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A series of cyclohumulanoids, i.e., tricocerapicanols A–C (1a–1c), tricoprotoilludenes A (2a) and B (3), tricosterpurol (4), and tricoilludins A–C (5–7) were isolated along with known violascensol (2b) and omphadiol (8) from the culture broth of Daedaleopsis tricolor, an inedible but not toxic mushroom. The structures were fully elucidated on the basis of NMR spectroscopic analysis, and the suggested relative structures were confirmed via density functional theory (DFT)-based chemical shift calculations involving a DP4 probability analysis. In the present study, the 1H chemical shifts were more informative than the 13C chemical shifts to distinguish the diastereomers at C-11. The absolute configurations of 1–5 were determined by comparing the experimental and calculated electronic circular dichroism (ECD) spectra. For 6 and 7, the same chirality was assigned according to their biosynthetic similarities with the other compounds. The successful assignment of some Cotton effects was achieved by utilizing DFT calculations using simple model compounds. The plausible biosynthesis of 1–7 was also discussed on the basis of the structural commonality and general cyclohumulanoid biosynthesis. Compounds 2a and 5 were found to simultaneously induce hyphal swelling and branching at 5.0 μg/mL against a test fungus Cochliobolus miyabeanus.
Ryuhi Kanehara; Akio Tonouchi; Katsuhiro Konno; Masaru Hashimoto. Cyclohumulanoid Sesquiterpenes from the Culture Broth of the Basidiomycetous Fungus Daedaleopsis tricolor. Molecules 2021, 26, 4364 .
AMA StyleRyuhi Kanehara, Akio Tonouchi, Katsuhiro Konno, Masaru Hashimoto. Cyclohumulanoid Sesquiterpenes from the Culture Broth of the Basidiomycetous Fungus Daedaleopsis tricolor. Molecules. 2021; 26 (14):4364.
Chicago/Turabian StyleRyuhi Kanehara; Akio Tonouchi; Katsuhiro Konno; Masaru Hashimoto. 2021. "Cyclohumulanoid Sesquiterpenes from the Culture Broth of the Basidiomycetous Fungus Daedaleopsis tricolor." Molecules 26, no. 14: 4364.
Purification of small peptide components in the venoms of the solitary sphecid wasps, Sphex argentatus argentatus and Isodontia harmandi, led to the isolation of several major peptides. Analysis of MS/MS spectra by MALDI-TOF/TOF revealed the sequence of a new peptide Sa112 (EDVDHVFLRF-NH2), which is structurally very similar to leucomyosupressin (pQDVDHVFLRF-NH2) and SchistoFLRFamide (PDVDHVFLRF-NH2), the FMRFamide-like peptides from cockroach and locust, respectively. Indeed, this new peptide, like SchistoFLRFamide, inhibited the frequency and amplitude of spontaneous contractions of the locust oviduct in a dose-dependent manner. A non-amidated peptide Sa12b (EDVDHVFLRF) was also isolated, but this peptide had no effect on spontaneous locust oviduct contraction. This is the first example of a FMRF-like peptide to be found in solitary wasp venom. Additionally, a truncated form of the myosuppressins, which has previously been synthesized and tested for biological activity, DVDHVFLRF-NH2 (Sh5b), was found for the first time as a natural product. Four other novel peptides were isolated and characterized as Sa81 (EDDLEDFNPTVS), Sa10 (EDDLEDFNPTIA), Sh41 (DDLSDFNPKV), and Sh42 (EDDLSDFNPKV). They are structurally related to each other, having a high content of acidic amino acids, but no structural similarity to any known peptides. Ion channel associated activities of Sh41 and Sh42 were tested, but did not show any activity for Na+, K+, Ca2+ channels.
Ken-Ichi Nihei; Steve Peigneur; Jan Tytgat; Angela B. Lange; Katsuhiro Konno. Isolation and characterization of FMRFamide-like peptides in the venoms of solitary sphecid wasps. Peptides 2021, 142, 170575 .
AMA StyleKen-Ichi Nihei, Steve Peigneur, Jan Tytgat, Angela B. Lange, Katsuhiro Konno. Isolation and characterization of FMRFamide-like peptides in the venoms of solitary sphecid wasps. Peptides. 2021; 142 ():170575.
