A recombinant Chlamydia trachomatis major outer membrane protein binds to heparan sulfate receptors on epithelial cells

摘要: Chlamydial attachment to columnar conjunctival or urogenital epithelial cells is an initial and critical step in the pathogenesis of chlamydial mucosal infections. The major outer membrane protein (MOMP) has been implicated as a putative cytoadhesin; however, direct evidence supporting this hypothesis not reported. function MOMP cytoadhesin was directly investigated by expressing fusion with Escherichia coli maltose binding (MBP-MOMP) studying its interaction human cells. recombinant MBP-MOMP bound specifically HeLa at 4 degrees C but internalized after shifting temperature 37 C. competitively inhibited infectivity viable chlamydiae for cells, indicating that intact bind same host receptor. Heparan sulfate markedly reduced whereas chondroitin had no effect on binding. Enzymatic treatment heparitinase chondroitinase MBP-MOMP. These treatments were also shown reduce Mutant cell lines defective heparan synthesis showed marked reduction less susceptible infection chlamydiae. Collectively, these findings provide strong functions proteoglycans are host-cell receptors which binds.