Ground squirrels use an infrared signal to deter rattlesnake predation.
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The evolution of communicative signals involves a major hurdle; signals need to effectively stimulate the sensory systems of their targets. Therefore, sensory specializations of target animals are important sources of selection on signal structure. Here we report the discovery of an animal signal that uses a previously unknown communicative modality, infrared radiation or "radiant heat," which capitalizes on the infrared sensory capabilities of the signal's target. California ground squirrels (Spermophilus beecheyi) add an infrared component to their snake-directed tail-flagging signals when confronting infrared-sensitive rattlesnakes (Crotalus oreganus), but tail flag without augmenting infrared emission when confronting infrared-insensitive gopher snakes (Pituophis melanoleucus). Experimental playbacks with a biorobotic squirrel model reveal this signal's communicative function. When the infrared component was added to the tail flagging display of the robotic models, rattlesnakes exhibited a greater shift from predatory to defensive behavior than during control trials in which tail flagging included no infrared component. These findings provide exceptionally strong support for the hypothesis that the sensory systems of signal targets should, in general, channel the evolution of signal structure. Furthermore, the discovery of previously undescribed signaling modalities such as infrared radiation should encourage us to overcome our own human-centered sensory biases and more fully examine the form and diversity of signals in the repertoires of many animal species. (+info)
Prey-predator communication: for your sensors only.
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Prey have evolved myriad strategies to escape predation. Ground squirrels tailor their defensive signals to the predator at hand and use infrared warning signals in response to heat-sensitive rattlesnakes. (+info)
Preliminary X-ray crystallographic studies of a tetrameric phospholipase A2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom.
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Crotoxin B is a basic phospholipase A2 found in the venom of Crotalus durissus terrificus and is one of the subunits that constitute crotoxin. This heterodimeric toxin, which is the main component of C. d. terrificus venom, is completed by an acidic, nontoxic and non-enzymatic component (crotoxin A) and is involved in important envenomation effects, such as neurological disorders, myotoxicity and renal failure. Although crotoxin was first crystallized in 1938, no crystal structure is currently available for crotoxin, crotoxin A or crotoxin B. In this work, the crystallization, X-ray diffraction data collection to 2.28 A resolution and molecular-replacement solution of a novel tetrameric complex formed by two dimers of crotoxin B isoforms (CB1 and CB2) is presented. (+info)
Quantitative analysis of snake venoms using soluble polymer-based isotope labeling.
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We present the design and synthesis of a new quantitative strategy termed soluble polymer-based isotope labeling (SoPIL) and its application as a novel and inclusive method for the identification and relative quantification of individual proteins in complex snake venoms. The SoPIL reagent selectively captures and isolates cysteine-containing peptides, and the subsequent tagged peptides are released and analyzed using nanoflow liquid chromatography-tandem mass spectrometry. The SoPIL strategy was used to quantify venom proteins from two pairs of venomous snakes: Crotalus scutulatus scutulatus type A, C. scutulatus scutulatus type B, Crotalus oreganus helleri, and Bothrops colombiensis. The hemorrhagic, hemolytic, clotting ability, and fibrinogenolytic activities of crude venoms were measured and correlated with difference in protein abundance determined by the SoPIL analysis. The SoPIL approach could provide an efficient and widely applicable tool for quantitative proteomics. (+info)
The venom gland transcriptome of the Desert Massasauga rattlesnake (Sistrurus catenatus edwardsii): towards an understanding of venom composition among advanced snakes (Superfamily Colubroidea).
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BACKGROUND: Snake venoms are complex mixtures of pharmacologically active proteins and peptides which belong to a small number of superfamilies. Global cataloguing of the venom transcriptome facilitates the identification of new families of toxins as well as helps in understanding the evolution of venom proteomes. RESULTS: We have constructed a cDNA library of the venom gland of a threatened rattlesnake (a pitviper), Sistrurus catenatus edwardsii (Desert Massasauga), and sequenced 576 ESTs. Our results demonstrate a high abundance of serine proteinase and metalloproteinase transcripts, indicating that the disruption of hemostasis is a principle mechanism of action of the venom. In addition to the transcripts encoding common venom proteins, we detected two varieties of low abundance unique transcripts in the library; these encode for three-finger toxins and a novel toxin possibly generated from the fusion of two genes. We also observed polyadenylated ribosomal RNAs in the venom gland library, an interesting preliminary obsevation of this unusual phenomenon in a reptilian system. CONCLUSION: The three-finger toxins are characteristic of most elapid venoms but are rare in viperid venoms. We detected several ESTs encoding this group of toxins in this study. We also observed the presence of a transcript encoding a fused protein of two well-characterized toxins (Kunitz/BPTI and Waprins), and this is the first report of this kind of fusion in a snake toxin transcriptome. We propose that these new venom proteins may have ancillary functions for envenomation. The presence of a fused toxin indicates that in addition to gene duplication and accelerated evolution, exon shuffling or transcriptional splicing may also contribute to generating the diversity of toxins and toxin isoforms observed among snake venoms. The detection of low abundance toxins, as observed in this and other studies, indicates a greater compositional similarity of venoms (though potency will differ) among advanced snakes than has been previously recognized. (+info)
Donning your enemy's cloak: ground squirrels exploit rattlesnake scent to reduce predation risk.
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