Identification and preliminary characterization of  Hc-clec-160 , a novel C-type lectin domain-containing gene of the strongylid nematode  Haemonchus contortus

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Abstract

Background

The strongylid parasite Haemonchus contortus causes severe anemia in domestic animals worldwide. Effective preventive and therapeutical agents are lacking, because of drug resistance and that little is known about the molecular mechanism of the interaction between H. contortus and host cells.

Methods

A new gene, Hc-clec-160, was discovered with RT-PCR. Transcriptional levels of Hc-clec-160 and Ce-clec-160 throughout different growth phases of corresponding nematodes were assayed by qPCR. Immunofluorescence staining of paraffin section were performed to determine the protein localization in adult worms of H. contortus. To monitor the promoter capacity of the 5'-flanking region of Ce-clec-160, micro-injection was used. Overexpression and RNAi constructs was carried out in the N2 strain of Caenorhabditis elegans to find out the gene function of Hc-clec-160.

Results

The full-length cDNA of 1224 bp of Hc-clec-160 was cloned by RT-PCR. The corresponding gene contained twelve exons. Its transcripts peaked in male adult worms. Hc-CLEC-160 was predicted to have a Willebrand factor type A (vWA) domain and a C-type lectin domain. The proteins were not detected by expression in C. elegans or paraffin section experiments in adult of H. contortus. Knockdown of Ce-clec-160 expression in C. elegans by RNAi resulted in shortened body length and decreased brood size.

Conclusions

In this experiment, a new gene Hc-clec-160 was obtained in H. contortus and its function was addressed using a model organism: C. elegans. Our study showed that Hc-clec-160 possesses characteristics similar to those of Ce-clec-160 and plays an important role in the growth and reproduction of this parasitic nematode.

Electronic supplementary material

The online version of this article (10.1186/s13071-018-3005-3) contains supplementary material, which is available to authorized users.

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Most cited references 16

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Immune regulation by helminth parasites: cellular and molecular mechanisms.

Rick Maizels, Maria Yazdanbakhsh (2003)

Immunology was founded by studying the body's response to infectious microorganisms, and yet microbial prokaryotes only tell half the story of the immune system. Eukaryotic pathogens--protozoa, helminths, fungi and ectoparasites--have all been powerful selective forces for immune evolution. Often, as with lethal protozoal parasites, the focus has been on acute infections and the inflammatory responses they evoke. Long-lived parasites such as the helminths, however, are more remarkable for their ability to downregulate host immunity, protecting themselves from elimination and minimizing severe pathology in the host.

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The C-type lectin-like domain superfamily.

Alex Zelensky, Jill Gready (2005)

The superfamily of proteins containing C-type lectin-like domains (CTLDs) is a large group of extracellular Metazoan proteins with diverse functions. The CTLD structure has a characteristic double-loop ('loop-in-a-loop') stabilized by two highly conserved disulfide bridges located at the bases of the loops, as well as a set of conserved hydrophobic and polar interactions. The second loop, called the long loop region, is structurally and evolutionarily flexible, and is involved in Ca2+-dependent carbohydrate binding and interaction with other ligands. This loop is completely absent in a subset of CTLDs, which we refer to as compact CTLDs; these include the Link/PTR domain and bacterial CTLDs. CTLD-containing proteins (CTLDcps) were originally classified into seven groups based on their overall domain structure. Analyses of the superfamily representation in several completely sequenced genomes have added 10 new groups to the classification, and shown that it is applicable only to vertebrate CTLDcps; despite the abundance of CTLDcps in the invertebrate genomes studied, the domain architectures of these proteins do not match those of the vertebrate groups. Ca2+-dependent carbohydrate binding is the most common CTLD function in vertebrates, and apparently the ancestral one, as suggested by the many humoral defense CTLDcps characterized in insects and other invertebrates. However, many CTLDs have evolved to specifically recognize protein, lipid and inorganic ligands, including the vertebrate clade-specific snake venoms, and fish antifreeze and bird egg-shell proteins. Recent studies highlight the functional versatility of this protein superfamily and the CTLD scaffold, and suggest further interesting discoveries have yet to be made.

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Roles of galectins in infection.

