Diversity of complement factor B/C2 in the common carp (Cyprinus carpio): three isotypes of B/C2-A expressed in different tissues

Nakao, Minoru; Matsumoto, Momoe; Nakazawa, Mika; Fujiki, Kazuhiro; Yano, Tomoki

doi:10.1016/s0145-305x(01)00083-0

Cited by 46 publications

(19 citation statements)

References 16 publications

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“…3). In teleost fish, the Bf/C2 genes are often duplicated, and one of these genes encodes a protein that, like C2, functions in the classical complement pathway (48,(52)(53)(54). However, upon phylogenetic tree analysis, most of the teleost genes form a monophyletic cluster independent of tetrapod Bf and C2 clusters.…”

Section: Class III Regionmentioning

confidence: 99%

Ancestral Organization of the MHC Revealed in the AmphibianXenopus

Ohta

Goetz

Hossain

et al. 2006

The Journal of Immunology

130

120

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With the advent of the Xenopus tropicalis genome project, we analyzed scaffolds containing MHC genes. On eight scaffolds encompassing 3.65 Mbp, 122 MHC genes were found of which 110 genes were annotated. Expressed sequence tag database screening showed that most of these genes are expressed. In the extended class II and class III regions the genomic organization, excluding several block inversions, is remarkably similar to that of the human MHC. Genes in the human extended class I region are also well conserved in Xenopus, excluding the class I genes themselves. As expected from previous work on the Xenopus MHC, the single classical class I gene is tightly linked to immunoproteasome and transporter genes, defining the true class I region, present in all nonmammalian jawed vertebrates studied to date. Surprisingly, the immunoproteasome gene PSMB10 is found in the class III region rather than in the class I region, likely reflecting the ancestral condition. Xenopus DMα, DMβ, and C2 genes were identified, which are not present or not clearly identifiable in the genomes of any teleosts. Of great interest are novel V-type Ig superfamily (Igsf) genes in the class III region, some of which have inhibitory motifs (ITIM) in their cytoplasmic domains. Our analysis indicates that the vertebrate MHC experienced a vigorous rearrangement in the bony fish and bird lineages, and a translocation and expansion of the class I genes in the mammalian lineage. Thus, the amphibian MHC is the most evolutionary conserved MHC so far analyzed.

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Section: Class III Regionmentioning

confidence: 99%

Ancestral Organization of the MHC Revealed in the AmphibianXenopus

Ohta

Goetz

Hossain

et al. 2006

The Journal of Immunology

130

120

View full text Add to dashboard Cite

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“…The complement system of teleost fish consists of three pathways, making it similar to of the system found in higher vertebrates (Boshra et al, 2004;Nonaka and Smith, 2000). Many complement proteins have been isolated from various teleost species (Holland and Lambris, 2002;Dodds and Petry, 1993;Endo et al, 1998;Yeo et al, 1997), and it has been suggested the complement system of fish may have wider recognition functions than in mammals (Sunyer and Tort, 1995) due to the larger diversity of complement proteins (Nakao et al, 2002).…”

Section: Introductionmentioning

confidence: 98%

RNA-seq profiles from grass carp tissues after reovirus (GCRV) infection based on singular and modular enrichment analyses

Shi

Huang

et al. 2014

Molecular Immunology

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“…A cDNA fragment coding for the 40S ribosomal protein S11 subunit (a positive control) was also amplified using P12 and P13 (Table I) as described elsewhere (41). As shown in Fig.…”

Section: Expression Analysis By Rt-pcrmentioning

confidence: 99%

Two Divergent Isotypes of the Fourth Complement Component from a Bony Fish, the Common Carp (Cyprinus carpio)

Mutsuro

Тanaka

Kato

et al. 2005

The Journal of Immunology

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Duplication and diversification of several complement components is a striking feature of bony fish complement systems. It gives an interesting insight into an evolutionary strategy for the possible enhancement of the repertoire of innate immunity. The present study is aimed at examining diversity in bony fish C4, a member of the thioester-containing complement components. Two diverged cDNA sequences sharing only ∼32% identity at the amino acid level were isolated from the common carp and designated C4-1 and C4-2. C4-1 and C4-2 share a number of C4-like structural signatures, such as the thioester site and a disulfide-linked three-chain structure. Interestingly, they differ at the residue corresponding to the thioester-catalytic histidine, as seen in the human C4A and C4B isotypes, suggesting their distinct substrate specificities in the binding reaction of the thioester. Phylogenetic analysis indicates that the divergence of C4-1 and C4-2 predated the separation of the cartilaginous and bony fish lineages. Genomic Southern hybridization suggests the presence of single copy genes each encoding C4-1 and C4-2 in the carp genome. An activation fragment, C4a, was shown to be released from each isotype in carp serum activated via the classical and/or lectin pathways. Synthetic peptides representing a putative C2 binding site on C4-1 and C4-2 inhibited the classical pathway-mediated hemolytic activity of carp serum in a dose-dependent manner. The results suggest that C4-1 and C4-2 represent two major lineages of C4 that are present in carp serum, have distinct binding specificities, and are functional in the classical/lectin pathways of complement activation.

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Diversity of complement factor B/C2 in the common carp (Cyprinus carpio): three isotypes of B/C2-A expressed in different tissues

Cited by 46 publications

References 16 publications

Ancestral Organization of the MHC Revealed in the AmphibianXenopus

Ancestral Organization of the MHC Revealed in the AmphibianXenopus

RNA-seq profiles from grass carp tissues after reovirus (GCRV) infection based on singular and modular enrichment analyses

Two Divergent Isotypes of the Fourth Complement Component from a Bony Fish, the Common Carp (Cyprinus carpio)

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