Identification of a concanavalin A-binding antigen of the cell surface ofSporothrix schenckii

Sporothrix schenckii (1099-18) cell wall peptido-rhamnomannan (CWPR) was fractionated by affinity chromatography with Concanavalin A. The Con A-bound and Con A-unbound fractions were probed with an anti-S. schenckii rabbit serum. We identified within the Con A-bound fraction three main antigens with approximate molecular weights of 84, 70 and 58 kDa. Glycopeptide beta-elimination reduced rabbit antiserum reactivity for the 84 kDa antigen (gp84) with concomittant enhanced reactivity for the 70 kDa antigen (gp70). By Western blot with Con A-HRP conjugate we demonstrated that gp84 strongly reacted with this lectin and this was the predominant antigen identified. The gp84 antigen was also demonstrated to be present on other S. schenckii strains.