Molecular characterisation and expression analysis of a fish-egg lectin in rock bream, and its response to bacterial or viral infection

Kim, Bong-Seok; Nam, Bo‐Hye; Kim, Juwon; Park, Hyoung-Jun; Song, Jeong-Hun; Park, Chan-Il

doi:10.1016/j.fsi.2011.10.024

Cited by 26 publications

(8 citation statements)

References 32 publications

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“…In contrast, limulus lectin L6 is located in large granules of hemocytes in the horseshoe crab despite the lack of classical secretory signal in its protein sequence (7). Similar to the induction of Lb-Tec2 by bacteria, a fish Tectonin has been shown to be induced upon challenge with pathogenic bacteria (11). The dual phenotype of C. elegans upon Lb-Tec2 treatment, skiddy movement and inhibition of larval development, is intriguing.…”

Section: Discussionmentioning

confidence: 99%

“…The Tectonin domain comprises a 33-37 amino acid consensus sequence that was first reported in Tectonin I and II proteins from the slime mold Physarum polycephalum (5). To date, Tectonins from various organisms including sponge, horseshoe crab, fish, and human have been characterized (6)(7)(8)(9)(10)(11)(12). Some of these proteins consist exclusively of Tectonin domain tandem repeats, whereas others comprise additional modules (Fig.…”

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confidence: 99%

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Methylated glycans as conserved targets of animal and fungal innate defense

Wohlschlager

Butschi

Grassi

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Effector proteins of innate immune systems recognize specific nonself epitopes. Tectonins are a family of β-propeller lectins conserved from bacteria to mammals that have been shown to bind bacterial lipopolysaccharide (LPS). We present experimental evidence that two Tectonins of fungal and animal origin have a specificity for O-methylated glycans. We show that Tectonin 2 of the mushroom Laccaria bicolor (Lb-Tec2) agglutinates Gram-negative bacteria and exerts toxicity toward the model nematode Caenorhabditis elegans, suggesting a role in fungal defense against bacteria and nematodes. Biochemical and genetic analysis of these interactions revealed that both bacterial agglutination and nematotoxicity of Lb-Tec2 depend on the recognition of methylated glycans, namely O-methylated mannose and fucose residues, as part of bacterial LPS and nematode cell-surface glycans. In addition, a C. elegans gene, termed samt-1, coding for a candidate membrane transport protein for the presumptive donor substrate of glycan methylation, S-adenosyl-methionine, from the cytoplasm to the Golgi was identified. Intriguingly, limulus lectin L6, a structurally related antibacterial protein of the Japanese horseshoe crab Tachypleus tridentatus, showed properties identical to the mushroom lectin. These results suggest that O-methylated glycans constitute a conserved target of the fungal and animal innate immune system. The broad phylogenetic distribution of O-methylated glycans increases the spectrum of potential antagonists recognized by Tectonins, rendering this conserved protein family a universal defense armor.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Methylated glycans as conserved targets of animal and fungal innate defense

Wohlschlager

Butschi

Grassi

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…Teleost fish have a very sophisticated repertoire of proteins involved in innate immunity that includes lectins, some of which have been identified and characterized in the eggs, where they are generally believed to have a protective function against pathogens during embryo development (Russell & Lumsden, 2005;Vasta et al, 2011;Zhu et al, 2013). The fact that most fish-egg lectins selectively bind rhamnose, a carbohydrate that is absent in animal cells but is very widely distributed in the bacterial cell wall, coupled to the observation that their expression can be up-regulated in the presence of challenging bacteria, has supported the proposal of a role in the defence mechanism against infection (Kim et al, 2011).…”

Section: Introductionmentioning

confidence: 95%

Three-dimensional structure and ligand-binding site of carp fishelectin (FEL)

