Two divergent isotypes of the fourth complement component from a bony fish, the common carp (Cyprinus carpio)

Junichi Mutsuro, Noriyuki Tanaka, Yoko Kato, Alister W. Dodds, Tomoki Yano, Miki Nakao

研究成果: ジャーナルへの寄稿記事

11 引用 (Scopus)

抄録

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 aad/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 seram 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.

元の言語英語
ページ(範囲)4508-4517
ページ数10
ジャーナルJournal of Immunology
175
発行部数7
DOI
出版物ステータス出版済み - 10 1 2005

Fingerprint

Carps
Fishes
Mannose-Binding Lectin Complement Pathway
Classical Complement Pathway
Nucleic Acid Hybridization
Substrate Specificity
Serum
Histidine
Lectins
Innate Immunity
Disulfides
Complementary DNA
Binding Sites
Genome
Amino Acids
Peptides
Genes

All Science Journal Classification (ASJC) codes

  • Immunology

これを引用

Two divergent isotypes of the fourth complement component from a bony fish, the common carp (Cyprinus carpio). / Mutsuro, Junichi; Tanaka, Noriyuki; Kato, Yoko; Dodds, Alister W.; Yano, Tomoki; Nakao, Miki.

:: Journal of Immunology, 巻 175, 番号 7, 01.10.2005, p. 4508-4517.

研究成果: ジャーナルへの寄稿記事

Mutsuro, Junichi ; Tanaka, Noriyuki ; Kato, Yoko ; Dodds, Alister W. ; Yano, Tomoki ; Nakao, Miki. / Two divergent isotypes of the fourth complement component from a bony fish, the common carp (Cyprinus carpio). :: Journal of Immunology. 2005 ; 巻 175, 番号 7. pp. 4508-4517.
@article{8411dcb7168846398aafc82418f98900,
title = "Two divergent isotypes of the fourth complement component from a bony fish, the common carp (Cyprinus carpio)",
abstract = "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 aad/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 seram 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.",
author = "Junichi Mutsuro and Noriyuki Tanaka and Yoko Kato and Dodds, {Alister W.} and Tomoki Yano and Miki Nakao",
year = "2005",
month = "10",
day = "1",
doi = "10.4049/jimmunol.175.7.4508",
language = "English",
volume = "175",
pages = "4508--4517",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "7",

}

TY - JOUR

T1 - Two divergent isotypes of the fourth complement component from a bony fish, the common carp (Cyprinus carpio)

AU - Mutsuro, Junichi

AU - Tanaka, Noriyuki

AU - Kato, Yoko

AU - Dodds, Alister W.

AU - Yano, Tomoki

AU - Nakao, Miki

PY - 2005/10/1

Y1 - 2005/10/1

N2 - 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 aad/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 seram 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.

AB - 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 aad/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 seram 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.

UR - http://www.scopus.com/inward/record.url?scp=25444469379&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=25444469379&partnerID=8YFLogxK

U2 - 10.4049/jimmunol.175.7.4508

DO - 10.4049/jimmunol.175.7.4508

M3 - Article

C2 - 16177094

AN - SCOPUS:25444469379

VL - 175

SP - 4508

EP - 4517

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 7

ER -