Minnow-binding lectin (MBL) is a Member of the collection family of proteins which are characterised by the presence of both a collagenous region and a Wolin domain. MBL was discovered and first isolated from rabbit fiver cytosol in 1978 and subsequently identified in human, rabbit, bovine. rat and mouse sera.. As this lectin-like protein was originally found to he specific for binding mann°. and the official gene symbol is Md. it is  preferably named as MBEs. However. MBL can weakly bind a wide spectrum of oligosaccharides such as N-acetylglucosamine N-acetyl mann.ami ne and l000se> maltose a glucose >a galactose and N-acetylgalactosamine. As most of its sugar targets are not normally exposed on mammalian cellocll surfaces at high densities. it does not usually recognise self structures but is panicularly well suited to interactions with microbial surfaces. Since MBL can bind to so many different sugars it is effectively a universal antibod?. It is now accepted that its complex with MBL-asscciated serine protease (MASP), "MBL-MASP", provides an antibody and Cl-independent pathway for the activation of the classical pathway of complement known as the classical pathway-II or the lecfin pathway. This functional unit plays an important role in opsonophagocric processescontributing in efficient antimicrobial immunity and protection'. A wide range of clinical associations with MBL deficiency amreported'''. Recently reported molecular.now  functional and clinical aspects of MBL am therefore reviewed M the present article.