Bacterial agglutination by the sialic acid specific serum lectin from Macrobrachium rosenbergii

Humoral defence factors in Indian river prawn, Macrobrachium malcolmsonii

“…The agglutinating capacity of serum of M. rosenbergii with Aeromonas sp. [4] and F. indicus with Vibrio sp. and Pseudomonas sp.…”

“…A variety of lectins including bacterial agglutinins [4] and haemagglutinins [5,6] that agglutinated a wide range of vertebrate erythrocytes have been purified and/or characterised from haemolymph of crustaceans. Characterising a natural haemagglutinin in Fenneropenaeus indicus, Maheswari et al [7] demonstrated the ability of the protein to agglutinate human red blood cells with an equal degree of reactivity to human blood group types, mouse, buffalo, rabbit, rat, sheep, goat and ox erythrocytes but none for horse red blood cells.…”

Dietary administration of bovine lactoferrin influences the immune ability of the giant freshwater prawn Macrobrachium rosenbergii (de Man) and its resistance against Aeromonas hydrophila infection and nitrite stress

“…Previous studies have shown that haemagglutinins in the sera of a few species of prawns and crayfish selectively agglutinate Gram-negative bacteria [47]. Vazquez et al [48] showed bacterial agglutinin in M. rosenbergii to agglutinate Bacillus cereus and Aeromonas sp. This lectin also agglutinates other types of bacteria such as Pasteurella haemolytica bio-type A (capsular serotype 12), several serotypes from P. multocida and Staphylococcus aureus and to a lesser extent E. coli and Salmonella arizona.…”

Purification and Partial Characterization of a 32-Kilodalton Sialic Acid-Specific Lectin from Aspergillus fumigatus

“…Among the compounds tested, only NANA and the sialoglycoproteins inhibited the lectin activity. Sialic acids, which are often found as terminal sugars of glycoconjugates, play an important role in many biological mechanisms (17,33,34,43,44). In a previous report, it was demonstrated that NANA and sialyl lactose inhibited the binding of laminin and fibrinogen to A. fumigatus conidia (3), suggesting an interaction mediated by a sialic acid-specific lectin of the conidial wall.…”