Isolierung und Strukturaufkl�rung eines h�molytisch aktiven Peptids aus der Seeanemone Metridium senile

Krebs, Hans C.; Habermehl, G.

doi:10.1007/bf00405472

Cited by 12 publications

(5 citation statements)

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“…Most of the cnidarian peptides are known to be potassium channel blockers, with the exception of metridin. Metridin does not have ion channel modulating activities, but instead has a hemolytic effect ( Krebs and Habermehl 1987 ). This may be correlated with the absence of the lysine residue (located in position 41 in the alignment of fig.…”

Section: Resultsmentioning

confidence: 99%

A Polychaete’s Powerful Punch: Venom Gland Transcriptomics of Glycera Reveals a Complex Cocktail of Toxin Homologs

Reumont

Campbell

Richter

et al. 2014

Genome Biology and Evolution

112

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Glycerids are marine annelids commonly known as bloodworms. Bloodworms have an eversible proboscis adorned with jaws connected to venom glands. Bloodworms prey on invertebrates, and it is known that the venom glands produce compounds that can induce toxic effects in animals. Yet, none of these putative toxins has been characterized on a molecular basis. Here we present the transcriptomic profiles of the venom glands of three species of bloodworm, Glycera dibranchiata, Glycera fallax and Glycera tridactyla, as well as the body tissue of G. tridactyla. The venom glands express a complex mixture of transcripts coding for putative toxin precursors. These transcripts represent 20 known toxin classes that have been convergently recruited into animal venoms, as well as transcripts potentially coding for Glycera-specific toxins. The toxins represent five functional categories: Pore-forming and membrane-disrupting toxins, neurotoxins, protease inhibitors, other enzymes, and CAP domain toxins. Many of the transcripts coding for putative Glycera toxins belong to classes that have been widely recruited into venoms, but some are homologs of toxins previously only known from the venoms of scorpaeniform fish and monotremes (stonustoxin-like toxin), turrid gastropods (turripeptide-like peptides), and sea anemones (gigantoxin I-like neurotoxin). This complex mixture of toxin homologs suggests that bloodworms employ venom while predating on macroscopic prey, casting doubt on the previously widespread opinion that G. dibranchiata is a detritivore. Our results further show that researchers should be aware that different assembly methods, as well as different methods of homology prediction, can influence the transcriptomic profiling of venom glands.

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Section: Resultsmentioning

confidence: 99%

A Polychaete’s Powerful Punch: Venom Gland Transcriptomics of Glycera Reveals a Complex Cocktail of Toxin Homologs

Reumont

Campbell

Richter

et al. 2014

Genome Biology and Evolution

112

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“…(a) Bovine pancreatic trypsin inhibitor [16]. (b) 6‐kDa protein (c) Sea anemone trypsin inhibitor [17]. (d) Snail ( Helix pomatia ) isoinhibitor K [18].…”

Section: Resultsmentioning

confidence: 99%

Primary structure and possible functions of a trypsin inhibitor of Bombyx mori

Kurioka

Yamazaki

Hirano

1999

European Journal of Biochemistry

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A protein with a low molecular mass of 6027 was purified from cocoon shell of silkworm, Bombyx mori. Twodimensional polyacrylamide gel electrophoresis (2D/PAGE) resolved this protein into a single spot with pI 4.3 and M r 6000. Amino acid sequence analysis revealed that this protein consists of 55 amino acids, six of these being cysteine residues and is highly homologous to bovine pancreatic trypsin inhibitor-type inhibitors. The 6-kDa protein is heat stable and acid stable and inhibits bovine trypsin by forming a low-dissociation complex with trypsin in a 1 : 1 molar ratio (K i = 2.8 £ 10 ±10 ), but does not a-chymotrypsin. This cocoon shell-associated trypsin inhibitor (CSTI) was thus concluded to belong to the bovine pancreatic trypsin inhibitor class. CSTI was developmentally regulated in the silk gland at the final stage of larval growth, and its specific distribution in the middle silk gland, an organ in which silk proteins are stored during the final larval instar, occurred before the onset of spinning. This inhibitor protects the tryptic degradation of fibroin light (L) chain in vitro. These results suggest that this trypsin inhibitor may play an important part on regulating proteolytic activity in the silk gland or protecting silk proteins from degradation during histolysis.Keywords: amino acid sequence; Bombyx mori; cocoon; trypsin inhibitor.The silkworm Bombyx mori produces massive amounts of silk proteins during the final stage of larval development (fifth instar), and these proteins are stored in the middle silk gland until they are discharged through the anterior duct and the spinneret at the end of the fifth instar. As major components of cocoons, two kinds of silk proteins have been distinguished: fibroin, a fibrous protein composed of one heavy (H) chain of about 350 kDa and a L-chain of about 25 kDa linked by disulfide bond(s); and sericin, serving as an adhesive to unite fibroin for making cocoons. The crystalline structures, chemical compositions and physical properties of the silk proteins have been extensively studied, but it is believed that these proteins in the cocoon shell are biologically inactive molecules. We previously have reported that four low-molecular-mass proteins are present in a water-soluble extract from the cocoon shell as minor components. These proteins with relative molecular masses of 10 kDa, 6 kDa, 4 kDa and 3 kDa were found to be distinct from both types of silk proteins on the basis of amino acid composition analysis [1,2]. N-terminal amino acid sequence analysis revealed that the 4-kDa protein was highly homologous to Kazal-type trypsin inhibitors [3]. Biologically active proteins would thus appear to quite likely coexist with silk proteins in the cocoon shell. Although trypsin and a-chymotrypsin inhibitors in the hemolymph of insects such as B. mori [4,5], Antheraea pernyi [6], Drosophila melanogaster [7] and Manduca sexta [8] have been demonstrated, such protease inhibitor has yet to be shown present in the cocoon shell.We here report the purification, protein se...

