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 inFrontiers in immunology Vol. 13; p. 993777
Main Authors Liu, Jinxiang, Liu, Xiaobing, Wang, Zhigang, Zhang, Quanqi
Format Journal Article
LanguageEnglish
Published Frontiers Media S.A 26.09.2022
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ISSN1664-3224
1664-3224
DOI10.3389/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.
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
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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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References Weis (B29) 1998; 163
Yu (B34) 2006; 36
Arasu (B8) 2013; 56
Park (B10) 2016; 65
Mandlik (B5) 2008; 16
Cagliari (B45) 2018; 119
de Santana Evangelista (B15) 2009; 284
Wang (B36) 2017; 67
Vasta (B2) 2011; 35
Vasta (B6) 2004; 14
Park (B32) 2012; 36
Huang (B9) 2016; 58
Takeuchi (B27) 2010; 140
Sá (B39) 2009; 149
Yu (B35) 2007; 179
Nakamura (B20) 2012; 33
Chandra (B30) 1999; 285
Gomes (B38) 2013; 114
Kennedy (B1) 1995; 26
Saraiva (B4) 2011; 11
Pan (B41) 2010; 133
Zelensky (B28) 2005; 272
Chenna (B23) 2003; 31
Zhang (B25) 2018; 76
Fontenelle (B44) 2018; 112
Qu (B24) 2016; 594
Lam (B18) 2002; 26
Liu (B22) 2019; 92
Hester (B31) 1995; 2
Dias (B17) 2015; 20
Ngai (B40) 2007; 74
Kawai (B26) 2009; 21
Kugapreethan (B14) 2018; 81
Zhou (B21) 2015; 50
Sharon (B3) 2004; 14
de Freitas Pires (B42) 2019; 125
Campos (B43) 2016; 2
da Silva (B16) 2012; 166
Costa (B37) 2010; 45
Mason (B19) 2015; 20
Yu (B33) 2013; 34
Tsutsui (B7) 2003; 278
Tasumi (B11) 2016; 59
Sun (B13) 2016; 55
Arasu (B12) 2017; 67
References_xml – volume: 14
  year: 2004
  ident: B6
  article-title: Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates
  publication-title: Curr Opin Struct Biol
  doi: 10.1016/j.sbi.2004.09.008
– volume: 16
  start-page: 33
  year: 2008
  ident: B5
  article-title: Pili in gram-positive bacteria: assembly, involvement in colonization and biofilm development
  publication-title: Trends Microbiol
  doi: 10.1016/j.tim.2007.10.010
– volume: 74
  year: 2007
  ident: B40
  article-title: A mannose-specific tetrameric lectin with mitogenic and antibacterial activities from the ovary of a teleost, the cobia (Rachycentron canadum)
  publication-title: Appl Microbiol Biotechnol
  doi: 10.1007/s00253-006-0649-2
– volume: 594
  year: 2016
  ident: B24
  article-title: A new LDLa domain-containing c-type lectin with bacterial agglutinating and binding activity in amphioxus
  publication-title: Gene
  doi: 10.1016/j.gene.2016.09.009
– volume: 133
  year: 2010
  ident: B41
  article-title: Isolation and characterization of a novel fucose-binding lectin from the gill of bighead carp (Aristichthys nobilis)
  publication-title: Vet Immunol Immunopathol
  doi: 10.1016/j.vetimm.2009.07.015
– volume: 2
  year: 2016
  ident: B43
  article-title: Anti-inflammatory and antinociceptive activities of Bauhinia monandra leaf lectin
  publication-title: Biochimie Open
  doi: 10.1016/j.biopen.2016.03.001
– volume: 114
  year: 2013
  ident: B38
  article-title: Antimicrobial lectin from Schinus terebinthifolius leaf
  publication-title: J Appl Microbiol
  doi: 10.1111/jam.12086
– volume: 2
  year: 1995
  ident: B31
  article-title: Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family
  publication-title: Nat Struct Biol
  doi: 10.1038/nsb0695-472
– volume: 36
  year: 2006
  ident: B34
  article-title: Calcium is not required for immulectin-2 binding, but protects the protein from proteinase digestion
  publication-title: Insect Biochem Mol Biol
  doi: 10.1016/j.ibmb.2006.03.010
– volume: 26
  year: 1995
  ident: B1
  article-title: Lectins, versatile proteins of recognition: A review
  publication-title: Carbohydr Polymers
  doi: 10.1016/0144-8617(94)00091-7
– volume: 65
  start-page: 25
  year: 2016
  ident: B10
  article-title: Molecular cloning and expression analysis of a new lily-type lectin in the rock bream
  publication-title: Oplegnathus fasciatus Dev Comp Immunol
  doi: 10.1016/j.dci.2016.06.014
– volume: 76
  year: 2018
  ident: B25
  article-title: Molecular cloning of a c-type lectin from Portunus trituberculatus, which might be involved in the innate immune response
  publication-title: Fish Shellfish Immunol
  doi: 10.1016/j.fsi.2018.01.051
– volume: 56
  start-page: 497
  year: 2013
  ident: B8
