Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteins
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.1/18274 |
Resumo: | 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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Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteinsConserved domainFunctional homologuesParallel evolutionComplement C3C4C5 familyC3-like protein a-subunitComplement 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.Frontiers Media SASapientiaPeng, MaoxiaoLi, ZhiCardoso, JoãoNiu, DonghongLiu, XiaojunDong, ZhiguoLi, JialePower, Deborah2022-09-21T13:33:25Z2022-032022-03-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/18274eng1664-322410.3389/fimmu.2022.840861info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-24T10:30:30Zoai:sapientia.ualg.pt:10400.1/18274Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:08:04.731220Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteins |
title |
Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteins |
spellingShingle |
Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteins Peng, Maoxiao Conserved domain Functional homologues Parallel evolution Complement C3 C4 C5 family C3-like protein a-subunit |
title_short |
Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteins |
title_full |
Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteins |
title_fullStr |
Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteins |
title_full_unstemmed |
Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteins |
title_sort |
Domain-dependent evolution explains functional homology of protostome and deuterostome complement C3-like proteins |
author |
Peng, Maoxiao |
author_facet |
Peng, Maoxiao Li, Zhi Cardoso, João Niu, Donghong Liu, Xiaojun Dong, Zhiguo Li, Jiale Power, Deborah |
author_role |
author |
author2 |
Li, Zhi Cardoso, João Niu, Donghong Liu, Xiaojun Dong, Zhiguo Li, Jiale Power, Deborah |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Peng, Maoxiao Li, Zhi Cardoso, João Niu, Donghong Liu, Xiaojun Dong, Zhiguo Li, Jiale Power, Deborah |
dc.subject.por.fl_str_mv |
Conserved domain Functional homologues Parallel evolution Complement C3 C4 C5 family C3-like protein a-subunit |
topic |
Conserved domain Functional homologues Parallel evolution Complement C3 C4 C5 family C3-like protein a-subunit |
description |
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. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-09-21T13:33:25Z 2022-03 2022-03-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.1/18274 |
url |
http://hdl.handle.net/10400.1/18274 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1664-3224 10.3389/fimmu.2022.840861 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Frontiers Media SA |
publisher.none.fl_str_mv |
Frontiers Media SA |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799133326472118272 |