Immunological characterization and function analysis of L-type lectin from spotted knifejaw, Oplegnathus punctatus
Lily-type lectin (LTL) plays significant roles in innate immune response against pathogen infection. LTL in animals and plants has received widespread attention. In the present study, an LTL (OppLTL) was identified from spotted knifejaw Oplegnathus punctatus . The OppLTL encoded a typical Ca 2+ -dep...
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Published in | Frontiers in immunology Vol. 13; p. 993777 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Frontiers Media S.A
26.09.2022
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ISSN | 1664-3224 1664-3224 |
DOI | 10.3389/fimmu.2022.993777 |
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Abstract | Lily-type lectin (LTL) plays significant roles in innate immune response against pathogen infection. LTL in animals and plants has received widespread attention. In the present study, an LTL (OppLTL) was identified from spotted knifejaw
Oplegnathus punctatus
. The OppLTL encoded a typical Ca
2+
-dependent carbohydrate-binding protein containing a CRD domain. The qRT-PCR showed that it was mainly expressed in the gill and was significantly upregulated after
Vibrio anguillarum
challenge. The agglutination analysis showed that the recombinant OppLTL could bind and agglutinate Gram-negative and Gram-positive bacteria in a Ca
2+
-dependent manner. However, the binding activity was different. Meanwhile, the recombinant OppLTL could hemagglutinate mammalian and teleost erythrocytes. Subcellular localization revealed that OppLTL was mainly detected in the cytoplasm of HEK293T cells. The dual-luciferase analysis revealed that OppLTL could inhibit the activity of the NF-κB signal pathway in HEK293T cells after OppLTL overexpression. These findings collectively demonstrated that OppLTL could be involved in host innate immune response and defense against bacterial infection in spotted knifejaw. |
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AbstractList | Lily-type lectin (LTL) plays significant roles in innate immune response against pathogen infection. LTL in animals and plants has received widespread attention. In the present study, an LTL (OppLTL) was identified from spotted knifejaw Oplegnathus punctatus. The OppLTL encoded a typical Ca2+-dependent carbohydrate-binding protein containing a CRD domain. The qRT-PCR showed that it was mainly expressed in the gill and was significantly upregulated after Vibrio anguillarum challenge. The agglutination analysis showed that the recombinant OppLTL could bind and agglutinate Gram-negative and Gram-positive bacteria in a Ca2+-dependent manner. However, the binding activity was different. Meanwhile, the recombinant OppLTL could hemagglutinate mammalian and teleost erythrocytes. Subcellular localization revealed that OppLTL was mainly detected in the cytoplasm of HEK293T cells. The dual-luciferase analysis revealed that OppLTL could inhibit the activity of the NF-κB signal pathway in HEK293T cells after OppLTL overexpression. These findings collectively demonstrated that OppLTL could be involved in host innate immune response and defense against bacterial infection in spotted knifejaw. Lily-type lectin (LTL) plays significant roles in innate immune response against pathogen infection. LTL in animals and plants has received widespread attention. In the present study, an LTL (OppLTL) was identified from spotted knifejaw Oplegnathus punctatus . The OppLTL encoded a typical Ca 2+ -dependent carbohydrate-binding protein containing a CRD domain. The qRT-PCR showed that it was mainly expressed in the gill and was significantly upregulated after Vibrio anguillarum challenge. The agglutination analysis showed that the recombinant OppLTL could bind and agglutinate Gram-negative and Gram-positive bacteria in a Ca 2+ -dependent manner. However, the binding activity was different. Meanwhile, the recombinant OppLTL could hemagglutinate mammalian and teleost erythrocytes. Subcellular localization revealed that OppLTL was mainly detected in the cytoplasm of HEK293T cells. The dual-luciferase analysis revealed that OppLTL could inhibit the activity of the NF-κB signal pathway in HEK293T cells after OppLTL overexpression. These findings collectively demonstrated that OppLTL could be involved in host innate immune response and defense against bacterial infection in spotted knifejaw. Lily-type lectin (LTL) plays significant roles in innate immune response against pathogen infection. LTL in animals and plants has received widespread attention. In the present study, an LTL (OppLTL) was identified from spotted knifejaw Oplegnathus punctatus. The OppLTL encoded a typical Ca2+-dependent carbohydrate-binding protein containing a CRD domain. The qRT-PCR showed that it was mainly expressed in the gill and was significantly upregulated after Vibrio anguillarum challenge. The agglutination analysis showed that the recombinant OppLTL could bind and agglutinate Gram-negative and