Chicago/Turabian StyleKen-Ichi Nihei; Steve Peigneur; Jan Tytgat; Angela B. Lange; Katsuhiro Konno. 2021. "Isolation and characterization of FMRFamide-like peptides in the venoms of solitary sphecid wasps." Peptides 142, no. : 170575.
Solitary wasp venoms may be a rich source of neuroactive substances, since their venoms are used for paralyzing preys. We have been exploring bioactive constituents of solitary wasp venoms and, in this study, the component profile of the venom from a solitary scoliid wasp, Scolia decorata ventralis, was investigated through a comprehensive analysis using LC-MS. Two peptides were synthesized, and their neuroprotective properties were evaluated. A reverse-phase HPLC connected to ESI-MS was used for LC-MS analyses. Online mass fingerprinting was performed from TIC, and data-dependent tandem mass spectrometry gave the MS/MS spectra. The sequences of two major peptide components were determined by MALDI-TOF/TOF MS analysis, confirmed by solid phase synthesis. Using the synthetic peptides, biological activities were assessed. Cell integrity tests and neuroprotection analyzes using H2O2 as an oxidative stress inducer were performed for both peptides. Online mass fingerprinting revealed that the venom contains 123 components, and the MS/MS analysis resulted in 33 full sequences of peptide components. The two main peptides, α-scoliidine (DYVTVKGFSPLR) and β-scoliidine (DYVTVKGFSPLRKA), present homology with the bradykinin C-terminal. Despite this, both peptides did not behave as substrates or inhibitors of ACE, indicating that they do not interact with this metallopeptidase. In further studies, β-scoliidine, but not α -scoliidine, showed protective effects against oxidative stress-induced neurotoxicity in PC12 cells through integrity and metabolism cell assays. Interestingly, β-scoliidine has the extension of the KA dipeptide at the C-terminal in comparison with α-scoliidine. Comprehensive LC-MS and MS/MS analyses from the Scolia decorata ventralis venom displayed the component profile of this venom. β-scoliidine showed an effective cytoprotective effect, probably due to the observed increase in the number of cells. This is the first report of solitary wasp venom peptides showing neuroprotective activity.
Carlos Alberto-Silva; Fernanda Calheta Vieira Portaro; Roberto Tadashi Kodama; Halyne Queiroz Pantaleão; Marisa Rangel; Ken-Ichi Nihei; Katsuhiro Konno. Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis. Journal of Venomous Animals and Toxins including Tropical Diseases 2021, 27, 1 .
AMA StyleCarlos Alberto-Silva, Fernanda Calheta Vieira Portaro, Roberto Tadashi Kodama, Halyne Queiroz Pantaleão, Marisa Rangel, Ken-Ichi Nihei, Katsuhiro Konno. Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis. Journal of Venomous Animals and Toxins including Tropical Diseases. 2021; 27 ():1.
Chicago/Turabian StyleCarlos Alberto-Silva; Fernanda Calheta Vieira Portaro; Roberto Tadashi Kodama; Halyne Queiroz Pantaleão; Marisa Rangel; Ken-Ichi Nihei; Katsuhiro Konno. 2021. "Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis." Journal of Venomous Animals and Toxins including Tropical Diseases 27, no. : 1.
Arthropods comprise a predominant and well-succeeded phylum of the animal kingdom that evolved and diversified in millions of species grouped in four subphyla, namely, Chelicerata (arachnids), Crustacea, Myriapoda (centipedes), and Hexapoda (insects)
Gandhi Rádis-Baptista; Katsuhiro Konno. Arthropod Venom Components and Their Potential Usage. Toxins 2020, 12, 82 .
AMA StyleGandhi Rádis-Baptista, Katsuhiro Konno. Arthropod Venom Components and Their Potential Usage. Toxins. 2020; 12 (2):82.
Chicago/Turabian StyleGandhi Rádis-Baptista; Katsuhiro Konno. 2020. "Arthropod Venom Components and Their Potential Usage." Toxins 12, no. 2: 82.
