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Updated: Jul 30, 2026

Immuno-fluorescence Assay of Leptospiral Surface-exposed Proteins
Published on: July 1, 2011
Heparin-binding outer membrane protein of chlamydiae
R S Stephens1, K Koshiyama, E Lewis
1Division of Infectious Diseases, School of Public Health, 235 Earl Warren Hall, University of California, Berkeley, CA 94720, USA. rss@uclink4.berkeley.edu
Abstract:
As an intracellular pathogen, the mechanism by which Chlamydia invade eukaryotic cells represents a cornerstone to understanding chlamydial biology. The ability of chlamydiae specifically to bind heparan sulphate or heparin and the association of this ability to bind and enter mammalian host cells was approached by searching experimentally for chlamydial outer membrane proteins that bind heparin. The 60 000 molecular weight cysteine-rich outer membrane complex protein, OmcB, bound heparin. The ability of OmcB to bind heparin was supported by mapping the region of the protein with heparin-binding capacity and demonstrating that an OmcB synthetic 20-mer peptide from this region specifically bound heparin. Surface localization of OmcB was shown using monospecific antisera specific to the 20-mer OmcB peptide that bound the surfaces of elementary bodies (EB) and by heparin-binding peptide cross-linking of EB surface proteins.
Insights
Chlamydia
Area of Science:
- Microbiology
- Cell Biology
- Infectious Diseases
Background:
- Chlamydia are obligate intracellular pathogens crucial for understanding host-pathogen interactions.
- Chlamydial invasion of eukaryotic cells is a key aspect of their lifecycle.
- Heparan sulfate and heparin binding are implicated in Chlamydia's entry mechanism.
Purpose of the Study:
- To identify Chlamydia outer membrane proteins responsible for heparin binding.
- To investigate the role of heparin binding in the invasion of mammalian host cells.
Main Methods:
- Screening Chlamydia outer membrane proteins for heparin-binding activity.
- Mapping the heparin-binding region of the identified protein.
- Synthesizing a peptide from the identified region to confirm heparin binding.
- Confirming surface localization of the protein on elementary bodies (EB) using specific antibodies and cross-linking techniques.
Main Results:
- The 60,000 molecular weight cysteine-rich outer membrane complex protein, OmcB, was identified as a heparin-binding protein.
- A specific region within OmcB was mapped for heparin-binding capacity.
- A synthetic 20-mer peptide from this region demonstrated specific binding to heparin.
- Monospecific antisera confirmed OmcB's surface localization on EB, further supported by heparin-binding peptide cross-linking.
Conclusions:
- OmcB is a surface-exposed outer membrane protein of Chlamydia that binds heparin.
- This heparin-binding ability of OmcB likely contributes to Chlamydia's invasion of mammalian host cells.
- Further research into OmcB could reveal novel therapeutic targets for Chlamydia infections.
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