Purification, characterization and cDNA cloning of two natterin-like toxins from the skin secretion of oriental catfish Plotosus lineatus

Tamura, Saki; Yamakawa, Masafumi; Shiomi, Kazuro

doi:10.1016/j.toxicon.2011.08.001

Cited by 33 publications

(21 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Another homolog, the human ZG16p, exhibits high affinity toward the mannan of yeast and pathogenic fungi and has been suggested to attack the invading pathogens in the digestive system . Similar to its homologs in catfish and lamprey , Dln1 might be also a defense molecule in zebrafish, most likely via forming a transmembrane pore on the target cells similar to the previously reported mammal perforin‐2 .…”

Section: Discussionsupporting

confidence: 55%

“…Bioinformatic analysis revealed that the zebrafish Danio rerio encodes 16 hypothetical aerolysin‐like isoforms , which share a 55–98% sequence identity between isoforms over the full‐length protein of ~300 residues. Moreover, these isoforms share a sequence identity of ~60% to catfish and lamprey natterin‐like proteins, which are hypothetical defense molecules against predators . Here, we report the structures of one isoform (NCBI: NP_001013322.1), termed Dln1, in both water‐soluble dimeric form (at 1.86 Å) and membrane‐bound octameric form (at 20 Å) using X‐ray crystallography and electron microscopy (EM), respectively.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Structural basis for receptor recognition and pore formation of a zebrafish aerolysin‐like protein

et al. 2015

View full text Add to dashboard Cite

Various aerolysin-like pore-forming proteins have been identified from bacteria to vertebrates. However, the mechanism of receptor recognition and/or pore formation of the eukaryotic members remains unknown. Here, we present the first crystal and electron microscopy structures of a vertebrate aerolysin-like protein from Danio rerio, termed Dln1, before and after pore formation. Each subunit of Dln1 dimer comprises a b-prism lectin module followed by an aerolysin module. Specific binding of the lectin module toward high-mannose glycans triggers drastic conformational changes of the aerolysin module in a pH-dependent manner, ultimately resulting in the formation of a membrane-bound octameric pore. Structural analyses combined with computational simulations and biochemical assays suggest a pore-forming process with an activation mechanism distinct from the previously characterized bacterial members. Moreover, Dln1 and its homologs are ubiquitously distributed in bony fishes and lamprey, suggesting a novel fish-specific defense molecule.

show abstract

Section: Discussionsupporting

confidence: 55%

Section: Introductionmentioning

confidence: 99%

Structural basis for receptor recognition and pore formation of a zebrafish aerolysin‐like protein

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Here we identified two lectins namely natterin (spot 22) and pentraxin (spot 46). Natterin was first isolated from venom gland of Thalassophryne natteri [22] Natterin like proteinaceous toxins (I and II) were purified from skin secretions of oriental catfish ( Plotosus lineatus ) [23] . Natterin has a pore forming toxin like domain with kinogenase activity [22] .…”

Section: Resultsmentioning

confidence: 99%

Skin mucus proteins of lumpsucker (Cyclopterus lumpus)

Patel

Brinchmann

2017

Biochemistry and Biophysics Reports

View full text Add to dashboard Cite

Fish skin mucus serves as a first line of defense against pathogens and external stressors. In this study the proteomic profile of lumpsucker skin mucus was characterized using 2D gels coupled with tandem mass spectrometry. Mucosal proteins were identified by homology searches across the databases SwissProt, NCBInr and vertebrate EST. The identified proteins were clustered into ten groups based on their gene ontology biological process in PANTHER (www.patherdb.org). Calmodulin, cystatin-B, histone H2B, peroxiredoxin1, apolipoprotein A1, natterin-2, 14-3-3 protein, alfa enolase, pentraxin, warm temperature acclimation 65 kDa (WAP65kDa) and heat shock proteins were identified. Several of the proteins are known to be involved in immune and/or stress responses. Proteomic profile established in this study could be a benchmark for differential proteomics studies.

show abstract

“…Presence or absence of Echotoxin-2- and Natterin-4-like genes was also similar to that of SE-cephalotoxin-like genes. Interestingly, SE-cephalotoxin and natterins have previously been found only in cephalopods and fish, respectively ( Tamura et al 2011 ; Barathkuma et al 2013 ). SE-cephalotoxin is found in salivary glands of the cuttlefish Sepia esculenta and is utilized in predation, but its precise biochemical function is unknown ( Ueda et al 2008 ).…”

Section: Discussionmentioning

confidence: 98%

Nemertean Toxin Genes Revealed through Transcriptome Sequencing

Whelan

Kocot

Santos

et al. 2014

Genome Biology and Evolution

View full text Add to dashboard Cite

Nemerteans are one of few animal groups that have evolved the ability to utilize toxins for both defense and subduing prey, but little is known about specific nemertean toxins. In particular, no study has identified specific toxin genes even though peptide toxins are known from some nemertean species. Information about toxin genes is needed to better understand evolution of toxins across animals and possibly provide novel targets for pharmaceutical and industrial applications. We sequenced and annotated transcriptomes of two free-living and one commensal nemertean and annotated an additional six publicly available nemertean transcriptomes to identify putative toxin genes. Approximately 63–74% of predicted open reading frames in each transcriptome were annotated with gene names, and all species had similar percentages of transcripts annotated with each higher-level GO term. Every nemertean analyzed possessed genes with high sequence similarities to known animal toxins including those from stonefish, cephalopods, and sea anemones. One toxin-like gene found in all nemerteans analyzed had high sequence similarity to Plancitoxin-1, a DNase II hepatotoxin that may function well at low pH, which suggests that the acidic body walls of some nemerteans could work to enhance the efficacy of protein toxins. The highest number of toxin-like genes found in any one species was seven and the lowest was three. The diversity of toxin-like nemertean genes found here is greater than previously documented, and these animals are likely an ideal system for exploring toxin evolution and industrial applications of toxins.

show abstract

Purification, characterization and cDNA cloning of two natterin-like toxins from the skin secretion of oriental catfish Plotosus lineatus

Cited by 33 publications

References 16 publications

Structural basis for receptor recognition and pore formation of a zebrafish aerolysin‐like protein

Structural basis for receptor recognition and pore formation of a zebrafish aerolysin‐like protein

Skin mucus proteins of lumpsucker (Cyclopterus lumpus)

Nemertean Toxin Genes Revealed through Transcriptome Sequencing

Contact Info

Product

Resources

About