Abstract

Collections are a group of multimeric proteins mostly consisting of 9–18 polypeptides organised into either ‘bundle‐of‐tulips’ or ‘X‐like’ overall structures. Each polypeptide contains a short N‐terminal segment followed by a collagen‐like sequence and then by a C‐terminal lectin domain. A collectin molecule is assembled from identical or very similar polypeptides by disulphide bonds at the N‐terminal segment, formation of triple helices in the collagen‐like region and clusters of three lectin domains at the peripheral ends of triple helices. These proteins can bind to sugar residues on microorganisms via the peripheral lectin domains and subsequently interact, via the collagen‐like triple‐helices, with receptor(s) on phagocytes and/or the complement system to bring about the killing and clearance of the targets without the involvement of antibodies. The collectins can also bind to phagocyte receptor(s) to enhance phagocytosis mediated by other phagocytic receptors. Lack, or low levels, of collectin expression can lead to higher susceptibility to infections, especially during childhood when specific immunity has not fully developed. Therefore, the collectins play important roles in the enhancement of innate immunity.