Gram-positive bacteria in a Ca2+-dependent manner. However, the binding activity was different. Meanwhile, the recombinant OppLTL could hemagglutinate mammalian and teleost erythrocytes. Subcellular localization revealed that OppLTL was mainly detected in the cytoplasm of HEK293T cells. The dual-luciferase analysis revealed that OppLTL could inhibit the activity of the NF-κB signal pathway in HEK293T cells after OppLTL overexpression. These findings collectively demonstrated that OppLTL could be involved in host innate immune response and defense against bacterial infection in spotted knifejaw.Lily-type lectin (LTL) plays significant roles in innate immune response against pathogen infection. LTL in animals and plants has received widespread attention. In the present study, an LTL (OppLTL) was identified from spotted knifejaw Oplegnathus punctatus. The OppLTL encoded a typical Ca2+-dependent carbohydrate-binding protein containing a CRD domain. The qRT-PCR showed that it was mainly expressed in the gill and was significantly upregulated after Vibrio anguillarum challenge. The agglutination analysis showed that the recombinant OppLTL could bind and agglutinate Gram-negative and Gram-positive bacteria in a Ca2+-dependent manner. However, the binding activity was different. Meanwhile, the recombinant OppLTL could hemagglutinate mammalian and teleost erythrocytes. Subcellular localization revealed that OppLTL was mainly detected in the cytoplasm of HEK293T cells. The dual-luciferase analysis revealed that OppLTL could inhibit the activity of the NF-κB signal pathway in HEK293T cells after OppLTL overexpression. These findings collectively demonstrated that OppLTL could be involved in host innate immune response and defense against bacterial infection in spotted knifejaw. |
Author | Liu, Xiaobing Liu, Jinxiang Zhang, Quanqi Wang, Zhigang |
AuthorAffiliation | 2 Laboratory for Marine Fisheries Science and Food Production Processes, Qingdao National Laboratory for Marine Science and Technology , Qingdao , China 3 Key Laboratory of Tropical Aquatic Germplasm of Hainan Province, Sanya Oceanographic Institution, Ocean University of China , Sanya , China 1 MOE Key Laboratory of Marine Genetics and Breeding, College of Marine Life Sciences, Ocean University of China , Qingdao , China 4 Hainan Yazhou Bay Seed Laboratory , Sanya , China |
AuthorAffiliation_xml | – name: 4 Hainan Yazhou Bay Seed Laboratory , Sanya , China – name: 1 MOE Key Laboratory of Marine Genetics and Breeding, College of Marine Life Sciences, Ocean University of China , Qingdao , China – name: 2 Laboratory for Marine Fisheries Science and Food Production Processes, Qingdao National Laboratory for Marine Science and Technology , Qingdao , China – name: 3 Key Laboratory of Tropical Aquatic Germplasm of Hainan Province, Sanya Oceanographic Institution, Ocean University of China , Sanya , China |
Author_xml | – sequence: 1 givenname: Jinxiang surname: Liu fullname: Liu, Jinxiang – sequence: 2 givenname: Xiaobing surname: Liu fullname: Liu, Xiaobing – sequence: 3 givenname: Zhigang surname: Wang fullname: Wang, Zhigang – sequence: 4 givenname: Quanqi surname: Zhang fullname: Zhang, Quanqi |
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Cites_doi | 10.1016/j.sbi.2004.09.008 10.1016/j.tim.2007.10.010 10.1007/s00253-006-0649-2 10.1016/j.gene.2016.09.009 10.1016/j.vetimm.2009.07.015 10.1016/j.biopen.2016.03.001 10.1111/jam.12086 10.1038/nsb0695-472 10.1016/j.ibmb.2006.03.010 10.1016/0144-8617(94)00091-7 10.1016/j.dci.2016.06.014 10.1016/j.fsi.2018.01.051 10.1016/j.molimm.2013.06.020 10.1016/j.dci.2016.01.007 10.1016/j.dci.2016.10.001 10.1074/jbc.M301038200 10.1007/s12010-011-9438-1 10.1074/jbc.M109.002873 10.1016/j.fsi.2019.05.054 10.1016/j.dci.2011.08.011 10.1016/j.fsi.2016.08.025 10.1016/j.dci.2017.11.006 10.1016/j.fsi.2012.07.003 10.1016/j.fsi.2017.06.012 10.1093/intimm/dxp017 10.4049/jimmunol.179.12.8425 10.1016/j.dci.2015.10.003 10.1016/j.ijbiomac.2018.02.058 10.1016/j.procbio.2009.11.013 10.3390/molecules20022229 10.1016/j.dci.2011.05.011 10.1016/j.cell.2010.01.022 10.1016/j.cbpc.2008.08.004 10.1016/j.ijbiomac.2018.07.156 10.3390/molecules20010519 10.1111/j.1600-065X.1998.tb01185.x 10.1093/glycob/cwh122 10.1006/jmbi.1998.2353 10.1016/j.intimp.2011.05.012 10.1016/S1046-5928(02)00559-4 10.1111/j.1742-4658.2005.05031.x 10.1016/j.ijbiomac.2018.11.233 10.1093/nar/gkg500 10.1016/j.fsi.2012.11.033 10.1016/j.dci.2015.01.007 |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Reviewed by: Monica Fengsrud Brinchmann, Nord University, Norway; Jason W Holland, University of Aberdeen, United Kingdom Edited by: Carlos Angulo, Centro de Investigación Biológica del Noroeste (CIBNOR), Mexico This article was submitted to Comparative Immunology, a section of the journal Frontiers in Immunology |
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Title | Immunological characterization and function analysis of L-type lectin from spotted knifejaw, Oplegnathus punctatus |
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