Complement C1q subunit molecules from Xenopus laevis possess conserved function in C1q-immunoglobulin interaction. (February 2020)
- Record Type:
- Journal Article
- Title:
- Complement C1q subunit molecules from Xenopus laevis possess conserved function in C1q-immunoglobulin interaction. (February 2020)
- Main Title:
- Complement C1q subunit molecules from Xenopus laevis possess conserved function in C1q-immunoglobulin interaction
- Authors:
- Yan, Fangfang
Zhou, Enxu
Liu, Shuo
Gao, Along
Kong, Linghe
Li, Bingxi
Tu, Xiao
Guo, Zheng
Mo, Jinfeng
Chen, Meng
Ye, Jianmin - Abstract:
- Abstract: Complement component 1q (C1q), together with C1r and C1s to form C1, recognize and bind immune complex to initiate the classical complement pathway. In this study, C1q subunit molecules ( XlC1qA, XlC1qB, XlC1qC ) were cloned and analyzed from Xenopus laevis ( X. laevis ). The open reading frame (ORF) of XlC1qA is 819 bp of nucleotide sequence encoding 272 amino acids, the ORF of XlC1qB is 711 bp encoding 236 aa, and the XlC1qC is consists of 732 bp encoding 243 aa. The deduced amino acid sequences contain a collagen-like region (CLR), Gly-X-Y repeats in the N-terminus and a C1q family domain at the C-terminus. Phylogenetic analysis revealed that the XlC1qs are clustered with the amphibian clade. Expression analysis indicated that the XlC1qs exhibited constitutive expression in all examined tissues, with the highest expression in liver. Additionally, XlC1q could interact with heat-aggregated mouse IgG and IgM, Xenopus IgM and Nile tilapia IgM, respectively, indicating the functional conservation of XlC1q binding to immunoglobulins. Further, XlC1qs can inhibit C1q-dependent hemolysis of sensitized sheep red blood cells with concentration-dependent manner. These data collectively suggest that the function of C1qs in X. laevis may be conserved in interaction with immunoglobulins, as that of mammals and teleosts. Highlights: The XlC1qA, XlC1qB and XlC1qC genes are cloned and identified in Xenopus laevis. XlC1qA, XlC1qB and XlC1qC are broadly expressed in all examinedAbstract: Complement component 1q (C1q), together with C1r and C1s to form C1, recognize and bind immune complex to initiate the classical complement pathway. In this study, C1q subunit molecules ( XlC1qA, XlC1qB, XlC1qC ) were cloned and analyzed from Xenopus laevis ( X. laevis ). The open reading frame (ORF) of XlC1qA is 819 bp of nucleotide sequence encoding 272 amino acids, the ORF of XlC1qB is 711 bp encoding 236 aa, and the XlC1qC is consists of 732 bp encoding 243 aa. The deduced amino acid sequences contain a collagen-like region (CLR), Gly-X-Y repeats in the N-terminus and a C1q family domain at the C-terminus. Phylogenetic analysis revealed that the XlC1qs are clustered with the amphibian clade. Expression analysis indicated that the XlC1qs exhibited constitutive expression in all examined tissues, with the highest expression in liver. Additionally, XlC1q could interact with heat-aggregated mouse IgG and IgM, Xenopus IgM and Nile tilapia IgM, respectively, indicating the functional conservation of XlC1q binding to immunoglobulins. Further, XlC1qs can inhibit C1q-dependent hemolysis of sensitized sheep red blood cells with concentration-dependent manner. These data collectively suggest that the function of C1qs in X. laevis may be conserved in interaction with immunoglobulins, as that of mammals and teleosts. Highlights: The XlC1qA, XlC1qB and XlC1qC genes are cloned and identified in Xenopus laevis. XlC1qA, XlC1qB and XlC1qC are broadly expressed in all examined tissues. Recombinant XlC1qA, XlC1qB and XlC1qC have the binding ability to heat-aggregated mouse IgM/IgG, Xenopus IgM and Nile tilapia IgM. Recombinant XlC1qA, XlC1qB and XlC1qC inhibit C1q-dependent hemolysis of sensitized sheep red blood cells. … (more)
- Is Part Of:
- Developmental and comparative immunology. Volume 103(2020)
- Journal:
- Developmental and comparative immunology
- Issue:
- Volume 103(2020)
- Issue Display:
- Volume 103, Issue 2020 (2020)
- Year:
- 2020
- Volume:
- 103
- Issue:
- 2020
- Issue Sort Value:
- 2020-0103-2020-0000
- Page Start:
- Page End:
- Publication Date:
- 2020-02
- Subjects:
- Xenopus laevis -- Complement component 1q (C1q) -- Immunoglobulin (Ig) -- C1q-Ig interaction -- Hemolysis
Immunology -- Periodicals
Developmental immunology -- Periodicals
616.079 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0145305X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.dci.2019.103532 ↗
- Languages:
- English
- ISSNs:
- 0145-305X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3579.051000
British Library DSC - BLDSS-3PM
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- 12138.xml