Abstract
Ficolins are members of the collectin family of proteins which are able to recognize pathogen-associated molecular pattern (PAMP) on microbial surfaces. Upon binding to their specific PAMP, ficolins may trigger activation of the immune system by either binding to cellular receptors for collectins or by initiating activation of complement via the lectin pathway. For the latter, the human ficolins ...
Abstract
Ficolins are members of the collectin family of proteins which are able to recognize pathogen-associated molecular pattern (PAMP) on microbial surfaces. Upon binding to their specific PAMP, ficolins may trigger activation of the immune system by either binding to cellular receptors for collectins or by initiating activation of complement via the lectin pathway. For the latter, the human ficolins (i.e. L-, H- and M-ficolin) and murine ficolin-A were shown to associate with the lectin pathway-specific serine protease MBL-associated serine protease-2 (MASP-2) and catalyse its activation which in turn activates C4 and C4b-bound C2 to generate the C3 convertase C4b2a. There is mounting evidence underlining the lectin nature of ficolins with a wide range of carbohydrate moieties recognized on microbial surfaces. However, not all members of the ficolin family appear to act as lectin pathway recognition components. For example, murine ficolin-B does not associate with MASP-2 and appears to be absent in plasma and other humoral fluids. Its stringent cellular localization points to other functions within the immune response, possibly acting as an intracellular scavenger to target and facilitate clearance of PAMP-bearing debris. When comparing ficolin orthologues from different species, it appears evident that human, murine, and porcine ficolins differ in many aspects, a specific point that we aim to address in this review. (C) 2007 Elsevier GmbH. All rights reserved.
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