Gerardo Vasta (2009)

Galectins, which were first characterized in the mid-1970s, were assigned a role in the recognition of endogenous ('self') carbohydrate ligands in embryogenesis, development and immune regulation. Recently, however, galectins have been shown to bind glycans on the surface of potentially pathogenic microorganisms, and function as recognition and effector factors in innate immunity. Some parasites subvert the recognition roles of the vector or host galectins to ensure successful attachment or invasion. This Review discusses the role of galectins in microbial infection, with particular emphasis on adaptations of pathogens to evasion or subversion of host galectin-mediated immune responses.

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Author and article information

Contributors

Ling Zhang: 21517040@zju.edu.cn

Lingyun Mou: 394257646@qq.com

Xueqiu Chen: chenxueqiu@zju.edu.cn

Yi Yang: yangyi0607@zju.edu.cn

Xiangrui Li: lixiangrui@njau.edu.cn

Xun Suo: suoxun@cau.edu.cn

Xing-Quan Zhu: zhuxingquan@caas.cn

Aifang Du: afdu@zju.edu.cn

Journal

Journal ID (nlm-ta): Parasit Vectors

Journal ID (iso-abbrev): Parasit Vectors

Title: Parasites & Vectors

Publisher: BioMed Central (London )

ISSN (Electronic): 1756-3305

Publication date (Electronic): 20 July 2018

Publication date PMC-release: 20 July 2018

Publication date Collection: 2018

Volume: 11

Electronic Location Identifier: 430

Affiliations

[1 ]ISNI 0000 0004 1759 700X, GRID grid.13402.34, College of Animal Sciences, Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Zhejiang University, ; Hangzhou, China

[2 ]ISNI 0000 0004 1790 4137, GRID grid.35155.37, State Key Laboratory of Agricultural Microbiology, , College of Veterinary Medicine, Huazhong Agricultural University, ; Wuhan, China

[3 ]ISNI 0000 0000 9750 7019, GRID grid.27871.3b, College of Veterinary Medicine, Nanjing Agricultural University, ; Nanjing, China

[4 ]ISNI 0000 0004 0530 8290, GRID grid.22935.3f, State Key Laboratory of Agrobiotechnology, Key Laboratory of Zoonosis of Ministry of Agriculture, , National Animal Protozoa Laboratory and College of Veterinary Medicine, China Agricultural University, ; Beijing, China

[5 ]ISNI 0000 0001 0018 8988, GRID grid.454892.6, State Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, , Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, ; Lanzhou, 730046 Gansu Province China

Article

Publisher ID: 3005

DOI: 10.1186/s13071-018-3005-3

PMC ID: 6054721

PubMed ID: 30029661

SO-VID: 79616005-85af-4094-95af-32e43e9215d8

License:

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

History

Date received : 7 April 2018

Date accepted : 9 July 2018

Funding

Funded by: the National Key Basic Research Program (973 Program) of China

Award ID: No. 2015CB150300

Award Recipient : Aifang Du

Funded by: the National Key Research and Development Program of China

Award ID: No. 2017YFD0501200

Award Recipient : Aifang Du

Funded by: the National Natural Science Foundation of China

Award ID: No. 31602041

Award Recipient : Yi Yang

Funded by: the Opening Fund of State Key Laboratory of Veterinary Etiological Biology

Award ID: No. SKLVEB2016KFKT018

Award Recipient : Yi Yang

Funded by: the Science and Technology Plan Project of Jiaxing

Award ID: No. 2016AY23025

Award Recipient : Yi Yang

Custom metadata

ScienceOpen disciplines: Parasitology

Keywords: hc-clec-160,haemonchus contortus,caenorhabditis elegans,c-type lectin

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ScienceOpen disciplines: Parasitology

Keywords: hc-clec-160, haemonchus contortus, caenorhabditis elegans, c-type lectin

Identification and preliminary characterization of Hc-clec-160, a novel C-type lectin domain-containing gene of the strongylid nematode Haemonchus contortus

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Abstract

Background

Methods

Results

Conclusions

Electronic supplementary material

Related collections

Malaria vaccine development

Most cited references 16

Immune regulation by helminth parasites: cellular and molecular mechanisms.

The C-type lectin-like domain superfamily.

Roles of galectins in infection.

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