PUBLICATION
Characterization of C1Q in teleosts: insight into the molecular and functional evolution of C1Q family and classical pathway
- Authors
- Hu, Y.L., Pan, X.M., Xiang, L.X., and Shao, J.Z.
- ID
- ZDB-PUB-100719-38
- Date
- 2010
- Source
- The Journal of biological chemistry 285(37): 28777-28786 (Journal)
- Registered Authors
- Keywords
- Complement, Evolution, Gene structure, Protein structure, Zebra fish
- MeSH Terms
-
- Animals
- Complement C1q/chemistry
- Complement C1q/genetics
- Complement C1q/immunology
- Complement C1q/metabolism*
- Complement Pathway, Classical/physiology*
- Escherichia coli
- Evolution, Molecular*
- Hemolysis
- Humans
- Immunoglobulin G/chemistry
- Immunoglobulin G/genetics
- Immunoglobulin G/immunology
- Immunoglobulin G/metabolism
- Immunoglobulin M/chemistry
- Immunoglobulin M/genetics
- Immunoglobulin M/immunology
- Immunoglobulin M/metabolism
- Phylogeny*
- Recombinant Proteins/chemistry
- Recombinant Proteins/genetics
- Recombinant Proteins/immunology
- Recombinant Proteins/metabolism
- Zebrafish/genetics
- Zebrafish/immunology
- Zebrafish/metabolism*
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics
- Zebrafish Proteins/immunology
- Zebrafish Proteins/metabolism*
- PubMed
- 20615881 Full text @ J. Biol. Chem.
Citation
Hu, Y.L., Pan, X.M., Xiang, L.X., and Shao, J.Z. (2010) Characterization of C1Q in teleosts: insight into the molecular and functional evolution of C1Q family and classical pathway. The Journal of biological chemistry. 285(37):28777-28786.
Abstract
C1qs are key components of the classical complement pathway. They have been well-documented in human and mammals but little is known about their molecular and functional characteristics in fish. In the present study, full length cDNAs of C1qA, C1qB, and C1qC from zebrafish (Danio rerio) were cloned, revealing the conservation of their chromosomal synteny and organization between zebrafish and other species. For functional analysis, the globular heads of C1qA (ghA), C1qB (ghB), and C1qC (ghC) were expressed in Escherichia coli as soluble proteins. Hemolytic inhibitory assays showed that hemolytic activity in carp serum can be significantly inhibited by anti-C1qA, -C1qB, and -C1qC of zebrafish, respectively, indicating that C1qA, C1qB, and C1qC are involved in the classical pathway and are functionally conserved from fish to human. Zebrafish C1qs could also specifically bind to heat-aggregated zebrafish IgM, human IgG, and IgM. The involvement of globular head modules in the C1q-dependent classical pathway demonstrates the structural and functional conservation of these molecules in the classical pathway and their IgM or IgG binding sites during evolution. Phylogenetic analysis revealed that C1qA, C1qB, and C1qC may be formed by duplications of a single copy of C1qB, and that the C1q family is, evolutionarily, closely related to the Emu family. This study improves current understanding of the evolutionary history of the C1q family and C1q-mediated immunity.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping