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The putative neurotoxins are characterized N-terminally by an ICK motif, a fourth disulfide bridge C6—C7 , and a C-terminal tail composed of five to 15 amino acid residues. CsTx 8. Its signal and pro-peptide sequence exhibits a high identity The mature peptides show a lower identity of Amino acid residue differences within the different subgroups are given in red characters, C-terminal amidation is highlighted in green, and cysteines are highlighted in black.
Not shown are identical amino acid sequences with silent and visible mutations within the signal and pro-peptide. CsTx 0. For CsTx 1. A peptide similar to CsTx 0. This peptide inhibits L-type calcium channels [ 93 ], produces paralysis in the posterior limbs and decreases movements after intracerebro-ventricular injection in mice [ 94 ].
Moreover, an identity of The identity towards CsTx is very high In our in-house hemocyte transcriptome of C. The agatoxin-like peptide from hemocytes exhibits Surprisingly, the agatoxin-like peptide shows identities between It may be possible that this widespread peptide from the neuronal tissue of several major arthropod groups was convergently recruited into the venom glands of different venomous arthropods [ 98 ].
Sequence relationship was calculated using Bayesian inference methods. Sequences derived from venom gland transcriptomes are highlighted in dark gray, sequences from transcriptomes of other tissues or genomes in light gray. Nodes are labeled with posterior probability values. The peptide sequences used for analysis are accessible online with the following sequence identifiers: C. Recruitment of agatoxin-like tissue peptides occurs not only in the venom glands of spiders, but also in the venom glands of pseudoscorpions.
In such a venom gland transcriptome of Synsphyronus apimelus , 11 transcripts have been identified that exhibit high identities with precursors from different spiders [ 65 ]. With seven disulfide bridges, these putative neurotoxins exhibit the highest number of cysteines in venomous peptides so far identified in spider venoms. They show identities between Multiple sequence alignment of mature peptides belonging to different low abundant peptide families.
Amino acid residue differences within the different subgroups are given in red characters, C-terminal amidation is highlighted in green, post-translational removal of amino acid residues is given in yellow, and cysteines are highlighted in black. The peptide exhibits high identities with transcripts from pisaurids Moreover, CsTx exhibits an identity of Besides CsTx-1, we identified another putative neurotoxin, CsTxa, b, c 0.
This stretch is at minimum twice as long as the longest C-terminal stretch identified in peptides of other spider families and might be an innovation of C. Identities of So far, an Interpro scan could not identify any known protein family memberships for both peptide groups.
CsTxa, CsTxb, CsTxc shows high identities with putative neurotoxins from other spiders, such as pisaurids Therefore, it is tempting to speculate that this family of putative neurotoxins could be widespread at least among entelegyne spiders Supplementary Figure S2. The peptide shows identities between With CsTx 0. PT1, which shows antinociceptive activity by the inhibition of P2X3 receptors of rat dorsal root sensory neurons [ ], was first isolated from the lycosid Alopecosa marikovskyi.
In contrast to the conserved sequences of mature peptides, signal peptide and pro-peptide exhibit lower sequence identities, between Dibasic motifs have been postulated to serve as pro-peptide cleavage sites in some neurotoxin precursors of mygalomorph spiders. This presence of multiple known cleavage motifs at possible pro-peptide cleavage sites shows the importance of proteomic data for accurate determination of the actual cleavage site.
Proteomic top-down analysis revealed that, in the case of CsTx, the PQM motif is used as pro-peptide-cutting site. In contrary, CsTx and some peptides of H. Further investigations are needed to explain the observed specificity in pro-peptide cleavage. However, we observed an evident similarity between the nucleotide sequences of the non-dibasic motif containing CsTx-9, , , and CsTx in the region of the pro-peptide-mature peptide junction Figure 7 B , possibly indicating an evolutionary relationship of these transcript parts.
The only mutations within the first 21 N-terminal nucleotides of the mature peptides of CsTx, , and are two point-mutations causing the dibasic motif in CsTx Identification of different pro-peptide cleavage motifs in one precursor. The sequence parts shown include the ends of pro-peptides and the beginning of mature peptides.
