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Comparative analysis of C‐type lectin domain proteins in the ghost moth, Thitarodes xiaojinensis (Lepidoptera: Hepialidae)

Insects have a large family of C‐type lectins involved in cell adhesion, pathogen recognition and activation of immune responses. In this study, 32 transcripts encoding C‐type lectin domain proteins (CTLDPs) were identified from the Thitarodes xiaojinensis transcriptome. According to their domain st...

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Autores principales: Meng, Qian, Zhang, Ji‐Hong, Zhang, Huan, Zhou, Gui‐Ling, Ni, Ruo‐Yao, Zhao, Yan‐Ni, Qin, Qi‐Lian, Zou, Zhen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7379682/
https://www.ncbi.nlm.nih.gov/pubmed/29274206
http://dx.doi.org/10.1111/1744-7917.12564
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author Meng, Qian
Zhang, Ji‐Hong
Zhang, Huan
Zhou, Gui‐Ling
Ni, Ruo‐Yao
Zhao, Yan‐Ni
Qin, Qi‐Lian
Zou, Zhen
author_facet Meng, Qian
Zhang, Ji‐Hong
Zhang, Huan
Zhou, Gui‐Ling
Ni, Ruo‐Yao
Zhao, Yan‐Ni
Qin, Qi‐Lian
Zou, Zhen
author_sort Meng, Qian
collection PubMed
description Insects have a large family of C‐type lectins involved in cell adhesion, pathogen recognition and activation of immune responses. In this study, 32 transcripts encoding C‐type lectin domain proteins (CTLDPs) were identified from the Thitarodes xiaojinensis transcriptome. According to their domain structures, six CTLDPs with one carbohydrate‐recognition domain (CRD) were classified into the CTL‐S subfamily. The other 23 CTLDPs with two CRDs were grouped into the immulectin (IML) subfamily. The remaining three with extra regulatory domains were sorted into the CTL‐X subfamily. Phylogenetic analysis showed that CTL‐S and CTL‐X members from different insects could form orthologous groups. In contrast, no T. xiaojinensis IML orthologues were found in other insects. Remarkable lineage‐specific expansion in this subfamily was observed reflecting that these CTLDPs, as important receptors, have evolved diversified members in response to a variety of microbes. Prediction of binding ligands revealed that T. xiaojinensis, a cold‐adapted species, conserved the ability of CRDs to combine with Ca(2+) to keep its receptors from freezing. Comparative analysis of induction of CTLDP genes after different immune challenges indicated that IMLs might play critical roles in immune defenses. This study examined T. xiaojinensis CTLDPs and provides a basis for further studies of their characteristics.
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spelling pubmed-73796822020-07-27 Comparative analysis of C‐type lectin domain proteins in the ghost moth, Thitarodes xiaojinensis (Lepidoptera: Hepialidae) Meng, Qian Zhang, Ji‐Hong Zhang, Huan Zhou, Gui‐Ling Ni, Ruo‐Yao Zhao, Yan‐Ni Qin, Qi‐Lian Zou, Zhen Insect Sci Original Articles Insects have a large family of C‐type lectins involved in cell adhesion, pathogen recognition and activation of immune responses. In this study, 32 transcripts encoding C‐type lectin domain proteins (CTLDPs) were identified from the Thitarodes xiaojinensis transcriptome. According to their domain structures, six CTLDPs with one carbohydrate‐recognition domain (CRD) were classified into the CTL‐S subfamily. The other 23 CTLDPs with two CRDs were grouped into the immulectin (IML) subfamily. The remaining three with extra regulatory domains were sorted into the CTL‐X subfamily. Phylogenetic analysis showed that CTL‐S and CTL‐X members from different insects could form orthologous groups. In contrast, no T. xiaojinensis IML orthologues were found in other insects. Remarkable lineage‐specific expansion in this subfamily was observed reflecting that these CTLDPs, as important receptors, have evolved diversified members in response to a variety of microbes. Prediction of binding ligands revealed that T. xiaojinensis, a cold‐adapted species, conserved the ability of CRDs to combine with Ca(2+) to keep its receptors from freezing. Comparative analysis of induction of CTLDP genes after different immune challenges indicated that IMLs might play critical roles in immune defenses. This study examined T. xiaojinensis CTLDPs and provides a basis for further studies of their characteristics. John Wiley and Sons Inc. 2018-02-22 2019-06 /pmc/articles/PMC7379682/ /pubmed/29274206 http://dx.doi.org/10.1111/1744-7917.12564 Text en © 2017 The Authors. Insect Science published by John Wiley & Sons Australia, Ltd on behalf of Institute of Zoology, Chinese Academy of Sciences This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Articles
Meng, Qian
Zhang, Ji‐Hong
Zhang, Huan
Zhou, Gui‐Ling
Ni, Ruo‐Yao
Zhao, Yan‐Ni
Qin, Qi‐Lian
Zou, Zhen
Comparative analysis of C‐type lectin domain proteins in the ghost moth, Thitarodes xiaojinensis (Lepidoptera: Hepialidae)
title Comparative analysis of C‐type lectin domain proteins in the ghost moth, Thitarodes xiaojinensis (Lepidoptera: Hepialidae)
title_full Comparative analysis of C‐type lectin domain proteins in the ghost moth, Thitarodes xiaojinensis (Lepidoptera: Hepialidae)
title_fullStr Comparative analysis of C‐type lectin domain proteins in the ghost moth, Thitarodes xiaojinensis (Lepidoptera: Hepialidae)
title_full_unstemmed Comparative analysis of C‐type lectin domain proteins in the ghost moth, Thitarodes xiaojinensis (Lepidoptera: Hepialidae)
title_short Comparative analysis of C‐type lectin domain proteins in the ghost moth, Thitarodes xiaojinensis (Lepidoptera: Hepialidae)
title_sort comparative analysis of c‐type lectin domain proteins in the ghost moth, thitarodes xiaojinensis (lepidoptera: hepialidae)
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7379682/
https://www.ncbi.nlm.nih.gov/pubmed/29274206
http://dx.doi.org/10.1111/1744-7917.12564
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