The isolation of a lectin-like molecule from Corynebacterium parvum (NCTC 10390).

A mannose specific lectin has been isolated by affinity chromatography from the cell wall of C. parvum. Polyacrylamide gel electrophoresis indicates that the lectin molecules lie in the molecular weight range 57,000--72,000. It appears that C. parvum like E. coli and salmonellae express lectins that bind to cells expressing mannose in their membranes. This may partly account for the interaction between C. parvum and the macrophage leading to the various immunological phenomena associated with C. parvum administration.