In this work, we evaluate the effect of two peptides Sa12b (EDVDHVFLRF) and Sh5b (DVDHVFLRF-NH2) on Acid-Sensing Ion Channels (ASIC). These peptides were purified from the venom of solitary wasps Sphex argentatus argentatus and Isodontia harmandi, respectively. Voltage clamp recordings of ASIC currents were performed in whole cell configuration in primary culture of dorsal root ganglion (DRG) neurons from (P7-P10) CII Long-Evans rats. The peptides were applied by preincubation for 25 s (20 s in pH 7.4 solution and 5 s in pH 6.1 solution) or by co-application (5 s in pH 6.1 solution). Sa12b inhibits ASIC current with an IC50 of 81 nM, in a concentration-dependent manner when preincubation application was used. While Sh5b did not show consistent results having both excitatory and inhibitory effects on the maximum ASIC currents, its complex effect suggests that it presents a selective action on some ASIC subunits. Despite the similarity in their sequences, the action of these peptides differs significantly. Sa12b is the first discovered wasp peptide with a significant ASIC inhibitory effect.
Carmen Hernández; Katsuhiro Konno; Emilio Salceda; Rosario Vega; André Junqueira Zaharenko; Enrique Soto; Vega; Soto. Sa12b Peptide from Solitary Wasp Inhibits ASIC Currents in Rat Dorsal Root Ganglion Neurons. Toxins 2019, 11, 585 .
AMA StyleCarmen Hernández, Katsuhiro Konno, Emilio Salceda, Rosario Vega, André Junqueira Zaharenko, Enrique Soto, Vega, Soto. Sa12b Peptide from Solitary Wasp Inhibits ASIC Currents in Rat Dorsal Root Ganglion Neurons. Toxins. 2019; 11 (10):585.
Chicago/Turabian StyleCarmen Hernández; Katsuhiro Konno; Emilio Salceda; Rosario Vega; André Junqueira Zaharenko; Enrique Soto; Vega; Soto. 2019. "Sa12b Peptide from Solitary Wasp Inhibits ASIC Currents in Rat Dorsal Root Ganglion Neurons." Toxins 11, no. 10: 585.
Solitary wasps use their stinging venoms for paralyzing insect or spider prey and feeding them to their larvae. We have surveyed bioactive substances in solitary wasp venoms, and found antimicrobial peptides together with some other bioactive peptides. Eumenine mastoparan-AF (EMP-AF) was the first to be found from the venom of the solitary eumenine wasp Anterhynchium flavomarginatum micado, showing antimicrobial, histamine-releasing, and hemolytic activities, and adopting an α-helical secondary structure under appropriate conditions. Further survey of solitary wasp venom components revealed that eumenine wasp venoms contained such antimicrobial α-helical peptides as the major peptide component. This review summarizes the results obtained from the studies of these peptides in solitary wasp venoms and some analogs from the viewpoint of (1) chemical and biological characterization; (2) physicochemical properties and secondary structure; and (3) channel-like pore-forming properties.
Marcia Perez Dos Santos Cabrera; Marisa Rangel; João Ruggiero Neto; Katsuhiro Konno. Chemical and Biological Characteristics of Antimicrobial α-Helical Peptides Found in Solitary Wasp Venoms and Their Interactions with Model Membranes. Toxins 2019, 11, 559 .
AMA StyleMarcia Perez Dos Santos Cabrera, Marisa Rangel, João Ruggiero Neto, Katsuhiro Konno. Chemical and Biological Characteristics of Antimicrobial α-Helical Peptides Found in Solitary Wasp Venoms and Their Interactions with Model Membranes. Toxins. 2019; 11 (10):559.
Chicago/Turabian StyleMarcia Perez Dos Santos Cabrera; Marisa Rangel; João Ruggiero Neto; Katsuhiro Konno. 2019. "Chemical and Biological Characteristics of Antimicrobial α-Helical Peptides Found in Solitary Wasp Venoms and Their Interactions with Model Membranes." Toxins 11, no. 10: 559.
Comprehensive LC-MS and MS/MS analysis of the crude venom extract from the solitary eumenine wasp Eumenes micado revealed the component profile of this venom mostly consisted of small peptides. The major peptide components, eumenine mastoparan-EM1 (EMP-EM1: LKLMGIVKKVLGAL-NH₂) and eumenine mastoparan-EM2 (EMP-EM2: LKLLGIVKKVLGAI-NH₂), were purified and characterized by the conventional method. The sequences of these new peptides are homologous to mastoparans, the mast cell degranulating peptides from social wasp venoms; they are 14 amino acid residues in length, rich in hydrophobic and basic amino acids, and C-terminal amidated. Accordingly, these new peptides can belong to mastoparan peptides (in other words, linear cationic α-helical peptides). Indeed, the CD spectra of these new peptides showed predominantly α-helix conformation in TFE and SDS. In biological evaluation, both peptides exhibited potent antibacterial activity, moderate degranulation activity from rat peritoneal mast cells, and significant leishmanicidal activity, while they showed virtually no hemolytic activity on human or mouse erythrocytes. These results indicated that EMP-EM peptides rather strongly associated with bacterial cell membranes rather than mammalian cell membranes.
