Immunomodulatory activity of a pedicellarial venom lectin from the toxopneustid sea urchin,<i>Toxopneustes pileolus</i>

Edo, Kozue; Sakai, Hitomi; Nakagawa, Hideyuki; Hashimoto, Tamiko; Shinohara, Mitsuko; Ohura, Kiyoshi

doi:10.3109/15569543.2012.730090

Cited by 10 publications

(7 citation statements)

References 29 publications

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“…They were found also in colonial ascidians [44] and in bivalves, like the penguin wing oyster [45]. RBLs are involved in several processes including mitogenic, chemotactic, cytolytic, and apoptotic activities [41,46,47]. They also showed hemagglutination activity on rabbit erythrocytes, that can be inhibited by L-rhamnose and/or other saccharides [48].…”

Section: Resultsmentioning

confidence: 99%

Venom Diversity and Evolution in the Most Divergent Cone Snail Genus Profundiconus

Fassio

Modica

Mary

et al. 2019

Toxins

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Profundiconus is the most divergent cone snail genus and its unique phylogenetic position, sister to the rest of the family Conidae, makes it a key taxon for examining venom evolution and diversity. Venom gland and foot transcriptomes of Profundiconus cf. vaubani and Profundiconus neocaledonicus were de novo assembled, annotated, and analyzed for differential expression. One hundred and thirty-seven venom components were identified from P. cf. vaubani and 82 from P. neocaledonicus, with only four shared by both species. The majority of the transcript diversity was composed of putative peptides, including conotoxins, profunditoxins, turripeptides, insulin, and prohormone-4. However, there were also a significant percentage of other putative venom components such as chymotrypsin and L-rhamnose-binding lectin. The large majority of conotoxins appeared to be from new gene superfamilies, three of which are highly different from previously reported venom peptide toxins. Their low conotoxin diversity and the type of insulin found suggested that these species, for which no ecological information are available, have a worm or molluscan diet associated with a narrow dietary breadth. Our results indicate that Profundiconus venom is highly distinct from that of other cone snails, and therefore important for examining venom evolution in the Conidae family.

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Section: Resultsmentioning

confidence: 99%

Venom Diversity and Evolution in the Most Divergent Cone Snail Genus Profundiconus

Fassio

Modica

Mary

et al. 2019

Toxins

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“…Proteins containing this domain fold can be found in different families, including some often present in animal venoms such as snake venom galactose-binding lectins ( Sartim and Sampaio 2015 ); nattectins, which are C-type lectins from the venomous fish Thalassophryne nattereri that have been also recently identified in the proteotranscriptome of the hoplonemertean A. lactifloreus ( Lopes-Ferreira et al 2011 ; von Reumont et al 2020 ); and SUL-I galactose-binding lectins present in the venom of the flower sea urchin Toxopneustes pileolus ( Hatakeyama et al 2017 ). These proteins have been reported to mediate several biological functions associated with envenomation including platelet aggregation and inflammation, as well as mitogenic, chemotactic, and cytotoxic activities ( Edo et al 2012 ; Sartim and Sampaio 2015 ). We also identified putative predatory toxins with antistasin-like domains ( table 1 , supplementary file S4, Supplementary Material online), which are common anticoagulants in leech saliva and have been also recorded from other nonblood-feeding invertebrates such as cnidarians and mollusks where they may act as modulators of the immune response ( Iwama et al 2021 ).…”

Section: Resultsmentioning

confidence: 99%

Evolution, Expression Patterns, and Distribution of Novel Ribbon Worm Predatory and Defensive Toxins

Verdes

Taboada

Hamilton

et al. 2022

Molecular Biology and Evolution

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Ribbon worms are active predators that use an eversible proboscis to inject venom into their prey and defend themselves with toxic epidermal secretions. Previous work on nemertean venom has largely focused on just a few species and has not investigated the different predatory and defensive secretions in detail. Consequently, our understanding of the composition and evolution of ribbon worm venoms is still very limited. Here, we present a comparative study of nemertean venom combining RNA-seq differential gene expression analyses of venom producing tissues, tandem mass spectrometry-based proteomics of toxic secretions, and mass spectrometry imaging of proboscis sections, to shed light onto the composition and evolution of predatory and defensive toxic secretions in Antarctonemertes valida. Our analyses reveal a wide diversity of putative defensive and predatory toxins with tissue-specific gene expression patterns and restricted distributions to the mucus and proboscis proteomes respectively, suggesting that ribbon worms produce distinct toxin cocktails for predation and defense. Our results also highlight the presence of numerous lineage-specific toxins, indicating that venom evolution is highly divergent across nemerteans, producing toxin cocktails that might be finely tuned to subdue different prey. Our data also suggests that the hoplonemertean proboscis is a highly specialized predatory organ that seems to be involved in a variety of biological functions besides predation, including secretion and sensory perception. Overall, our results advance our knowledge into the diversity and evolution of nemertean venoms and highlight the importance of combining different types of data to characterize toxin composition in understudied venomous organisms.

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“…Several biologically active proteins, including lectins, have been isolated from the venomous sea urchins, e.g., galactose-specific lectins SUL-I, II, and III from T. pileolus, and heparin-binding lectin TGL-1 from Tripneustes gratilla (Edo et al 2012;Nakagawa et al 2003;Sakai et al 2013), whereas very limited structural information has been obtained till date. Among these, SUL-I was characterized as a galactose-specific lectin, which exerts several biological activities such as chemotactic, mitogenic, and cytotoxic activities (Nakagawa et al 2003;Nakagawa et al 1999;Satoh et al 2002;Takei and Nakagawa 2006).…”

Section: Discussionmentioning

confidence: 99%

cDNA cloning and characterization of a rhamnose-binding lectin SUL-I from the toxopneustid sea urchin Toxopneustes pileolus venom

Hatakeyama

Ichise

Yonekura

et al. 2015

Toxicon

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The globiferous pedicellariae of the venomous sea urchin Toxopneustes pileolus contain several 25 biologically active proteins. Among these, a galactose-binding lectin SUL-I isolated from the venom 26in the large globiferous pedicellariae shows several activities such as mitogenic, chemotactic, and 27 cytotoxic activities through binding to the carbohydrate chains on the cells. We cloned cDNA 28 encoding SUL-I by reverse transcription-PCR using the degenerate primers designed on the basis of with the carbohydrate-recognition domains of the rhamnose-binding lectins, which have been mostly 34 found in fish eggs. While rSUL-I exhibited binding activity for several galactose-related sugars, the 35 highest affinity was found for L-rhamnose among carbohydrates tested, confirming that SUL-I is a 36 rhamnose-binding lectin. rSUL-I also showed hemagglutinating activity toward rabbit erythrocytes, 37 indicating the existence of more than one carbohydrate-binding site to cross-link the carbohydrate 38 chains on the cell surface, which may be closely related to its biological activities. 39 40

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Immunomodulatory activity of a pedicellarial venom lectin from the toxopneustid sea urchin,Toxopneustes pileolus

Cited by 10 publications

References 29 publications

Venom Diversity and Evolution in the Most Divergent Cone Snail Genus Profundiconus

Venom Diversity and Evolution in the Most Divergent Cone Snail Genus Profundiconus

Evolution, Expression Patterns, and Distribution of Novel Ribbon Worm Predatory and Defensive Toxins

cDNA cloning and characterization of a rhamnose-binding lectin SUL-I from the toxopneustid sea urchin Toxopneustes pileolus venom

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