The start of the mature peptide sequences is indicated with a bold red line. Amino acids of the mature peptide are in bold. Potential protease cleavage motifs are displayed in dashed boxes. Red boxes indicate the cleavage motif, which directly locates the N-terminal of the experimentally found start of the mature peptide.
B Sequence comparison of transcripts coding for CsTx and other C. Nucleotides differing between sequences are highlighted in red. Top-down proteomics of CsTx revealed another post-translational modification of the CsTx precursor. The last twelve C-terminal amino acid residues are post-translationally removed. This post-translational modification is comparable to the processing of the precursors of CsTx-8, 12, and 13 by the PQM-protease and a so far unknown carboxypeptidase [ 25 ] Figure 6.
The mature chains of CsTx and CsTx are less variable than their signal and pro-peptides when compared with the corresponding peptides of other related spiders. These findings are in contrast to the present opinion that the predominant mutation sites should be in the mature peptides when comparing peptides within a peptide family of one species. However, Kozlov and coworkers showed, for putative neurotoxin precursors of D.
A high identity of The disulfide bridge pattern for the present Cys-containing peptides has not yet been solved. Interestingly, this cysteine pattern is widespread within spiders of the RTA clade and can be found in pisaurids The post-translational modification of this peptide by a PQM protease produces a heterodimeric structure as shown previously [ 25 ].
This also holds true for the related sequences in the above-mentioned spider families. The resulting long chain, C-terminally comprises 10 amino acids after the last Cys residue. This C-terminal part is about two times longer than the corresponding sequence lengths of CsTx-8, , and Such long chains might be highly flexible and may interact with other peptides, resulting in increased toxic activity, comparable to CsTx-8, CsTx, and CsTx Related precursors have been identified only in lycosids As a result of top-down proteomics, post-translational modification has been identified for CsTx Here again, the C-terminal Arg residue is removed by an unknown carboxypeptidase [ 25 ] Supplementary Figure S2.
All these peptides possess five disulfide bridges Figure 8. Amino acid residue differences within the different subgroups are given in red characters, and cysteines are highlighted in black. With 86 amino acid residues and a molecular mass of 9. Interpro sequence analysis showed no relationship to any protein family and no domain could be identified. In contrast to MIT1 only Blast results show a broad distribution of CsTx homologs in araneomorph spiders of the RTA clade pisaurids, Identifying similar peptides in spider and scorpion venoms points to a common ancient precursor or a convergent evolution in both arachnid orders.
So far, no biological activity is described for these peptides isolated from spider and scorpion venom Supplementary Figure S2. Interpro analysis shows that CsTxa, b, c comprise the prokineticin domain IPR nearly over the whole length of the peptides amino acid residues 5—59, CsTx but the crucial N-terminal AVIT sequence part, responsible for its biological activity, is lacking. The prokineticin domain is identified in several putative toxin precursors from different araneomorph and mygalomorph spiders, but also, surprisingly, from ticks.
Sequence identities between CsTxa, b, c and such peptides are medium to high: for araneomorph spiders Sequence alignments even show CsTxa, b, c, d, e, f, g are classified as belonging to the atracotoxin family IPR They share sequence homologies to the above-mentioned MIT1 and Bm8f, but no pharmacological activity or biological function in the venom is known. Mature CsTx isoforms show amino acid sequence identities to peptides of other araneomorph spider in the range of Taking all arguments into account, it is most likely that CsTxa, b, c, d, e, f, g, and CsTxa, b, c can be classified as peptides that might exhibit the ancestral disulfide-directed beta-hairpin DDH domain as shown for the nontoxic atracotoxin-Hvf17 ACTX—Hvf17 identified in the atracid Hadronyche infensa.
Together with the determined disulfide bridge pattern of CsTx, it seems that CsTx, 21, and 22 are the only peptides in the venom of C. Identifying related peptides to CsTx, 21, and 22, not only in araneomorph and mygalomorph spider venoms [ ], but also in the venom of scorpions [ ], pseudoscorpions [ 65 ], and in the salivary glands of ticks [ ], may give a clue that these peptides may be one of the first compounds recruited into venom and salivary glands.
