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Bovine Collectins: Role in Health and Disease

ABSTRACT: Mammalian collectins play key roles in innate immunity, health and disease. These have been well studied in humans and other mammalian species, but much has still to be learned about the bovine collectins and the role they may play in the health and disease in cattle which have significant economic implications to the agricultural and food industries. This chapter focuses on the bovine collectins, which are important innate immune molecules and play a key role in immunoregulation and protection against pathogens. Like other mammalian collectins, they all have a related structure comprised of an N-terminal triple-helical collagen-like region and a ligand binding C-terminal C-type lectin domain. The bovine collectins are able to recognise and bind to complex glycoconjugates, particularly on the surface of microbes, neutralising infection, enhancing clearance by phagocytes and modulating immune response. Here, we will review the bovine collectins, surfactant proteins A (SP-A) and D (SP-D), mannose binding lectins (MBL-A and MBL-C), conglutinin (CGN), collectin 43 (CL-43) and collectin 46 (CL-46), and their role in bovine immunity and disease. We will particularly focus on the structural, functional and anti-microbial roles of these collectins with an additional focus on genetic polymorphisms in their genes and predisposition to infectious diseases in the bovine host. In the absence of specific data on the bovine host, findings from studies with other mammalian collectins will be discussed with respect to bovine health and disease.

SUBMITTER: Tsolaki A

PROVIDER: S-EPMC7972501 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Collectin-43 (CL-43) is a recently described bovine plasma protein containing both collagenous regions and C-type-lectin domains [Holmskov, Teisner, Willis, Reid and Jensenius (1993) J. Biol. Chem. 268, 10120-10125; Lim, Willis, Reid, Lu, Laursen, Jensenius and Holmskov (1994) J. Biol. Chem. 269, 11820-11824]. CL-43 was purified by affinity chromatography on mannan-Sepharose. On SDS/PAGE under reducing conditions the purified lectin showed a double band at about 43 kDa, with the upper band representing the intact molecule and the lower band a truncated form that lacked the N-terminal nine amino acid residues. Under non-reducing conditions, only one band was seen at 120 kDa. Analytical gel chromatography and sucrose-density-gradient centrifugation of the purified molecule, showed a Stokes radius of 9.1 +/- 0.3 nm (91 +/- 3 A) and a sedimentation coefficient (s20,w) of 3.6 +/- 0.1 S. These values correspond to a molecular mass of 119-138 kDa under non-denaturing condition in solution. The frictional coefficient (f/f0) was 2.7, indicating extreme elongation due to the collagenous segment. Only monomer subunits, with 37.4 +/- 1.7-nm-long rods, were seen by electron microscopy. These findings indicate that CL-43, in contrast with the other circulating collectins, is found only as a single subunit composed of three polypeptide chains. Two-dimensional gel electrophoresis showed that CL-43 has two isoforms, with pI values of 4.9 and 5.3, corresponding to the native form and the truncated form of the molecule respectively. CL-43, like conglutinin, lung surfactant protein A and mannan-binding protein (MBP), was shown to bind to the collectin receptor. Bovine MBP caused the activation of the complement system as revealed by the deposition of complement component C4 upon incubation of diluted serum in wells containing MBP bound to solid-phase mannan. CL-43, lung surfactant protein D (SP-D) and conglutinin showed no complement-activating properties under the same conditions. Conglutinin binds fluid- and solid-phase iC3b, while CL-43 and MBP do not show such reactivity.

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Bovine Collectins: Role in Health and Disease

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