Capaldi

Faggion

Carrizo

et al. 2015

Acta Crystallogr D Biol Crystallogr

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Carp FEL (fishelectin or fish-egg lectin) is a 238-amino-acid lectin that can be purified from fish eggs by exploiting its selective binding to Sepharose followed by elution with N-acetylglucosamine. Its amino-acid sequence and other biochemical properties have previously been reported. The glycoprotein has four disulfide bridges and the structure of the oligosaccharides linked to Asn27 has been described. Here, the three-dimensional structures of apo carp FEL (cFEL) and of its complex with N-acetylglucosamine determined by X-ray crystallography at resolutions of 1.35 and 1.70 Å, respectively, are reported. The molecule folds as a six-bladed β-propeller and internal short consensus amino-acid sequences have been identified in all of the blades. A calcium atom binds at the bottom of the funnel-shaped tunnel located in the centre of the propeller. Two ligand-binding sites, α and β, are present in each of the two protomers in the dimer. The first site, α, is closer to the N-terminus of the chain and is located in the crevice between the second and the third blades, while the second site, β, is located between the fourth and the fifth blades. The amino acids that participate in the contacts have been identified, as well as the conserved water molecules in all of the sites. Both sites can bind the two anomers, α and β, of N-acetylglucosamine, as is clearly recognizable in the electron-density maps. The lectin presents sequence homology to members of the tachylectin family, which are known to have a function in the innate immune system of arthropods, and homologous genes are present in the genomes of other fish and amphibians. This structure is the first of a protein of this group and, given the degree of homology with other members of the family, it is expected that it will be useful to experimentally determine other crystal structures using the coordinates of cFEL as a search probe in molecular replacement.

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“…A fish lily-type lectin sequence was identified in snakehead murrel ( Channa striata ), large yellow croaker ( Larimichthys crocea ), spotnape ponyfish ( Leiognathus nuchalis ), bartail flathead ( Platycephalus indicus ), turbot ( Scophthalmus maximus ), rock bream ( Oplegnathus fasciatus ), orange-spotted grouper ( Epinephelus coioides ) ( Arasu et al, 2013 ; Tasumi et al, 2016 ). In fish, several articles were published that lectins are involved in the immune response against pathogen infection ( Choi et al, 2015 ; Kim et al, 2011 ; Park et al, 2012 ; Thulasitha et al, 2016 ). However, these studies are limited to information that the lectin is involved in the innate immune response.…”

Section: Introductionmentioning

confidence: 99%

Expression Analysis of Lily Type Lectin Isotypes in the Rock Bream, Oplegnathus fasciatus: in the Tissue, Developmental Stage and Viral Infection

et al. 2016

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Lectins belong to the pattern-recognition receptors (PRRs) class and play important roles in the recognition and elimination of pathogens via the innate immune system. Recently, it was reported that lily-type lectin-1 is involved when a pathogen attacks in the early immune response of fish. However, this study is limited to information that the lectin is involved in the innate immune response against viral infection. In the present study, the lily-type lectin-2 and -3 of Oplegnathus fasciatus (OfLTL-2 and 3) have been presented to be included B-lectin domain and two D-mannose binding sites in the amino acid sequence that an important feature for the fundamental structure. To investigate the functional properties of OfLTLs, the tissue distribution in the healthy rock bream and temporal expression during early developmental stage analysis are performed using quantitative real-time PCR. OfLTL-2 and 3 are predominantly expressed in the liver and skin, but rarely expressed in other organ. Also, the transcripts of OfLTLs are not expressed during the early developmental stage but its transcripts are increased after immune-related organs which are fully formed. In the challenge experiment with RBIV (rock bream iridovirus), the expression of OfLTLs was increased much more strongly in the late response than the early, unlike previously known. These results suggest that OfLTLs are specifically expressed in the immune-related tissues when those organs are fully formed and it can be inferred that the more intensively involved in the second half to the virus infection.

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Molecular characterisation and expression analysis of a fish-egg lectin in rock bream, and its response to bacterial or viral infection

Cited by 26 publications

References 32 publications

Methylated glycans as conserved targets of animal and fungal innate defense

Methylated glycans as conserved targets of animal and fungal innate defense

Three-dimensional structure and ligand-binding site of carp fishelectin (FEL)

Expression Analysis of Lily Type Lectin Isotypes in the Rock Bream, Oplegnathus fasciatus: in the Tissue, Developmental Stage and Viral Infection

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