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Division of Infectious Diseases, School of Public Health, 235 Earl Warren Hall, University of California, Berkeley, CA 94720, USA. rss@uclink4.berkeley.edu
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.
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