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 journalArticle

6 Citations (Scopus)

Abstract

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
Volume43
Issue number1
DOIs
Publication statusPublished - Mar 1 2014

Fingerprint

Hagfishes
Sepharose
Edetic Acid
Aptitude
Peptidoglycan
Monosaccharides
Lectins
Lipopolysaccharides
Polymers
Proteins
Complementary DNA
Ligands

All Science Journal Classification (ASJC) codes

  • Immunology
  • Developmental Biology

Cite this

Yamaguchi, T., Takamune, K., Kondo, M., Takahashi, Y., Kato-Unoki, Y., Nakao, M., ... Fujii, T. (2014). Hagfish C1q: Its unique binding property. Developmental and Comparative Immunology, 43(1), 47-53. https://doi.org/10.1016/j.dci.2013.10.009

Hagfish C1q : Its unique binding property. / Yamaguchi, Tomokazu; Takamune, Kazufumi; Kondo, Masakazu; Takahashi, Yukinori; Kato-Unoki, Yoko; Nakao, Miki; Sano, Naomi; Fujii, Tamotsu.

In: Developmental and Comparative Immunology, Vol. 43, No. 1, 01.03.2014, p. 47-53.

Research output: Contribution to journalArticle

Yamaguchi, T, Takamune, K, Kondo, M, Takahashi, Y, Kato-Unoki, Y, Nakao, M, Sano, N & Fujii, T 2014, 'Hagfish C1q: Its unique binding property', Developmental and Comparative Immunology, vol. 43, no. 1, pp. 47-53. https://doi.org/10.1016/j.dci.2013.10.009
Yamaguchi T, Takamune K, Kondo M, Takahashi Y, Kato-Unoki Y, Nakao M et al. Hagfish C1q: Its unique binding property. Developmental and Comparative Immunology. 2014 Mar 1;43(1):47-53. https://doi.org/10.1016/j.dci.2013.10.009
Yamaguchi, Tomokazu ; Takamune, Kazufumi ; Kondo, Masakazu ; Takahashi, Yukinori ; Kato-Unoki, Yoko ; Nakao, Miki ; Sano, Naomi ; Fujii, Tamotsu. / Hagfish C1q : Its unique binding property. In: Developmental and Comparative Immunology. 2014 ; Vol. 43, No. 1. pp. 47-53.
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