Unfortunately, their targets still need to be elucidated. We identified a defensin-like peptide in the venom gland, with a so far unknown function, which we named defensin Transcripts coding for this peptide have not been identified in our C. Neither reverse-transcriptase-PCR nor sequencing showed any expression in the venom glands of the spider [ ].
Illumina sequencing, however, revealed defensin-1 and defensin-2 homolog transcripts in the venom glands of Cupiennius getazi , a sister species of C. It is tempting to assume that this inconsistency is due to the higher read-depth of Illumina sequencing compared to sequencing, allowing to detect very low-abundant transcripts that may emerge from a few hemocytes present in dissected venom glands. The amino acid differences between hemocyte defensins-1 from both sister species are small The same holds true for defensins-2 from venom glands Multiple sequence alignment of mature defensin-like peptides from different arachnids and types of tissue.
Sequences belong to the spiders C. Defensins so far identified in other arachnids show higher sequence identities to C. In fact, BmKDfsin4 shows inhibitory activity against Gram-positive bacteria, and potassium channel current-blocking activity. It is hypothesized that scorpion defensins and some scorpion neurotoxins originated from one precursor [ 83 , ]. To the best of our knowledge, it is the first time that a venom gland-specific defensin has been identified in spider venom.
Further investigations are necessary to elucidate the recruitment and possible neofunctionalization of defensins in terms of antimicrobial and potassium channel-blocking activities of these spider venom gland peptides. We used a combined approach of top-down and bottom-up mass spectrometry to validate the sequence of venom-neurotoxins and -proteins identified on the transcriptome level. From a total of 54 putative neurotoxins and their mature peptide isoforms identified by transcriptome analysis, we validated the presence of 49 by mass spectrometry of venom fractions Supplementary Figure S4.
The venom presence of all proteins identified on the transcriptome level, except for the house keeping protein signal peptidase, could be validated with high sequence coverages Table 1 , Supplementary Figures S1. Proteomic analysis is inevitable for identification or validation of post-translational modifications.
Thereby, mass spectrometric analysis of undigested peptides top-down proteomics proved to be highly suitable to identify post-translational processing by proteases as discussed to occur in precursors of CsTx-8, , , , and including the allocation of the cleaved signal peptide e. However, very low-expressed peptides or large proteins could not be assessed by top-down proteomics.
In such cases, mass spectrometric analysis of digested peptides bottom-up proteomics , using multiple proteases for digestion, provided a reasonable alternative with high sensitivity and sequence coverage Table 2 , Supplementary Table S1. High sensitivity and sequence coverage are thereby the key to validate low-expressed peptides and highly similar isoforms of peptides. In addition to mature peptides, we also surprisingly identified fragments of pro-peptides of some neurotoxins by bottom-up proteomics.
It is tempting to assume that these identifications indicate the presence of immature peptides comprising unprocessed pro- peptides and mature peptides in the venom or trace amounts of cleaved-off intact pro-peptides. The presence of high quantities of intact pro-peptides, however, is not likely as pro-peptides of CsTx-1 and CsTx could not be observed by the anion exchange chromatography of venom Supplementary Figure S5.
Previously published data on low molecular mass compounds [ 92 , ] and cytolytic peptides cupiennins [ , ], together with the here presented proteins and putative neurotoxins open a holistic view on the synergistic mode of action of C. Analyzing all interacting compounds, we hypothesize a specific and an unspecific prey inactivation pathway, resulting in a dual prey-inactivation strategy Figure Dual prey-inactivation strategy of the venom of C. Main interactions of the major venom components are shown in the venom gland upper half and, after venom injection, in the target organism lower half.
The specific pathway, mainly based on neurotoxins and other compounds, usually leads to death. The unspecific or metabolic pathway, based on a variety of regulatory elements, disturbs homeostasis or leads to hyperglycemia. The thickness of the gray arrows indicates the estimated impact on the prey.
Dashed lines represent vague or uninvestigated connections for further details compare text. Compounds of the specific pathway are neurotoxins, low molecular mass compounds, a highly active hyaluronidase, phospholipase A2 and the cupiennins. In the specific pathway, a great variety of neurotoxins act synergistically [ 26 ], but also with small molecular mass compounds and cupiennins, all affecting ion channel targets of the nervous system and in muscle tissues, finally resulting in paralysis, convulsion and death.
The spreading of these toxins into the tissue is supported by hyaluronidase, phospholipase A2 and the cupiennins, through destruction of negatively charged membrane types. The unspecific inactivation pathway is characterized by different enzymes, which play a central part by interacting with the regulation of important metabolic pathways, thus unbalancing the homeostasis of an organism.
Furthermore, some of the cupiennins inhibit the formation of nitric oxide by neuronal nitric oxide synthase, which dramatically disturbs numerous processes using nitric oxide as a neurotransmitter [ ].
The dual prey-inactivation strategy of spiders reduces the development of resistance against single venom compounds and the risk of losing prey due to escape. We roughly divide the proteins mentioned here into three different groups with overlapping functions. Most of these proteins, identified on a transcriptomic and proteomic site in C.
This wide distribution may be an example of convergent evolution, especially when the glands, where these substances are expressed, are not homologous. In contrast with other spider venoms, the number of different neurotoxin families and neurotoxins in C. Eleven further neurotoxin families are present in the venom in low concentrations; they may belong to a common heritage of spider toxins, but their evolutionary origin remains unclear.
Our detection of the first spider venom gland-specific defensin and its origin in hemocytes offers a fascinating possibility to track the origin of toxic compounds, the so-called neofunctionalization, and provides insight into the process that leads from a nontoxic to a toxic compound. Moreover, comparable transcriptomic studies of venom glands of different spider families may be a fascinating approach to filter out the essential constellation of venomous components present in each spider venom.
Such a constellation might yield a principal composition that is not only realized in spider venoms, but also in the venoms of other arachnids. Breeding of Cupiennius salei and venom collection were done as described earlier [ ]. The cDNA libraries of venom glands and hemocytes of C.
For transcriptomic studies, Ancylometes rufus, Viridasius fasciatus and Cupiennius getazi were laboratory-bred. Oxyopes heterophthalmus, Oxyopes lineatus, and Cheiracanthium sp. Nephila pilipes was collected in Taiwan, and Xysticus cristatus and Atypus piceus in Switzerland. No specific permissions for collecting the spiders were required. Collections were done on publicly accessible land without any protection status, such as common land. None of the spiders described here belongs to a protected or endangered species.
Structural analysis of the protein domains was performed using InterPro [ ], and classification of the sequences into different families with HMMcompete [ 79 ] that had to be enlarged to cover a wider number of neurotoxins. Information about the secondary structure of the peptides was obtained using the GOR IV secondary-structure prediction method [ ]. All obtained contigs and the corresponding reads, referring to venom gland-specific proteins, putative neurotoxins, and peptides, were further analyzed on the nucleotide level to detect transcript isoforms.
We analyzed the venom proteome of C. Peptide-containing fractions 2—7 were additionally analyzed with a top-down proteomic approach. The column effluent was directly coupled with the mass spectrometer via a nanoflex electrospray source Thermo Fischer, Bremen, Germany. For top-down proteomics, ng of reduced and alkylated protein was analyzed on the same nano-LC-MS 2 setup as for bottom-up.
Top-down data were analyzed using the TopPIC suite [ ]. The resulting files were used for deconvolution with TopFD version 1. The output files were used for identification of proteoforms with TopPIC version 1. For analysis of the bottom-up proteomic data, fragment spectra peak list files were generated as mzXML files with MSConvert version 3. Interpretation of fragment spectra was done with the search engines Comet version Statistical validations of peptide identifications were performed using Peptide Prophet [ ] implemented in TPP version 5.
Protein and peptide match tables are available as supporting information Supplementary Dataset EV3. The Bayesian tree was estimated from a cropped and manually validated amino acid sequence alignment of C. We ran Mr. Bayes version 3. Trees were sampled every generations. Other parameters were left at default values.
Conceptualization: L. Toxins Basel. Published online Mar Find articles by Lucia Kuhn-Nentwig. Find articles by Nicolas Langenegger. Find articles by Wolfgang Nentwig. Author information Article notes Copyright and License information Disclaimer. Received Mar 5; Accepted Mar This article has been cited by other articles in PMC.
Associated Data Supplementary Materials toxinss Abstract Most knowledge of spider venom concerns neurotoxins acting on ion channels, whereas proteins and their significance for the envenomation process are neglected. Introduction With more than 47, species [ 1 ], spiders are the most species-rich terrestrial invertebrate group after insects.
Results and Discussion 2. Open in a separate window. Figure 1. Table 1 Overview of the main identified proteins in the venom glands of C. Proteins of the Protein- and Peptide-Processing Machinery 2. Signal Peptidase SPase Removal of the signal peptide of protein and peptide precursors by SPase is the initial step in the translocation of excretory and secretory proteins across the ER membrane [ 19 ].
Protein Disulfide-Isomerase PDI This enzyme, located in the ER, catalyzes the formation and breakage of disulfide bonds during the folding of proteins and peptides. Venom Serine Proteases VSPs Most biologically active spider venom peptides comprise a pro-peptide that is removed during the maturation process. Carboxypeptidase A-Like Protein CPA Within the maturation process of precursors, the next step requires a carboxypeptidase for the removal of the C-terminal Arg in heterodimeric neurotoxins and the C-terminus of cytolytic peptide precursors [ 25 , 26 , 28 ].
Recruited and Neofunctionalized Proteins Recruitment of genes in the venom glands and neofunctionalization after gene duplication is thought to be the origin of venomous peptides and proteins in venom glands of not only arthropods but also other animals. Angiotensin-Converting Enzyme ACE ACE-like enzymes are known from the venom gland transcriptome of Phoneutria nigriventer [ 11 ] and of scorpions [ 51 , 52 ], but also from the salivary glands of hematophagous insects [ 53 ].
Phospholipase A2 PLA2 PLA2 activity was identified in the venom of different spider families, such as eresids, miturgids, lycosids, and hexathelids, indicating a widespread existence of the enzyme [ 3 ]. Cystatin CST CSTs occur in prokaryotes and eukaryotes [ 59 ], and have been identified in the venom glands of invertebrates and vertebrates [ 31 , 60 ]. Proteins Belonging to the Innate Immune System 2. Cysteine-Containing Putative Neurotoxins To obtain comparable expression data of different neurotoxins, besides real-time PCR, two possibilities exist.
Table 2 Overview of the 56 identified putative neurotoxins und their cysteine framework in the venom glands of C. Figure 2. Signal Peptides and Pro-peptides of Putative Neurotoxins The lengths of the signal peptides of the precursors described here vary only between 16 and 22 amino acid residues, and are independent from the lengths of pro-peptides and mature peptides. Figure 3. Figure 4. Figure 5. Figure 6. Figure 7. Figure 8.
Defensin-Like Peptide We identified a defensin-like peptide in the venom gland, with a so far unknown function, which we named defensin Figure 9. Proteomics We used a combined approach of top-down and bottom-up mass spectrometry to validate the sequence of venom-neurotoxins and -proteins identified on the transcriptome level.
The Dual Prey-Inactivation Strategy of Spiders Previously published data on low molecular mass compounds [ 92 , ] and cytolytic peptides cupiennins [ , ], together with the here presented proteins and putative neurotoxins open a holistic view on the synergistic mode of action of C. Figure Conclusions We roughly divide the proteins mentioned here into three different groups with overlapping functions.
Materials and Methods 4. Tandem Mass Spectrometry We analyzed the venom proteome of C. Sequence Analysis The Bayesian tree was estimated from a cropped and manually validated amino acid sequence alignment of C. Click here for additional data file. Author Contributions Conceptualization: L. Conflicts of Interest The authors declare no conflict of interest. References 1. Natural History Museum Bern; [ accessed on 11 September ].
