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. 1997 May 5;185(9):1557–1564. doi: 10.1084/jem.185.9.1557

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Binding specificity of OpaC bacteria for both heparan sulfate and CD66 receptors. OpaC GC were incubated with wild-type CHO-K1 cells and the isogenic mutants 745 and 677 lacking surface heparan sulfate. OpaC GC adhered to CHO-K1 cells, but not the 745 and 677 mutants (A). (B) pGEM, pEXA, and pEXC were incubated with HeLa-CGM1a cells in RPMI 1640 medium for 4.5 h. The adherent and intracellular E. coli were distinguished by incubation with gentamicin. Only pEXC was recovered in large numbers after gentamicin treatment, although both pEXA and pEXC adhered to the HeLa-CGM1a.

Binding specificity of OpaC bacteria for both heparan sulfate and CD66 receptors. OpaC GC were incubated with wild-type CHO-K1 cells and the isogenic mutants 745 and 677 lacking surface heparan sulfate. OpaC GC adhered to CHO-K1 cells, but not the 745 and 677 mutants (A). (B) pGEM, pEXA, and pEXC were incubated with HeLa-CGM1a cells in RPMI 1640 medium for 4.5 h. The adherent and intracellular E. coli were distinguished by incubation with gentamicin. Only pEXC was recovered in large numbers after gentamicin treatment, although both pEXA and pEXC adhered to the HeLa-CGM1a.