  article-title: Fish lily type lectin-1 contains β-prism architecture: Immunological characterization
  publication-title: Mol Immunol
  doi: 10.1016/j.molimm.2013.06.020
– volume: 59
  start-page: 48
  year: 2016
  ident: B11
  article-title: Identification and characterization of pufflectin from the grass pufferfish Takifugu niphobles and comparison of its expression with that of Takifugu rubripes
  publication-title: Dev Comp Immunol
  doi: 10.1016/j.dci.2016.01.007
– volume: 67
  year: 2017
  ident: B12
  article-title: Bacterial membrane binding and pore formation abilities of carbohydrate recognition domain of fish lectin
  publication-title: Dev Comp Immunol
  doi: 10.1016/j.dci.2016.10.001
– volume: 278
  year: 2003
  ident: B7
  article-title: Lectins homologous to those of monocotyledonous plants in the skin mucus and intestine of pufferfish, Fugu rubripes
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M301038200
– volume: 166
  year: 2012
  ident: B16
  article-title: Purification and characterization of a mannose recognition lectin from Oreochromis niloticus (tilapia fish): Cytokine production in mice splenocytes
  publication-title: Appl Biochem Biotechnol
  doi: 10.1007/s12010-011-9438-1
– volume: 284
  year: 2009
  ident: B15
  article-title: Plumieribetin, a fish lectin homologous to mannose-binding b-type lectins, inhibits the collagen-binding α1β1 integrin
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M109.002873
– volume: 92
  start-page: 11
  year: 2019
  ident: B22
  article-title: A novel c-type lectin from spotted knifejaw, Oplegnathus punctatus possesses antibacterial and anti-inflammatory activity
  publication-title: Fish Shellfish Immunol
  doi: 10.1016/j.fsi.2019.05.054
– volume: 35
  year: 2011
  ident: B2
  article-title: Structural and functional diversity of the lectin repertoire in teleost fish: Relevance to innate and adaptive immunity
  publication-title: Dev Comp Immunol
  doi: 10.1016/j.dci.2011.08.011
– volume: 58
  year: 2016
  ident: B9
  article-title: Immunological characterization and expression of lily-type lectin in response to environmental stress in turbot (Scophthalmus maximus)
  publication-title: Fish Shellfish Immunol
  doi: 10.1016/j.fsi.2016.08.025
– volume: 81
  start-page: 54
  year: 2018
  ident: B14
  article-title: Identification and characterization of a calcium-dependent lily-type lectin from black rockfish (Sebastes schlegelii): Molecular antennas are involved in host defense via pathogen recognition
  publication-title: Dev Comp Immunol
  doi: 10.1016/j.dci.2017.11.006
– volume: 33
  year: 2012
  ident: B20
  article-title: Galectins in the abdominal cavity of the conger eel Conger myriaster participate in the cellular encapsulation of parasitic nematodes by host cells
  publication-title: Fish Shellfish Immunol
  doi: 10.1016/j.fsi.2012.07.003
– volume: 67
  year: 2017
  ident: B36
  article-title: A c-type lectin, nattectin-like protein (CaNTC) in qihe crucian carp Carassius auratus: Binding ability with LPS, PGN and various bacteria, and agglutinating activity against bacteria
  publication-title: Fish Shellfish Immunol
  doi: 10.1016/j.fsi.2017.06.012
– volume: 21
  year: 2009
  ident: B26
  article-title: The roles of TLRs, RLRs and NLRs in pathogen recognition
  publication-title: Int Immunol
  doi: 10.1093/intimm/dxp017
– volume: 179
  year: 2007
  ident: B35
  article-title: A short-form c-type lectin from amphioxus acts as a direct microbial killing protein via interaction with peptidoglycan and glucan
  publication-title: J Immunol
  doi: 10.4049/jimmunol.179.12.8425
– volume: 55
  start-page: 194
  year: 2016
  ident: B13
  article-title: Three novel b-type mannose-specific lectins of Cynoglossus semilaevis possess varied antibacterial activities against gram-negative and gram-positive bacteria
  publication-title: Dev Comp Immunol
  doi: 10.1016/j.dci.2015.10.003
– volume: 112
  year: 2018
  ident: B44
  article-title: Lectin obtained from the red seaweed Bryothamnion triquetrum: Secondary structure and anti-inflammatory activity in mice
  publication-title: Int J Biol Macromol
  doi: 10.1016/j.ijbiomac.2018.02.058
– volume: 45
  year: 2010
  ident: B37
  article-title: A new mistletoe Phthirusa pyrifolia leaf lectin with antimicrobial properties
  publication-title: Process Biochem
