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* Departments of Immunology and Microbiology and Medical Biology, University of Southern Denmark, Odense, Denmark;
Department of Animal Breeding and Genetics, Research Center Foulum, Tjele, Denmark; and
Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford, United Kingdom
Collectins are oligomeric molecules with C-type lectin domains
attached to collagen-like regions via 
-helical neck regions. They
bind nonself glycoconjugates on the surface of microorganisms and
inhibit infection by direct neutralization, agglutination, or
opsonization. During the characterization of the gene encoding bovine
CL-43 (43-kDa collectin), we identified a novel collectin-gene. We
report the cloning and partial characterization of the novel collectin
CL-46. The mRNA comprises 1188 nucleotides encoding a protein of 371 aa
with an included leader peptide of 20 residues. CL-46 has two cysteine
residues in the N-terminal segment, a potential
N-glycosylation site in the collagen region, and an
extended hydrophilic loop close to the binding site of the carbohydrate
recognition domain. It is expressed in the thymus, liver, mammary
gland, and tissues of the digestive system. Recombinant CL-46
corresponding to the -helical neck region and the C-type lectin
domain binds preferential
N-acetyl-D-glucoseamine and
N-acetyl-D-mannoseamine. The gene encoding
CL-46 spans 
10 kb and consists of eight exons, with high structural
resemblance to the gene encoding human surfactant protein D. It is
located on the bovine chromosome 28 at position q1.8 together with the
gene encoding conglutinin and CL-43. Several potential thymus-related
cis-regulatory elements were identified in the
5'-upstream sequence, indicating that the expression in thymus may be
modulated by signals involved in T cell
development.
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