Identification and characterization of a novel human collectin CL-K1

Microbiol Immunol. 2006;50(12):1001-13. doi: 10.1111/j.1348-0421.2006.tb03868.x.


Collectins are a family of C-type lectins with two characteristic structures, collagen like domains and carbohydrate recognition domains. They recognize carbohydrate antigens on microorganisms and act as host-defense. Here we report the cloning and characterization of a novel collectin CL-K1. RT-PCR analyses showed CL-K1 mRNA is present in all organs. The deduced amino acid sequence and the data from immunostaining of CL-K1 cDNA expressing CHO cells revealed that CL-K1 is expressed as a secreted protein. CL-K1 is found in blood by immunoblotting and partial amino acid analyses. CL-K1 showed Ca(2+)-dependent sugar binding activity of fucose and weakly mannose but not N-acetyl-galactosamine, N-acetyl-glucosamine, or maltose, though mannose-binding lectin (MBL) containing similar amino acid motif. CL-K1 can recognize specially several bacterial saccharides due to specific sugar-binding character. Elucidation of the role of two ancestor collectins of CL-K1 and CL-L1 could lead to see the biological function of collectin family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • CHO Cells
  • Collectins / classification
  • Collectins / genetics*
  • Collectins / isolation & purification*
  • Cricetinae
  • Cricetulus
  • Humans
  • Kidney / chemistry
  • Kidney / metabolism*
  • Molecular Sequence Data


  • Collectins
  • collectin CL-K1, human

Associated data

  • GENBANK/AB119525
  • GENBANK/AB119650
  • GENBANK/AB119651
  • GENBANK/AB119652