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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↗
PubMed1978

Intracellular transport of proteins in active and resting secretory cells of the venom gland of Vipera palaestinae.

The intracellular transport of venom proteins has been studied in active and resting venom glands of the snake Vipera palaestinae by electron microscope radioautography after an intra-arterial injection of [3H]leucine. In the active gland, most of the label is initially (10 min) found over the RER. By 30 min, the relative grain density of the Golgi complex reaches its maximum, with concomitant increase in the labeling of the condensing vacuoles. Later on, a steep increase in radioactivity of the secretory granules is observed. At 3 h, these granules, which comprise about 2% of the cell volume, contain 22% of the total grains. At the following hour, their labeling declines and at the same time the radioactivity of the secreted venom is increased. It is concluded that, in the active cell, venom proteins are transported via the Golgi apparatus into membrane-bounded granules which are the immediate source of the secreted venom. An alternative pathway, which involves the RER cisternae as a storage compartment, seems unlikely, since incorporated label does not accumulate in this compartment after prolonged postpulse intervals. The route of intracellular transport of proteins in the resting glands is similar to that of the active ones, but the rate of synthesis and transport is much slower. The present results and earlier data, thus, show that the increase in the rate of secretion after initiation of a new venom regeneration cycle is the result of accelerated rates of both synthesis and transport.

Animals↗
PubMed1978

Asynchrony in the synthesis of secretory proteins in the venom gland of the snake Vipera palaestinae.

1. Venom of Vipera palastinae was subjected to isoelectrofocusing on polyacrylamide gel. The protein separation profiles were similar for different venom samples; more than 25 protein bands with a wide range of pI values could be demonstrated by this technique. 2. Labelled venom was obtained 8h after an intracardial injection of [3H]leucine. The relative radioactivities of four out of 12 main protein bands were significantly different in the venom synthesized during the 2nd day of the venom regeneration cycle as compared with the venom of the 4th day. The comparison was made in venom samples obtained from the two glands of the same snake at two different secretory stages. 3. It is concluded that the asynchronous synthesis of exportable proteins after the initiation of a new venom regeneration cycle is responsible for the non-parallel secretion of some venom proteins by the venom gland of Vipera palaestinae during the first few days after milking.

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↗