler P, Heinz C, den Camp HJMO, Toenshoff ER, Ammerer G, Mechtler K, Wagner M, Horn M

Publication type: Article

Publication status: Published

Journal: Proteomics

Year: 2010

Volume: 10

Issue: 24

Pages: 4363-4376

Print publication date: 23/11/2010

ISSN (print): 1615-9853

ISSN (electronic): 1615-9861

Publisher: Wiley - VCH Verlag GmbH & Co. KGaA

URL: http://dx.doi.org/10.1002/pmic.201000302

DOI: 10.1002/pmic.201000302

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