World Spider Catalog. Version Wise D. Spiders in Ecological Webs. Kuhn-Nentwig L. Venom composition and strategies in spiders: Is everything possible? Insect Physiol. Saez N. Spider-venom peptides as therapeutics. Smith J. The insecticidal potential of venom peptides. Life Sci. The venom gland transcriptome of Latrodectus tredecimguttatus revealed by deep sequencing and cDNA library analysis.
Oldrati V. Peptidomic and transcriptomic profiling of four distinct spider venoms. Zhang Y. Toxin diversity revealed by a transcriptomic study of Ornithoctonus huwena. Biner O. Isolation, N-glycosylations and function of a hyaluronidase-like enzyme from the venom of the spider Cupiennius salei. Pedroso A.
BMC Evol. Diniz M. An overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches. Venom of Cupiennius salei. In: Gopalakrishnakone P. Spider Venoms. Trachsel C. Multicomponent venom of the spider Cupiennius salei : A bioanalytical investigation applying different strategies. FEBS J.
Barth F. Springer; Berlin, Germany: A Venom-derived neurotoxin, CsTx-1, from the spider Cupiennius salei exhibits cytolytic activities. Finn R. The Pfam protein families database: Towards a more sustainable future. Nucleic Acids Res. Malli H. Purification, cDNA structure and biological significance of a single insulin-like growth factor-binding domain protein SIBD-1 identified in the hemocytes of the spider Cupiennius salei.
Insect Biochem. Auclair S. Signal peptidase I: Cleaving the way to mature proteins. Protein Sci. Rawlings N. Ali Khan H. Protein disulfide isomerase a multifunctional protein with multiple physiological roles. Logunov D. Arthropoda Selecta. Veenstra J. Mono- and dibasic proteolytic cleavage sites in insect neuroendocrine peptide precursors. Kozlov S. The universal algorithm of maturation for secretory and excretory protein precursors.
Langenegger N. Identification of a precursor processing protease from the spider Cupiennius salei essential for venom neurotoxin maturation. Wullschleger B. CSTX, a highly synergistically acting two-chain neurotoxic enhancer in the venom of the spider Cupiennius salei Ctenidae Proc. A lysine rich C-terminal tail is directly involved in the toxocity of CSTX-1, a neurotoxic peptide from the venom of the spider Cupiennius salei.
Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi Zodariidae that exemplify biomolecular diversity. Ouafik L. Undheim E. Weaponization of a hormone: Convergent recruitment of hyperglycemic hormone into the venom of arthropod predators. Fry B. The toxicogenomic multiverse: Convergent recruitment of proteins into animal venoms.
Zhang Z. Transcriptome profiles reveal the crucial roles of hormone and sugar in the bud dormancy of Prunus mume. Mehta D. Bacterial and archaeal alpha-amylases: Diversity and amelioration of the desirable characteristics for industrial applications. Avwioroko O. Isolation, identification and in silico analysis of alpha-amylase gene of Aspergillus niger strain CSA35 obtained from cassava undergoing spoilage.
Boehlke C. Salivary amylase—The enzyme of unspecialized euryphagous animals. Oral Biol. DeLay B. Transcriptome analysis of the salivary glands of potato leafhopper, Empoasca fabae. Mommsen T. Fuzita F. High throughput techniques to reveal the molecular physiology and evolution of digestion in spiders. BMC Genom. Lipovsek S. Changes in the midgut diverticula in the harvestmen Amilenus aurantiacus Phalangiidae, Opiliones during winter diapause.
Arthropod Struct. Smrz J. Microwhip scorpions Palpigradi feed on heterotrophic cyanobacteria in Slovak caves—A curiosity among Arachnida. Tang B. Invertebrate trehalosephosphate synthase gene: Genetic architecture, biochemistry, physiological function, and potential applications. Gronke S. Molecular evolution and functional characterization of Drosophila insulin-like peptides. PLoS Genet. Kerekes E. Suren-Castillo S. FoxO is required for the activation of hypertrehalosemic hormone expression in cockroaches.