Katsuhiro Konno; Kohei Kazuma; Marisa Rangel; Joacir Stolarz-De-Oliveira; Renato Fontana; Marii Kawano; Hiroyuki Fuchino; Izumi Hide; Tadashi Yasuhara; Yoshihiro Nakata. New Mastoparan Peptides in the Venom of the Solitary Eumenine Wasp Eumenes micado. Toxins 2019, 11, 155 .
AMA StyleKatsuhiro Konno, Kohei Kazuma, Marisa Rangel, Joacir Stolarz-De-Oliveira, Renato Fontana, Marii Kawano, Hiroyuki Fuchino, Izumi Hide, Tadashi Yasuhara, Yoshihiro Nakata. New Mastoparan Peptides in the Venom of the Solitary Eumenine Wasp Eumenes micado. Toxins. 2019; 11 (3):155.
Chicago/Turabian StyleKatsuhiro Konno; Kohei Kazuma; Marisa Rangel; Joacir Stolarz-De-Oliveira; Renato Fontana; Marii Kawano; Hiroyuki Fuchino; Izumi Hide; Tadashi Yasuhara; Yoshihiro Nakata. 2019. "New Mastoparan Peptides in the Venom of the Solitary Eumenine Wasp Eumenes micado." Toxins 11, no. 3: 155.
We previously identified 92 toxin-like peptides and proteins, including pilosulin-like peptides 1–6 from the predatory ant Odontomachus monticola, by transcriptome analysis. Here, to further characterize venom components, we analyzed the venom and venom sac extract by ESI-MS/MS with or without trypsin digestion and reducing agent. As the low-molecular-mass components, we found amino acids (leucine/isoleucine, phenylalanine, and tryptophan) and biogenic amines (histamine and tyramine) in the venom and venom sac extract. As the higher molecular mass components, we found peptides and proteins such as pilosulin-like peptides, phospholipase A2s, hyaluronidase, venom dipeptidyl peptidases, conotoxin-like peptide, and icarapin-like peptide. In addition to pilosulin-like peptides 1–6, we found three novel pilosulin-like peptides that were overlooked by transcriptome analysis. Moreover, pilosulin-like peptides 1–6 were chemically synthesized, and some of them displayed antimicrobial, hemolytic, and histamine-releasing activities.
Naoki Tani; Kohei Kazuma; Yukio Ohtsuka; Yasushi Shigeri; Keiichi Masuko; Katsuhiro Konno; Hidetoshi Inagaki. Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components. Toxins 2019, 11, 50 .
AMA StyleNaoki Tani, Kohei Kazuma, Yukio Ohtsuka, Yasushi Shigeri, Keiichi Masuko, Katsuhiro Konno, Hidetoshi Inagaki. Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components. Toxins. 2019; 11 (1):50.
Chicago/Turabian StyleNaoki Tani; Kohei Kazuma; Yukio Ohtsuka; Yasushi Shigeri; Keiichi Masuko; Katsuhiro Konno; Hidetoshi Inagaki. 2019. "Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components." Toxins 11, no. 1: 50.
Bunodosine 391 (BDS 391), a low molecular weight compound isolated from the sea anemone Bunodosoma cangicum, increases the nociceptive threshold and inhibits inflammatory hyperalgesia. Serotonin receptors are involved in those effects. In this study, we have expanded the characterization of the antinociceptive effect of BDS 391 demonstrating that, in rats: (a) the compound inhibits (1.2–12 ng/paw) overt pain, in the formalin test, and mechanical hyperalgesia (0.6–6.0 ng/paw) detected in a model of neuropathic pain; (b) intraplantar administration of ondansetron, a selective 5-HT3 receptor antagonist, blocks the effect of BDS 391, whereas ketanserin, a 5-HT2 receptor antagonist, partially reversed this effect, indicating the involvement of peripheral 5-HT2 and 5-HT3 receptors in BDS 391 antinociception; and (c) in binding assay studies, BDS 391 was not able to displace the selective 5-HT receptor antagonists, suggesting that this compound does not directly bind to these receptors. The effect of biguanide, a selective 5-HT3 receptor agonist, was also evaluated. The agonist inhibited the formalin’s nociceptive response, supporting an antinociceptive role for 5-HT3 receptors. Our study is the first one to show that a non-peptidic low molecular weight compound obtained from a sea anemone is able to induce antinociception and that activation of peripheral 5-HT3 receptors contributes to this effect.
