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At least 19 recordsLinked to original sources
PubMed1975

Accumulation of some secretory enzymes in venom glands of Vipera palaestinae.

Secretion of venom in the venom glands of Vipera palaestinae was studied by measuring the protein content and enzymatic activities of L-amino acid oxidase (LAO), phosphodiesterase (PDE), and benzoylarginine ethyl esterase (BAEE). These were tested in the accumulating venom and gland homogenates at 0, 2, 3, 4,6, and 15 days after an intitial emptying of the venom glands by milking. Changes in the total activities of the enzymes and in the protein concentration were found in the venom samples, but not in the homogenates, at the different intervals after milking. In the venom the total activities of LAO, PDE, and BAEE were higher the longer the time intervals from the initial milking. When the data were fit by a straight line, the fluctuations from the line were of opposite signs for LAO and PDE at the 3- and the 4-day intervals. There were no significant correlations between the specific activities or between the changes in the specific activities of any two of the enzymes at any time interval. It is concluded that each of the enzymes is secreted at a rate independent of the other two; this pattern of secretion can best be described as nonparallel.

Amino Acid Oxidoreductases↗
PubMed1979

Herpesvirus-like infection of the venom gland of Siamese cobras.

The light and electron microscopic appearance of venom glands from two Siamese cobra snakes with a history of production of poor-quality venom was determined. Light microscopy revealed degeneration and necrosis of patches of columnar epithelial cells of glands and infiltration of the subepithelium by inflammatory cells. The lumina contained debris, venom, and necrotic cells. Electron microscopy revealed a deficiency of microvilli on the luminal surfaces of both degenerated and necrotic epithelial cells. The lumina contained fragmented microvilli, coated vesicles containing venom, and degenerated and necrotic cells. Naked and enveloped herpesvirus-like particles were seen in necrotic and ruptured cells. Occasionally, naked herpesvirus-like particles were seen in the nuclei of attached epithelial cells. It was concluded that herpesvirus-like infection of the venom gland was the probable cause of the production of poor-quality venom.

Animals↗
PubMed2026

Multifunctional lysozymes from the assassin bug Sycanus bifidus: Insecticidal proteins with anticoagulant and melanization inhibition properties.

BACKGROUND: Predatory hemipterans deploy complex venom cocktails to immobilize preys, yet the specific roles of many individual venom components remain poorly understood. RESULTS: Four lysozyme genes were identified from the genome of the predatory assassin bug Sycanus bifidus (Hemiptera: Reduviidae), comprising one i-type (SbLyzi) and three c-type lysozyme genes (SbLyzc1-3). Transcriptomic and quantitative (q)PCR analyses revealed that these lysozymes were expressed at different levels in various venom glands. Of them, SbLyzc1-3 with signal peptides displayed significant transcriptions in the venom glands, implicating these lysozymes as venom constituents. Functional assays found that SbLyzc1 and SbLyzc2 showed antibacterial activity against Pseudomonas aeruginosa and Enterococcus faecalis. Three lysozymes (SbLyzi, SbLyzc1 and SbLyzc3) suppressed thrombin-induced fibrin clot formation, indicating anticoagulant activity, with SbLyzc1 exhibiting the greatest potency [half-maximal inhibitory concentration (IC50) = 0.036 ± 0.003 μg μL-1]. SbLyzi and SbLyzc1 inhibited phenoloxidase activity in the hemolymph of the yellow mealworm Tenebrio molitor pupae, thereby suppressing its hemolymph melanization, with maximal inhibition rates of 78.4% and 74.3%, respectively. All four lysozymes exhibited insecticidal effects, causing >80% mortality in yellow mealworm pupae following injection of 6 μg per individual, with SbLyzc1 showing the highest insecticidal potency [half-maximal lethal dose (LD50) = 4.25 ± 0.51 μg g-1]. CONCLUSION: These findings demonstrate that lysozymes from S. bifidus possess multifunctional biological activities and SbLyzc1-3 act as significant venom components involved in capturing prey, providing new insights into the functional diversity of lysozymes in predatory bugs and their potential application in biological control strategies. © 2026 Society of Chemical Industry.

Animals↗
PubMed1977

Translation of melittin messenger RNA in vitro yields a product terminating with glutaminylglycine rather than with glutaminamide.

Melittin messenger RNA from queen bee venom glands has been translated in a cell-free system from wheat germ. A product larger than promelittin is formed which has the carboxy-terminal sequence-Gln-Gln-GlyCOOH. Melittin and promelittin from venom glands terminate in -Gln-GlnCONH2. The possible role of the extra glycine residue in the formation of a COOH-terminal amide via a transamidase-like reaction is discussed.

