Mannan-binding lectin Mannan-binding lectin Mannose-binding lectin (MBL), also called mannose-binding protein or mannan-binding protein (MBP), is a lectin that is instrumental in innate immunity via the lectin pathway. MBL has an oligomeric structure (400-700 kDa), built of subunits that contain three presumably identical peptide chains of about 30 kDa each. Although MBL can form several oligomeric forms, there are indications that dimers and trimers are not biologically active and at least a tetramer form is needed for activation of complement. Human MBL2 gene is located on chromosome 10q11.2-q21. Mice have two homologous genes, but in human the first of them was lost.
Lectin their particular high specificity for foreign glycoconjugates (e.g. those of fungi, invertebrates, and animals) and used in biomedicine for blood cell testing and in biochemistry for fractionation. Although they were first discovered more than 100 years ago in plants, now lectins are known to be present throughout nature. It is generally believed that the earliest description of a lectin was given by Peter Hermann Stillmark in his doctoral thesis presented in 1888 to the University of Dorpat. Stillmark isolated ricin, an extremely toxic hemagglutinin, from seeds of the castor plant ("Ricinus communis"). The first lectin to be purified on a