Wilson Alves Ferreira Junior; Andre Junqueira Zaharenko; Kohei Kazuma; Gisele Picolo; Vanessa Pacciari Gutierrez; Jose Carlos De Freitas; Katsuhiro Konno; Yara Cury. Peripheral 5-HT3 Receptors Are Involved in the Antinociceptive Effect of Bunodosine 391. Toxins 2017, 10, 12 .
AMA StyleWilson Alves Ferreira Junior, Andre Junqueira Zaharenko, Kohei Kazuma, Gisele Picolo, Vanessa Pacciari Gutierrez, Jose Carlos De Freitas, Katsuhiro Konno, Yara Cury. Peripheral 5-HT3 Receptors Are Involved in the Antinociceptive Effect of Bunodosine 391. Toxins. 2017; 10 (1):12.
Chicago/Turabian StyleWilson Alves Ferreira Junior; Andre Junqueira Zaharenko; Kohei Kazuma; Gisele Picolo; Vanessa Pacciari Gutierrez; Jose Carlos De Freitas; Katsuhiro Konno; Yara Cury. 2017. "Peripheral 5-HT3 Receptors Are Involved in the Antinociceptive Effect of Bunodosine 391." Toxins 10, no. 1: 12.
Ants (hymenoptera: Formicidae) have adapted to many different environments and have become some of the most prolific and successful insects. To date, 13,258 ant species have been reported. They have been classified into 333 genera and 17 subfamilies. Except for a few Formicinae, Dolichoderinae, and members of other subfamilies, most ant species have a sting with venom. The venoms are composed of formic acid, alkaloids, hydrocarbons, amines, peptides, and proteins. Unlike the venoms of other animals such as snakes and spiders, ant venoms have seldom been analyzed comprehensively, and their compositions are not yet completely known. In this study, we used both transcriptomic and peptidomic analyses to study the composition of the venom produced by the predatory ant species Odontomachus monticola. The transcriptome analysis yielded 49,639 contigs, of which 92 encoded toxin-like peptides and proteins with 18,106,338 mapped reads. We identified six pilosulin-like peptides by transcriptomic analysis in the venom gland. Further, we found intact pilosulin-like peptide 1 and truncated pilosulin-like peptides 2 and 3 by peptidomic analysis in the venom. Our findings related to ant venom peptides and proteins may lead the way towards development and application of novel pharmaceutical and biopesticidal resources.
Kohei Kazuma; Keiichi Masuko; Katsuhiro Konno; Hidetoshi Inagaki. Combined Venom Gland Transcriptomic and Venom Peptidomic Analysis of the Predatory Ant Odontomachus monticola. Toxins 2017, 9, 323 .
AMA StyleKohei Kazuma, Keiichi Masuko, Katsuhiro Konno, Hidetoshi Inagaki. Combined Venom Gland Transcriptomic and Venom Peptidomic Analysis of the Predatory Ant Odontomachus monticola. Toxins. 2017; 9 (10):323.
Chicago/Turabian StyleKohei Kazuma; Keiichi Masuko; Katsuhiro Konno; Hidetoshi Inagaki. 2017. "Combined Venom Gland Transcriptomic and Venom Peptidomic Analysis of the Predatory Ant Odontomachus monticola." Toxins 9, no. 10: 323.