Amino Acid Sequence↗
PubMed2026

The genomic alchemist's arsenal: A comprehensive review of gene recruitment, regulatory rewiring, and the evolutionary arms race in snake envenomation.

Snake venom represents a striking example of evolutionary innovation, in which ancestral physiological gene networks have been co-opted into potent biochemical weapons. Advances in multi-omics, single-cell genomics, and structural bioinformatics have catalyzed a conceptual shift from descriptive toxin cataloging to a systems-level understanding of venom evolution, regulation, and function. This Review integrates genomic, cellular, and structural perspectives to delineate the molecular architecture underpinning venom diversification and target-site co-evolution. Emphasis is placed on regulatory mechanisms driving rapid expression plasticity, including super-enhancer activity, transposable element insertion, spatial heterogeneity within the venom gland, and non-coding RNA-mediated modulation. At the protein level, the review examines how hypervariable toxins engage in structural arms races with prey targets, and how multi-toxin complex formation, functional synergy, and molecular dynamics simulations inform models of lethality and resistance. A comparative framework is provided by contrasting high-potency predatory snake venoms with low-potency defensive venoms of hymenopterans such as bees and wasps, revealing how ecological selective pressures shape toxin potency, composition, and target specificity across taxa. Finally, current translational strategies are evaluated, with a focus on the relative merits of recombinant human monoclonal antibodies versus catalytic-site small-molecule inhibitors as deployable interventions for snakebite. By synthesizing evolutionary genomics, structural biology, comparative toxinology, and synthetic antivenomics, this Review outlines a predictive framework for anticipating venom evolutionary trajectories and for designing broad-spectrum, next-generation therapeutics.

Animals↗
PubMed2026

Divergent evolutionary strategies in spider venoms: A comparative proteomic profiling of four sympatric species from Yunnan.

Spider venoms comprise complex cocktails of bioactive molecules evolved for predation and defense, representing a valuable resource for biological research and pharmaceutical discovery. In this study, we performed a systematic analysis of venom gland extracts from four common spider species indigenous to Yunnan, China: Agelena limbata, Hippasa lycosina, Lycosa grahami, and Sinopoda pengi. Using an integrated transcriptomic and proteomic targeted profiling approach, we successfully annotated 141 distinct toxins. Comparative analysis revealed significant interspecific heterogeneity, suggesting distinct evolutionary trajectories and "weapon system economics." Both A. limbata and L. grahami exhibited a "peptide-dominant" profile anchored by neurotoxic peptides and isomerases, optimized for rapid chemical paralysis. In contrast, S. pengi displayed a distinct "protein-dominant" signature enriched with high-molecular-weight enzymes and CAP superfamily proteins, likely functioning to facilitate tissue degradation and toxin diffusion. Occupying an intermediate position, H. lycosina demonstrated a hybrid composition. These findings suggest that although these species share the same geographical range, their venom systems have undergone divergent evolutionary adaptations driven by specific ecological niches and hunting strategies. This study represents the first systematic proteomic characterization of these venom components, providing a valuable reservoir of molecular candidates while highlighting the bioinformatic nuances of analyzing whole-gland homogenates.

Animals↗
PubMed2026

The genomic origins and evolutionary path to a key innovation in the world's most venomous snakes.

Evolutionary innovation is a catalyst for the colonization of new environments and the adaptive radiations of major groups. Novel traits typically evolve through the modification of preexisting characters, but the genetic paths underlying their origin have been challenging to trace, and the general requirements for and relative order of different kinds of gene mutations have been difficult to assess. Here, we trace the genomic origins of four procoagulant venom toxins (factor X, factor V, group I phospholipase A2, and Kunitz-type toxins) that collectively underlie a novel, especially potent blood-clotting venom type in the recently evolved Australian brown snake and taipan clade. We find evidence for a previously unknown fifth toxin, coagulation factor VII, and show that the toxins evolved through two distinct genetic paths. The factor X and factor V toxins evolved through the sequential de novo co-option of ancestral clotting factor proteins that entailed their heterotopic expression in the venom gland, the fixation of segmental duplications containing each locus, and subsequent gain-of-function mutations that rendered factor X and factor V constitutively active. In contrast, the phospholipase A2 and Kunitz-type toxins evolved by modifying the functions of neurotoxins that were part of the venom arsenal. Our findings support models in which innovative mutations in single-copy genes precede gene duplication in the evolution of novel proteins and offer a rare view into the genesis of a complex trait that has played a central role in a major adaptive radiation.

Animals↗
PubMed2026

The genomic origins and evolutionary path to a key innovation in the world's most venomous snakes.

