Collectins: Collectors of microorganisms for the innate immune system
- 1 June 1997
- Vol. 19 (6), 509-518
- https://doi.org/10.1002/bies.950190610
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.Keywords
This publication has 73 references indexed in Scilit:
- Biosynthesis of human ficolin, an Escherichia coli‐binding protein, by monocytes: comparison with the synthesis of two macrophage‐specific proteins, C1q and the mannose receptorImmunology, 1996
- The collectins in innate immunityCurrent Opinion in Immunology, 1996
- Collectins: collagenous C-type lectins of the innate immune defense systemImmunology Today, 1994
- Gene Organization and 5′-Flanking Region Sequence of Conglutinin: A C-Type Mammalian Lectin Containing a Collagen-like DomainBiochemical and Biophysical Research Communications, 1994
- Biology of Animal LectinsAnnual Review of Cell Biology, 1993
- Structural similarity between lung surfactant protein D and conglutininEuropean Journal of Biochemistry, 1993
- Engineering galactose-binding activity into a C-type mannose-binding proteinNature, 1992
- Ontogeny of surfactant apoprotein D, SP-D, in the rat lungBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1991
- Macromolecular organization of natural and recombinant lung surfactant protein SP 28–36Journal of Molecular Biology, 1988
- Increases in the 35kDa surfactant‐associated protein and its mRNA following in vivo dexamethasone treatment of fetal and neonatal ratsElectrophoresis, 1987