Interplay between invertebrate C3a with vertebrate macrophages: Functional characterization of immune activities of amphioxus C3a

Gao, Zhan; Li, Mengyang; Wu, Jie; Zhang, Shicui

doi:10.1016/j.fsi.2013.07.049

Cited by 26 publications

(6 citation statements)

References 49 publications

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“…A C3a-like peptide has been shown to mediate the chemotaxis of hemocytes in Ciona intestinalis (Pinto et al., 2003) and Pyura stolonifera (Raftos et al., 2003). The activated fragments of C3 (C3a and C3b) are also involved in the activation of macrophages and mastocytes (Gao et al., 2013).…”

Section: Discussionmentioning

confidence: 99%

Clam Genome Sequence Clarifies the Molecular Basis of Its Benthic Adaptation and Extraordinary Shell Color Diversity

et al. 2019

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SummaryRuditapes philippinarum is an economically important bivalve with remarkable diversity in its shell coloration patterns. In this study, we sequenced the whole genome of the Manila clam and investigated the molecular basis of its adaptation to hypoxia, acidification, and parasite stress with transcriptome sequencing and an RNA sequence analysis of different tissues and developmental stages to clarify these major issues. A number of immune-related gene families are expanded in the R. philippinarum genome, such as TEP, C3, C1qDC, Hsp70, SABL, and lysozyme, which are potentially important for its stress resistance and adaptation to a coastal benthic life. The transcriptome analyses demonstrated the dynamic and orchestrated specific expression of numerous innate immune-related genes in response to experimental challenge with pathogens. These findings suggest that the expansion of immune- and stress-related genes may play vital roles in resistance to adverse environments and has a profound effect on the clam's adaptation to benthic life.

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Section: Discussionmentioning

confidence: 99%

Clam Genome Sequence Clarifies the Molecular Basis of Its Benthic Adaptation and Extraordinary Shell Color Diversity

et al. 2019

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“…These results suggested that interaction of rPoC3a with target bacteria probably played a role in anti-bacterial immunity. In mammals, C3a has been shown to induce chemotaxis for eosinophils and mast cells, and promote the inflammation in immune response (36). In teleost, previous study has proved that recombinant C3a stimulated chemotaxis of macrophages (36).…”

Section: Discussionmentioning

confidence: 99%

“…In mammals, C3a has been shown to induce chemotaxis for eosinophils and mast cells, and promote the inflammation in immune response (36). In teleost, previous study has proved that recombinant C3a stimulated chemotaxis of macrophages (36). In mammals, C3a performed biological activity via binding to C3a receptors (C3aR), and C3a-C3aR interactions initiate chemotaxis via a C3aR-independent mechanism (79).…”

Section: Discussionmentioning

confidence: 99%

“…In rainbow trout and gilthead sea bream, mature C3 has been purified from serum (34,35), however, the function of C3 is less known in fish. In Branchiostoma japonicum, recombinant C3a can stimulate chemotaxis of macrophages, and enhance phagocytosis and respiratory burst of macrophage (36). In rainbow trout, C3a is also reported to enhance phagocytosis of head kidney leukocytes (37).…”

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confidence: 99%

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Complement C3 and Activated Fragment C3a Are Involved in Complement Activation and Anti-Bacterial Immunity

Jia

2022

Front. Immunol.

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In the complement system, C3 is a central component in complement activation, immune defense and immune regulation. In all pathways of complement activation, the pivotal step is conversion of the component C3 to C3b and C3a, which is responsible to eliminate the pathogen and opsonization. In this study, we examined the immunological properties of C3 and its activated fragment C3a from Japanese flounder (Paralichthys olivaceus) (PoC3 and PoC3a), a teleost species with important economic value. PoC3 is composed of 1655 amino acid residues, contains the six domains and highly conserved GCGEQ sequence of the C3 family. We found that PoC3 expression occurred in nine different tissues and was upregulated by bacterial challenge. In serum, PoC3 was able to bind to a broad-spectrum of bacteria, and purified native PoC3 could directly kill specific pathogen. When PoC3 expression in Japanese flounder was knocked down by siRNA, serum complement activity was significantly decreased, and bacterial replication in fish tissues was significantly increased. Recombinant PoC3a (rPoC3a) exhibited apparent binding capacities to bacteria and Japanese flounder peripheral blood leukocytes (PBL) and induce chemotaxis of PBL. Japanese flounder administered rPoC3a exhibited enhanced resistance against bacterial infection. Taken together, these results indicate that PoC3 is likely a key factor of complement activation, and PoC3 and PoC3a are required for optimal defense against bacterial infection in teleost.

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“…The complement a-protein subunit is produced from the ANATO domain, which contains six conserved cysteine residues and one cleavage site ( 35 ). The convertase cleavage site of the ANATO region (L-R) was conserved across most vertebrates ( 35 , 44 ) and was missing from the sea cucumber ( A. japonicus , R-R) ( 20 ), Ciona ( C. intestinalis , Q-G-R) ( 43 ) and sea squirt ( Halocynthia roretzi , T-S-R) ( 52 ). Nonetheless, although the L-R site was missing in cnidaria, protostomes and invertebrate deuterostomes LC-MS of razor clam C3-like revealed cleavage occurred at non-consensus sites (e.g V-N-R, R-N-R) to generate the a and b-protein subunit.…”

Section: Discussionmentioning

confidence: 99%

Domain-Dependent Evolution Explains Functional Homology of Protostome and Deuterostome Complement C3-Like Proteins

Peng

Cardoso

et al. 2022

Front. Immunol.

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Complement proteins emerged early in evolution but outside the vertebrate clade they are poorly characterized. An evolutionary model of C3 family members revealed that in contrast to vertebrates the evolutionary trajectory of C3-like genes in cnidarian, protostomes and invertebrate deuterostomes was highly divergent due to independent lineage and species-specific duplications. The deduced C3-like and vertebrate C3, C4 and C5 proteins had low sequence conservation, but extraordinarily high structural conservation and 2-chain and 3-chain protein isoforms repeatedly emerged. Functional characterization of three C3-like isoforms in a bivalve representative revealed that in common with vertebrates complement proteins they were cleaved into two subunits, b and a, and the latter regulated inflammation-related genes, chemotaxis and phagocytosis. Changes within the thioester bond cleavage sites and the a-subunit protein (ANATO domain) explained the functional differentiation of bivalve C3-like. The emergence of domain-related functions early during evolution explains the overlapping functions of bivalve C3-like and vertebrate C3, C4 and C5, despite low sequence conservation and indicates that evolutionary pressure acted to conserve protein domain organization rather than the primary sequence.

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Interplay between invertebrate C3a with vertebrate macrophages: Functional characterization of immune activities of amphioxus C3a

Cited by 26 publications

References 49 publications

Clam Genome Sequence Clarifies the Molecular Basis of Its Benthic Adaptation and Extraordinary Shell Color Diversity

Clam Genome Sequence Clarifies the Molecular Basis of Its Benthic Adaptation and Extraordinary Shell Color Diversity

Complement C3 and Activated Fragment C3a Are Involved in Complement Activation and Anti-Bacterial Immunity

Domain-Dependent Evolution Explains Functional Homology of Protostome and Deuterostome Complement C3-Like Proteins

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