Among the hymenopteran insect venoms, those from social wasps and bees – such as honeybee, hornets and paper wasps – have been well documented. Their venoms are composed of a number of peptides and proteins and used for defending their nests and themselves from predators. In contrast, the venoms of solitary wasps and bees have not been the object of further research. In case of solitary bees, only major peptide components in a few venoms have been addressed. Therefore, the aim of the present study was to explore the peptide component profile of the venom from the solitary bee Xylocopa appendiculata circumvolans by peptidomic analysis with using LC-MS. A reverse-phase HPLC connected to ESI-OrbiTrap MS was used for LC-MS. On-line mass fingerprinting was made from TIC, and data-dependent tandem mass spectrometry gave MSMS spectra. A major peptide component was isolated by reverse-phase HPLC by conventional way, and its sequence was determined by Edman degradation, which was finally corroborated by solid phase synthesis. Using the synthetic specimen, biological activities (antimicrobial activity, mast cell devaluation, hemolysis, leishmanicidal activity) and pore formation in artificial lipid bilayer were evaluated. On-line mass fingerprinting revealed that the crude venom contained 124 components. MS/MS analysis gave 75 full sequences of the peptide components. Most of these are related to the major and novel peptide, xylopin. Its sequence, GFVALLKKLPLILKHLH-NH2, has characteristic features of linear cationic α-helical peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, it can be predicted to adopt an amphipathic α-helix secondary structure. In biological evaluation, xylopin exhibited broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. Additionally, the peptide was able to incorporate pores in artificial lipid bilayers of azolectin, confirming the mechanism of the cytolytic activity by pore formation in biological membranes. LC-ESI-MS and MS/MS analysis of the crude venom extract from a solitary bee Xylocopa appendiculata circumvolans revealed that the component profile of this venom mostly consisted of small peptides. The major peptide components, xylopin and xylopinin, were purified and characterized in a conventional manner. Their chemical and biological characteristics, belonging to linear cationic α-helical peptides, are similar to the known solitary bee venom peptides, melectin and osmin. Pore formation in artificial lipid bilayers was demonstrated for the first time with a solitary bee peptide.
Kohei Kazuma; Kenji Ando; Ken-Ichi Nihei; Xiaoyu Wang; Marisa Rangel; Marcia Regina Franzolin; Kanami Mori-Yasumoto; Setsuko Sekita; Makoto Kadowaki; Motoyoshi Satake; Katsuhiro Konno. Peptidomic analysis of the venom of the solitary bee Xylocopa appendiculata circumvolans. Journal of Venomous Animals and Toxins including Tropical Diseases 2017, 23, 40 .
AMA StyleKohei Kazuma, Kenji Ando, Ken-Ichi Nihei, Xiaoyu Wang, Marisa Rangel, Marcia Regina Franzolin, Kanami Mori-Yasumoto, Setsuko Sekita, Makoto Kadowaki, Motoyoshi Satake, Katsuhiro Konno. Peptidomic analysis of the venom of the solitary bee Xylocopa appendiculata circumvolans. Journal of Venomous Animals and Toxins including Tropical Diseases. 2017; 23 (1):40.
Chicago/Turabian StyleKohei Kazuma; Kenji Ando; Ken-Ichi Nihei; Xiaoyu Wang; Marisa Rangel; Marcia Regina Franzolin; Kanami Mori-Yasumoto; Setsuko Sekita; Makoto Kadowaki; Motoyoshi Satake; Katsuhiro Konno. 2017. "Peptidomic analysis of the venom of the solitary bee Xylocopa appendiculata circumvolans." Journal of Venomous Animals and Toxins including Tropical Diseases 23, no. 1: 40.
Solitary wasps paralyze insects or spiders with stinging venom and feed the paralyzed preys to their larva. Accordingly, the venoms should contain a variety of constituents acting on nervous systems. However, only a few solitary wasp venoms have been chemically studied despite thousands of species inhabiting the planet. We have surveyed bioactive substances in solitary wasp venoms found in Japan and discovered a variety of novel bioactive peptides. Pompilidotoxins (PMTXs), in the venoms of the pompilid wasps Anoplius samariensis and Batozonellus maculifrons, are small peptides consisting of 13 amino acids without a disulfide bond. PMTXs slowed Na+ channel inactivation, in particular against neuronal type Na+ channels, and were rather selective to the Nav1.6 channel. Mastoparan-like cytolytic and antimicrobial peptides are the major components of eumenine wasp venoms. They are rich in hydrophobic and basic amino acids, adopting a α-helical secondary structure, and showing mast cell degranulating, antimicrobial and hemolytic activities. The venom of the spider wasp Cyphononyx fulvognathus contained four bradykinin-related peptides. They are hyperalgesic and, dependent on the structure, differently associated with B1 or B2 receptors. Further survey led to the isolation of leucomyosuppressin-like FMRFamide peptides from the venoms of the digger wasps Sphex argentatus and Isodontia harmandi. These results of peptide toxins in solitary wasp venoms from our studies are summarized.
Katsuhiro Konno; Kohei Kazuma; Ken-Ichi Nihei. Peptide Toxins in Solitary Wasp Venoms. Toxins 2016, 8, 114 .