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“…Overall completeness evaluated in BUSCO ranged from 88.1% to 97.9% complete (Table 1). [80,81]. As noted above, these ShK toxins may also confer structural and/or functional properties of interest for pharmacological research.…”

Section: Results For Sequencing and De-novo Transcriptome Assembly Ofmentioning

confidence: 95%

“…For select toxin families, gene trees were constructed using a representative set of venomous and non-venomous proteins for each protein family, modified from phylogenetic analyses in von [80] and [47]. Candidate cerianthids toxins and were aligned using the L-INS-I algorithm in MAFFT v7.312 [153].…”

Section: Phylogenetic Analysis Of Select Gene Familiesmentioning

confidence: 99%

Transcriptomic analysis of four cerianthid (Cnidaria, Ceriantharia) venoms

Klompen

Macrander

Reitzel

et al. 2020

Preprint

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Tube anemones, or cerianthids, are a phylogenetically informative group of cnidarians 14 with complex life histories, including a pelagic larval stage and tube-dwelling adult stage, both 15 known to utilize venom in stinging-cell rich tentacles. Cnidarians are an entirely venomous group 16 that utilize their proteinaceous-dominated toxins to capture prey and defend against predators, in 17 addition to several other ecological functions, including intraspecific interactions. At present there 18are no studies describing the venom for any species within cerianthids. Given their unique 19 development, ecology, and distinct phylogenetic-placement within Cnidaria, our objective is to 20 evaluate the venom-like gene diversity of four species of cerianthids from newly collected 21 transcriptomic data. We identified 525 venom-like genes between all four species. The venom-gene 22 profile for each species was dominated by enzymatic protein and peptide families, which is 23 consistent with previous findings in other cnidarian venoms. However, we found few toxins that 24 are typical of sea anemones and corals, and furthermore, three of the four species express toxin-like 25 genes closely related to potent pore-forming toxins in box jellyfish. Our study is the first to provide 26 a survey of the putative venom composition of cerianthids, and contributes to our general 27 understanding of the diversity of cnidarian toxins. 28 29 30 1. Introduction 31The phylum Cnidaria (sea anemones, corals, jellyfish, box jellies, hydroids/hydromedusae, 32 etc.) is the earliest diverging venomous lineage (~ 600 million years) [1,2]. Cnidaria deliver their 33 proteinaceous-dominant venom through organelles called nematocysts (a type of cnidae), housed in 34 cells called nematocytes [3,4]. Venom from discharged nematocysts is used in prey capture and 35 defense against predation, but cnidarians also use venom for a variety of other behaviors, such as 36 intraspecific competition [5][6][7] and maternal care [8] (see review by [9]). This ecological diversity is 37 complemented by the functional diversity of cnidarian venoms, which can include neurotoxic, 38 cytotoxic, and enzymatic (e.g. phospholipase and metalloprotease) proteins and peptides, in 39 addition to non-peptidic components [10,11]. For humans, stings from certain species can cause 40 intense localized pain, scarring, induced anaphylaxis, and in the worst cases, cardiac and 41 respiratory failure leading to death [12][13][14][15]. The venom of medically relevant species, such as the 42 Portuguese Man-o-War (Physalia physalis) [16][17][18] and several species of box jellyfish ([19-22], 43 reviewed in [23]), or easy to collect species, such as sea anemones [24,25], have been explored more 44 extensively at a biochemical and pharmacological level [26]. However, these species represent a 45 small fraction of the species diversity within the group, and only recently has the exploration the 46 2 venom composition for a wider number of cnidarians increased in an effort to characterize the 4...

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Isolierung und Strukturaufkl�rung eines h�molytisch aktiven Peptids aus der Seeanemone Metridium senile

Cited by 12 publications

References 10 publications

A Polychaete’s Powerful Punch: Venom Gland Transcriptomics of Glycera Reveals a Complex Cocktail of Toxin Homologs

A Polychaete’s Powerful Punch: Venom Gland Transcriptomics of Glycera Reveals a Complex Cocktail of Toxin Homologs

Primary structure and possible functions of a trypsin inhibitor of Bombyx mori

Transcriptomic analysis of four cerianthid (Cnidaria, Ceriantharia) venoms

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