The Lectin Pathway Originates With Host Proteins Binding Microbial Surfaces

Lectins are proteins that recognize and bind to specific carbohydrate targets. (Because the lectin that activates comple ment binds to mannose residues, some authors designate this the MBLectin pathway or mannan-binding lectin pathway.) The lectin pathway, like the alternative pathway, does not depend on antibody for its activation. However, the mechanism is more like that of the classical pathway, because after initiation, it proceeds, through the action of C4 and C2, to produce a C5 convertase (see Figure 13-2).

The lectin pathway is activated by the binding of man-nose-binding lectin (MBL) to mannose residues on glyco-proteins or carbohydrates on the surface of microorganisms including certain Salmonella, Listeria, and Neisseria strains, as well as Cryptococcus neoformans and Candida albicans. MBL is an acute phase protein produced in inflammatory responses. Its function in the complement pathway is similar to that of C1q, which it resembles in structure. After MBL binds to the surface of a cell or pathogen, MBL-associated serine proteases, MASP-1 and MASP-2, bind to MBL. The active complex formed by this association causes cleavage and activation of C4 and C2. The MASP-1 and -2 proteins have structural similarity to C1r and C1s and mimic their activities. This means of activating the C2-C4 components to form a C5 convertase without need for specific antibody binding represents an important innate defense mechanism comparable to the alternative pathway, but utilizing the elements of the classical pathway except for the C1 proteins.

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