Host passage-dependent wheat germ agglutinin-binding proteins of Chlamydia trachomatis

Wheat germ agglutinin (WGA)-binding proteins in the highly purified elementary bodies (EB) of Chlamydia trachomatis were detected by an ELISA-like assay of immobilized EB. Trypsin-sensitivity of the WGA-binding moieties was detected only in the chlamydiae grown in HeLa cells. A nonionic detergent, beta-octyl-D-glucopyranoside (OG), was used to extract proteins from the purified EB. Proteins in the extract were resolved by SDS-PAGE and probed with 125I-labelled WGA. Several proteins reacted with WGA in a specific manner. Some of these WGA-binding proteins in the EB of serovars L1 and E exhibited altered molecular mass after adaptation in the two alternate hosts, HeLa and McCoy cells. These results suggest that WGA-binding proteins exist in chlamydiae.