Evolutionary innovation is a key driver of the colonization of new environments and the adaptive radiations of major groups. Novel traits typically evolve through the modification of pre-existing characters but the genetic paths underlying their origin have been challenging to trace, and the general requirements for and relative order of different kinds of gene mutations have been difficult to assess. Here, we trace the genomic origins of four procoagulant venom toxins (factor X, factor V, group I phospholipase A2, and Kunitz-type toxins) that collectively underlie a novel, especially potent blood-clotting venom type in the recently evolved Australian brown snake and taipan clade. We discover evidence for a previously unknown fifth toxin, coagulation factor VII, and show that the toxins evolved through two distinct genetic paths. The factor X and factor V toxins evolved through the sequential de novo co-option of ancestral clotting factor proteins that entailed their heterotopic expression in the venom gland, the fixation of segmental duplications containing each locus, and subsequent gain-of-function mutations that rendered factor X and factor V constitutively active. In contrast, the phospholipase A2 and Kunitz-type toxins evolved by modifying the functions of neurotoxins that were part of the venom arsenal. Our findings support models in which innovative mutations in single-copy genes precede gene duplication in the evolution of novel proteins and offer a rare view into the genesis of a complex trait that has played a central role in a major adaptive radiation.

Biological Sciences: Evolution↗
PubMed1978

Amino acid sequence of honeybee prepromelittin synthesized in vitro.

Translation of melittin messenger RNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44--69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine, proline, and acidic residues. At least three post-translational reactions are required to convert prepromelittin to mellitin.

Amino Acid Sequence↗
PubMed1979

Phospholipase A of sea snake Laticauda semifasciata venom. Isolation and properties of novel forms lacking tryptophan.

The venom gland extracts of the sea snake Laticauda semifasciata contained at least four forms of phospholipase A separable on a CM-cellulose column. They were designated as phospholipases A I-IV in the order of elution from the column. Phospholipases A I, III, and IV were isolated in a homogeneous state. They were similar to one another in amino acid composition and molecular weight (14,000) as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Phospholipase A I contained one tryptophan residue. whereas III and IV did not. Although all these forms had the same A2-type positional specificity, they were classified into two groups (I, and III and IV) on the basis of enzymic properties. Phospholipase A I had a higher specific activity and showed normal kinetics, whereas III and IV had approximately one-tenth of the specific activity of I and showed biphasic kinetics due to their activation by the reaction products. Phospholipase A I, the major form, seems to be identical with phospholipase A reported previously (Tu, A.T., Passey, R.B., & Toom, P.M. (1970) Arch. Biochem. Biophys. 140, 96-106), whereas the other two, III and IV, are new. Phospholipase A I became more like III and IV in enzymic properties on modification with N-bromosuccinimide.

Amino Acids↗
PubMed1975

Prolonged C3 depletion by cobra venom factor in thymus-deprived mice and its implication for the role of C3 as an essential second signal for B-cell triggering.

Cobra venom factor (CoF) is a potent immunogen in intact mice, and its capacity to deplete C3 is neutralized by antibody. In thymus-deprived (T times B) mice antibody was not elicited; C3 depletion by CoF was prolonged, and subsequent injections were also effective. The effect of prolonged C3 depletion was examined on the antibody response to two T cell-independent immunogens, levan and SIII. The spleen PFC responses to levan were unaffected by C3 depletion or thymus deprivation; those to SIII were unaffected by thymus deprivation but were diminished (not abolished) by C3 depletion. It is argued that the capacity to activate C3 is neither sufficient nor necessary to cause an immunogen to be T cell-independent.

Animals↗
PubMed1979

[Overview of the epidemiology of stonefish poisonings, their treatment and preventive measures].

A review is presented of work on envenomation by stonefish (Synanceja spp.), which represent not only a danger for the inhabitants of tropical coasts but also for tourists. Stonefish are common in shallow water of reef areas by the shores of the Indian and Indopacific Ocean. The bizarrely shaped fish is often taken for a weed-covered stone and accidents occur when swimmers, divers or fishermen step on the stings of the dorsal fin. These stings are provided with poison glands. The venom has neurotoxic, myotoxic and hemorrhagic effects. The case of a 39-year-old diver is cited who suffered a stonefish stab which lasted for several weeks. Generally envenomations by Synanceja cause severe local pain and enormous swelling of the limb; systemic symptoms as usually found with neurotoxins are common; death may occur by shock, by paralysis of the diaphragm or cardiac arrest. For first aid bathing of the limb in hot water is recommended. Clinical measures are local analgesia, local neutralization of the venom, if possible antiserum therapy and intensive care with symptomatic treatment of systemic complications. The most effective prevention is adequate foot protection when wading in the sea.

Adult↗