AMA StyleKatsuhiro Konno, Kohei Kazuma, Ken-Ichi Nihei. Peptide Toxins in Solitary Wasp Venoms. Toxins. 2016; 8 (4):114.
Chicago/Turabian StyleKatsuhiro Konno; Kohei Kazuma; Ken-Ichi Nihei. 2016. "Peptide Toxins in Solitary Wasp Venoms." Toxins 8, no. 4: 114.
Ken-Ichi Nihei; Kohei Kazuma; Kenji Ando; Katsuhiro Konno. 96. Chemical and Biological Characterization of a Novel Neuropeptide in the Venom of Solitary Digger Wasp. Toxicon 2012, 60, 144 .
AMA StyleKen-Ichi Nihei, Kohei Kazuma, Kenji Ando, Katsuhiro Konno. 96. Chemical and Biological Characterization of a Novel Neuropeptide in the Venom of Solitary Digger Wasp. Toxicon. 2012; 60 (2):144.
Chicago/Turabian StyleKen-Ichi Nihei; Kohei Kazuma; Kenji Ando; Katsuhiro Konno. 2012. "96. Chemical and Biological Characterization of a Novel Neuropeptide in the Venom of Solitary Digger Wasp." Toxicon 60, no. 2: 144.
Four novel peptides were isolated from the venoms of the solitary eumenine wasps Eumenes rubrofemoratus and Eumenes fraterculus. Their sequences were determined by MALDI-TOF/TOF (matrix assisted laser desorption/ionization time-of-flight mass spectrometry) analysis, Edman degradation and solid-phase synthesis. Two of them, eumenitin-R (LNLKGLIKKVASLLN) and eumenitin-F (LNLKGLFKKVASLLT), are highly homologous to eumenitin, an antimicrobial peptide from a solitary eumenine wasp, whereas the other two, EMP-ER (FDIMGLIKKVAGAL-NH2) and EMP-EF (FDVMGIIKKIAGAL-NH2), are similar to eumenine mastoparan-AF (EMP-AF), a mast cell degranulating peptide from a solitary eumenine wasp. These sequences have the characteristic features of linear cationic cytolytic peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, they can be predicted to adopt an amphipathic α-helix secondary structure. In fact, the CD (circular dichroism) spectra of these peptides showed significant α-helical conformation content in the presence of TFE (trifluoroethanol), SDS (sodium dodecylsulfate) and asolectin vesicles. In the biological evaluation, all the peptides exhibited a significant broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity.
Marisa Rangel; Marcia P. Dos Santos Cabrera; Kohei Kazuma; Kenji Ando; Xiaoyu Wang; Manabu Kato; Ken-Ichi Nihei; Izaura Yoshico Hirata; Tyra J. Cross; Angélica Nunes Garcia; Eliana L. Faquim-Mauro; Marcia Franzolin; Hiroyuki Fuchino; Kanami Mori-Yasumoto; Setsuko Sekita; Makoto Kadowaki; Motoyoshi Satake; Katsuhiro Konno. Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps. Toxicon 2011, 57, 1081 -1092.
AMA StyleMarisa Rangel, Marcia P. Dos Santos Cabrera, Kohei Kazuma, Kenji Ando, Xiaoyu Wang, Manabu Kato, Ken-Ichi Nihei, Izaura Yoshico Hirata, Tyra J. Cross, Angélica Nunes Garcia, Eliana L. Faquim-Mauro, Marcia Franzolin, Hiroyuki Fuchino, Kanami Mori-Yasumoto, Setsuko Sekita, Makoto Kadowaki, Motoyoshi Satake, Katsuhiro Konno. Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps. Toxicon. 2011; 57 (7-8):1081-1092.
Chicago/Turabian StyleMarisa Rangel; Marcia P. Dos Santos Cabrera; Kohei Kazuma; Kenji Ando; Xiaoyu Wang; Manabu Kato; Ken-Ichi Nihei; Izaura Yoshico Hirata; Tyra J. Cross; Angélica Nunes Garcia; Eliana L. Faquim-Mauro; Marcia Franzolin; Hiroyuki Fuchino; Kanami Mori-Yasumoto; Setsuko Sekita; Makoto Kadowaki; Motoyoshi Satake; Katsuhiro Konno. 2011. "Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps." Toxicon 57, no. 7-8: 1081-1092.