Abstract
Using highly purified elementary bodies of C. trachomatis UW-31 (serotype K), HeLa 229 [human cervical carcinoma] monolayer cultures were found to bind more 32P-labeled chlamydiae after pretreatment with the lectin wheat germ agglutinin. The lectin inhibited competitively when chlamydial association was assayed in the presence of polycations. The 2 effects of wheat germ agglutinin were abolished when N-acetylneuraminic acid (NeuNAc)- or N-acetylglucosamine (GlcNAc)-preincubated wheat germ agglutinin was used. Brief exposure of HeLa cells to neuraminidase abolished the ability to bind the elementary bodies, whether or not polycations were present. At 5.degree. C, but not at 37.degree. C, NeuNAc, GlcNAc and N-acetylgalactosoamine inhibited chlamydial association only in the absence of the polycation DEAE-dextran. Apparently, NeuNAc residues on the plasma membrane are the principal, but not the only, receptors for this strain of C. trachomatis.