  doi: 10.1016/j.procbio.2009.11.013
– volume: 20
  year: 2015
  ident: B19
  article-title: Human lectins and their roles in viral infections
  publication-title: Molecules (Basel Switzerland)
  doi: 10.3390/molecules20022229
– volume: 36
  year: 2012
  ident: B32
  article-title: Molecular cloning and expression analysis of two distinct f-type lectins from the rock bream
  publication-title: Oplegnathus fasciatus Dev Comp Immunol
  doi: 10.1016/j.dci.2011.05.011
– volume: 140
  year: 2010
  ident: B27
  article-title: Pattern recognition receptors and inflammation
  publication-title: Cell
  doi: 10.1016/j.cell.2010.01.022
– volume: 149
  year: 2009
  ident: B39
  article-title: Larvicidal activity of lectins from Myracrodruon urundeuva on Aedes aegypti
  publication-title: Comp Biochem Physiol Part C: Toxicol Pharmacol
  doi: 10.1016/j.cbpc.2008.08.004
– volume: 119
  year: 2018
  ident: B45
  article-title: Bauhinia lectins: Biochemical properties and biotechnological applications
  publication-title: Int J Biol Macromol
  doi: 10.1016/j.ijbiomac.2018.07.156
– volume: 20
  year: 2015
  ident: B17
  article-title: Insights into animal and plant lectins with antimicrobial activities
  publication-title: Molecules
  doi: 10.3390/molecules20010519
– volume: 163
  start-page: 19
  year: 1998
  ident: B29
  article-title: The c-type lectin superfamily in the immune system
  publication-title: Immunol Rev
  doi: 10.1111/j.1600-065X.1998.tb01185.x
– volume: 14
  start-page: 53R
  year: 2004
  ident: B3
  article-title: History of lectins: From hemagglutinins to biological recognition molecules
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwh122
– volume: 285
  year: 1999
  ident: B30
  article-title: Crystal structure of a dimeric mannose-specific agglutinin from garlic: Quaternary association and carbohydrate specificity
  publication-title: J Mol Biol
  doi: 10.1006/jmbi.1998.2353
– volume: 11
  year: 2011
  ident: B4
  article-title: Nattectin a fish c-type lectin drives Th1 responses in vivo: Licenses macrophages to differentiate into cells exhibiting typical DC function
  publication-title: Int Immunopharmacol
  doi: 10.1016/j.intimp.2011.05.012
– volume: 26
  year: 2002
  ident: B18
  article-title: Purification and characterization of a rhamnose-binding lectin with immunoenhancing activity from grass carp (Ctenopharyngodon idellus) ovaries
  publication-title: Protein Expression Purif
  doi: 10.1016/S1046-5928(02)00559-4
– volume: 272
  year: 2005
  ident: B28
  article-title: The c-type lectin-like domain superfamily
  publication-title: FEBS J
  doi: 10.1111/j.1742-4658.2005.05031.x
– volume: 125
  start-page: 53
  year: 2019
  ident: B42
  article-title: Lectin purified from Lonchocarpus campestris seeds inhibits inflammatory nociception
  publication-title: Int J Biol Macromol
  doi: 10.1016/j.ijbiomac.2018.11.233
– volume: 31
  year: 2003
  ident: B23
  article-title: Multiple sequence alignment with the clustal series of programs
  publication-title: Nucleic Acids Res
  doi: 10.1093/nar/gkg500
– volume: 34
  year: 2013
  ident: B33
  article-title: Molecular cloning and characterization of a c-type lectin in roughskin sculpin (Trachidermus fasciatus)
  publication-title: Fish Shellfish Immunol
  doi: 10.1016/j.fsi.2012.11.033
– volume: 50
  start-page: 69
  year: 2015
  ident: B21
  article-title: CsCTL1, a teleost c-type lectin that promotes antibacterial and antiviral immune defense in a manner that depends on the conserved EPN motif
  publication-title: Dev Comp Immunol
  doi: 10.1016/j.dci.2015.01.007
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Snippet Lily-type lectin (LTL) plays significant roles in innate immune response against pathogen infection. LTL in animals and plants has received widespread...
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StartPage 993777
SubjectTerms agglutination
hemagglutination
Immunology
innate immune
lily-type lectin
Oplegnathus punctatus
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Title Immunological characterization and function analysis of L-type lectin from spotted knifejaw, Oplegnathus punctatus
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https://pubmed.ncbi.nlm.nih.gov/PMC9549603
https://doaj.org/article/0ede869a871747979cdfbcccbce2230f
Volume 13
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