Hagfish C1q: Its unique binding property

Tomokazu Yamaguchi, Kazufumi Takamune, Masakazu Kondo, Yukinori Takahashi, Yoko Kato-Unoki, Miki Nakao, Naomi Sano, Tamotsu Fujii

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


Hagfish C1q (HaC1q) was identified and characterized as a pattern-recognition molecule (PRM) in the hagfish complement system. The serum from hagfish, Eptatretus burgeri, was applied to a GlcNAc-agarose column and eluted sequentially with GlcNAc and EDTA. Four (31, 27, 26, and 19kDa) and one (26kDa) proteins were detected as bound molecules in the GlcNAc- and the EDTA-eluates, respectively. Among these, the 26kDa protein from the EDTA eluate was found to be a homologue of mammalian C1q through cDNA analysis. HaC1q had an ability to bind to various microbes in a Ca2+-dependent manner and its target ligands on the microbes were lipopolysaccharide, lipoteichoic acid, and peptidoglycan. The binding of HaC1q to GlcNAc-agarose was not inhibited by an excess amount of monosaccharide such as GlcNAc. While HaC1q bound to Sepharose 6B with a matrix of GlcNAc-agarose (polymer of agarobiose), it did not bind to Sepharose 4B that contained lower concentration of agarobiose than Sepharose 6B. Therefore, the target of HaC1q on GlcNAc-agarose was concluded to be agarobiose and high density of the target moiety seemed to be required for the stable binding. This finding was in accordance with the known behavior of other lectins involved in the complement system. We have concluded that HaC1q recognizes agarobiose-like structures present on the surface of microbes and acts as a pattern-recognition molecule in the process for elimination of invading microbes.

Original languageEnglish
Pages (from-to)47-53
Number of pages7
JournalDevelopmental and Comparative Immunology
Issue number1
Publication statusPublished - Mar 2014

All Science Journal Classification (ASJC) codes

  • Immunology
  • Developmental Biology


Dive into the research topics of 'Hagfish C1q: Its unique binding property'. Together they form a unique fingerprint.

Cite this