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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

Molecular Microbiology

|May 22, 2001

Summary

Chlamydia

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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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