Albany, NY -- (SBWire) -- 07/05/2018 --Recently, there has been rising interest in mannose-binding lectin (MBL) that is chiefly a liver-derived collagen like serum protein. This is partially due to its central role as a recognition molecule in the complement system. In addition, it has also created interest because of the potential clinical implications of genetically determined differences in MBL oligomerization and serum level between individuals. The discovery of MBL may be traced down back after the Second World War, when it was discovered that factors in non-immune bovine and murine serums could inhibit influenza virus-induced haemagglutination that leads to influenza virus neutralization.

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Repetition of these seminal findings has taken place and it is observed that atleast one of these factors can be MBL. The clinical interest in MBL originates from an observation made 40 years ago when serum-dependent defect of phagocytosis on yeast particles was described.

Mannan-binding lectin is a vital component of the innate immune system. MBL consists of an oligomeric structure which contains three most likely identical peptide chains of 30kDa each. Even though MBL can form several oligomeric forms, some indications presume that trimers and dimers are not always biologically active and need a tetramer form to activate the complement. It helps binding of sugar structure on microorganism and on fading host cells. It is one of the four recognized mediators. These mediators initiate the activation of the component system through the lectin pathway.

Oligomeric mannose belongs to the class of collectins in the C type lectin superfamily. It function is similar to pattern recognition in the first line of defence in the pre-immune host. It recognizes carbohydrate patterns, set up on the surface of an enormous number of pathogenic microorganisms that include virus, bacteria, fungi and protozoa.

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The lectin pathway of the complement system is activated when the MBL binds to a micro-organism. Recent studies have verified that MBL is capable of recognizing carbohydrate structures from both altered self and infectious agents. This binding specificity confers upon MBL the capability to function as a defense factor that is dynamic not only against infectious agents but also against cells and molecules abnormally produced in the host. The recognition of the final targets may be of significance for the host to become accustomed to abnormal physiological conditions.