A sialic acid-binding lectin that agglutinates a variety of erythrocytes and bacteria and react with sialoconjugates and purified lipopolysaccharides from marine vibrios has been affinity purified from hemolymph of the horse mussel Modiolus modiolus using Bovine submaxillary mucin conjugated to CNBr-activated Sepharose 4B. The lectin demonstrated heterogeneous activity, and at least two main entities were partially characterized, and are referred to as modiolin H and modiolin E activities for the agglutination of human and horse (equine) erythrocytes, respectively. Only modiolin E activity required calcium ions for hemagglutination. The M. modiolus lectin was mainly specific for NeuAc, although the lectin demonstrated a broader range of specificity, similarly to the Limulus polyphemus lectin. The purified lectin was a glycoprotein, and in the native state existed as aggregates with M-r in the range of 100-1,300 kDa as observed by gradient-gel electrophoresis and gel filtration on Biogel and Superose. SDS-PAGE under reducing conditions revealed three subunits of M-r 14, 17.5 and 20 kDa. Various marine bacteria adsorbed the hemagglutinating activities of the M. modiolus lectin. Purified LPS preparations from various pathogenic marine vibrios were also effective inhibitors, in particular for modiolin E activity. These results indicate that the lectin play a role in recognition of bacteria. (C) 1997 Elsevier Science Inc.
