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 language | English |
|---|---|
| Pages (from-to) | 47-53 |
| Number of pages | 7 |
| Journal | Developmental and Comparative Immunology |
| Volume | 43 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Mar 1 2014 |
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All Science Journal Classification (ASJC) codes
- Immunology
- Developmental Biology
Cite this
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 journal › Article
}
TY - JOUR
T1 - Hagfish C1q
T2 - Its unique binding property
AU - Yamaguchi, Tomokazu
AU - Takamune, Kazufumi
AU - Kondo, Masakazu
AU - Takahashi, Yukinori
AU - Kato-Unoki, Yoko
AU - Nakao, Miki
AU - Sano, Naomi
AU - Fujii, Tamotsu
PY - 2014/3/1
Y1 - 2014/3/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84887952784&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84887952784&partnerID=8YFLogxK
U2 - 10.1016/j.dci.2013.10.009
DO - 10.1016/j.dci.2013.10.009
M3 - Article
C2 - 24201131
AN - SCOPUS:84887952784
VL - 43
SP - 47
EP - 53
JO - Developmental and Comparative Immunology
JF - Developmental and Comparative Immunology
SN - 0145-305X
IS - 1
ER -