Post S. Graham P. Drosophila as a model for diabetes and diseases of insulin resistance. Milne T. Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily. Hansson K. A single gamma-carboxyglutamic acid residue in a novel cysteine-rich secretory protein without propeptide. Qian J. Cloning and isolation of a Conus cysteine-rich protein homologous to Tex31 but without proteolytic activity.
Acta Biochim. Assumpcao T. Cajado-Carvalho D. Insights into the hypertensive effects of Tityus serrulatus scorpion venom: Purification of an angiotensin-converting enzyme-like peptidase. Proteomic endorsed transcriptomic profiles of venom glands from Tityus obscurus and T.
Hernandez-Vargas M. Proteomic and transcriptomic analysis of saliva components from the hematophagous reduviid Triatoma pallidipennis. Yan H. The angiotensin-converting enzyme ACE gene family of Bombyx mori. Yamagishi T. Glucose, some amino acids and a plant secondary metabolite, chlorogenic acid induce the secretion of a regulatory hormone, tachykinin-related peptide, from the silkworm midgut.
Scott D. Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue. Shipolini R. The amino-acid sequence and carbohydrate content of phospholipase A2 from bee venom. Valdez-Cruz N.
Sequence analysis and phylogenetic relationship of genes encoding heterodimeric phospholipases A2 from the venom of the scorpion Anuroctonus phaiodactylus. Kordis D. Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes. Tan K.
Comparative venom gland transcriptomics of Naja kaouthia monocled cobra from Malaysia and Thailand: Elucidating geographical venom variation and insights into sequence novelty. Turk V. Cystatins: Biochemical and structural properties, and medical relevance. Salat J. Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata.
Choo Y. Antifibrinolytic role of a bee venom serine protease inhibitor that acts as a plasmin inhibitor. Zhao R. SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. Santibanez-Lopez C. Transcriptomic analysis of pseudoscorpion venom reveals a unique cocktail dominated by enzymes and protease inhibitors. Wan H. A spider-derived Kunitz-type serine protease inhibitor that acts as a plasmin inhibitor and an elastase inhibitor. Soares T. Expression and functional characterization of boophilin, a thrombin inhibitor from Rhipicephalus Boophilus microplus midgut.
Tsujimoto H. Simukunin from the salivary glands of the black fly Simulium vittatum inhibits enzymes that regulate clotting and inflammatory responses. Corral-Rodriguez M. Tick-derived Kunitz-type inhibitors as antihemostatic factors. Peigneur S. A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties.
Venom gland transcriptomic and proteomic analyses of the enigmatic scorpion Superstitionia donensis Scorpiones: Superstitioniidae , with insights on the evolution of its venom components. Anatriello E. An insight into the sialotranscriptome of the brown dog tick, Rhipicephalus sanguineus.
Mihelic M. Two decades of thyroglobulin type-1 domain research. Chandler J. Understanding insulin endocrinology in decapod Crustacea: Molecular modelling characterization of an insulin-binding protein and insulin-like peptides in the eastern spiny lobster, Sagmariasus verreauxi. Mulenga A. The molecular basis of the Amblyomma americanum tick attachment phase. Gokudan S. Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen.
Kawabata S. Role of tachylectins in host defense of the Japanese horseshoe crab Tachypleus tridentatus. Maeda H. Identification of the Babesia -responsive leucine-rich repeat domain-containing protein from the hard tick Haemaphysalis longicornis.
Koua D. Spider neurotoxins, short linear cationic peptides and venom protein classification improved by an automated competition between exhaustive profile HMM classifiers. King G. A rational nomenclature for naming peptide toxins from spiders and other venomous animals.
Norton R. Newell Power Electronics award as well as a dozen of other awards. D study in Bayreuth University Germany. He currently works as a Professor at the same department. He has authored or co-authored many scientific papers and chaired a serial conference European Conference on Renewable Energy Systems since He has served as a guest editor for several SCI-indexed special issue journals.
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