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Journal articles on the topic 'Pseudonoja textilis'

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Published: 18 May 2024

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1

Tibballs, J., and S. Sutherland. "The Efficacy of Antivenom in Prevention of Cardiovascular Depression and Coagulopathy Induced by Brown Snake (Pseudonaja) Species Venom." Anaesthesia and Intensive Care 19, no. 4 (November 1991): 530–34. http://dx.doi.org/10.1177/0310057x9101900407.

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The efficacy of antivenom in prevention of cardiovascular depression and coagulopathy induced by Brown Snake species (Pseudonaja textilis, Pseudonaja affinis) was investigated in anaesthetised mechanically ventilated dogs. Venom and antivenom in variable amounts were incubated together at 37°C for 30 minutes prior to intravenous injection. The dose of antivenom required to prevent severe cardiovascular depression and coagulopathy induced by Pseudonaja textilis venom was 25 times the current recommended dose for clinical use. A tenfold dose of antivenom was required to neutralise similar effects induced by Pseudonaja affinis venom. Large amounts of antivenom may be required in clinical use if coagulopathy or cardiovascular depression are present after envenomation by species of the Brown Snake genus.

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2

Tibballs, J., S. K. Sutherland, R. A. Rivera, and P. P. Masci. "The Cardiovascular and Haematological Effects of Purified Prothrombin Activator from the Common Brown Snake (Pseudonaja textilis) and their Antagonism with Heparin." Anaesthesia and Intensive Care 20, no. 1 (February 1992): 28–32. http://dx.doi.org/10.1177/0310057x9202000105.

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The cardiovascular and haematological effects of purified prothrombin activator derived from the venom of the Australian Common Brown Snake (Pseudonaja textilis) were studied in anaesthetised, mechanically ventilated dogs. Severe depression of systemic blood pressure and cardiac output and a rise in central venous pressure were observed. Thrombocytopenia, prolongation of both prothrombin time and activated partial thromboplastin time and a reduction in serum fibrinogen were also observed. All of these observed effects were prevented by the prior administration of heparin — a naturally occurring anticoagulant. We conclude that the prothrombin activator in Pseudonaja textilis venom may cause cardiovascular depression due to myocardial dysfunction secondary to disseminated intravascular coagulation.

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3

Armugam, Arunmozhiarasi, NanLing Gong, XiaoJie Li, Phui Yee Siew, Siaw Ching Chai, Ramkishen Nair, and Kandiah Jeyaseelan. "Group IB phospholipase A2 from Pseudonaja textilis." Archives of Biochemistry and Biophysics 421, no. 1 (January 2004): 10–20. http://dx.doi.org/10.1016/j.abb.2003.09.045.

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4

Gong, Nanling, Arunmozhiarasi Armugam, and Kandiah Jeyaseelan. "Postsynaptic short-chain neurotoxins from Pseudonaja textilis." European Journal of Biochemistry 265, no. 3 (December 25, 2001): 982–89. http://dx.doi.org/10.1046/j.1432-1327.1999.00800.x.

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5

Tibballs, J., and S. K. Sutherland. "The Efficacy of Heparin in the Treatment of Common Brown Snake (Pseudonaja textilis) Envenomation." Anaesthesia and Intensive Care 20, no. 1 (February 1992): 33–37. http://dx.doi.org/10.1177/0310057x9202000106.

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The efficacy of heparin therapy after subcutaneous injection of Common Brown Snake (Pseudonaja textilis) venom was studied in anaesthetised, mechanically ventilated dogs. Intravenous heparin (100 U/kg), administered fifteen minutes after envenomation, neither prevented nor hastened the recovery from cardiovascular depression and coagulopathy observed after venom administration. Heparin therapy is not recommended for the treatment of established human envenomation.

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6

Watson, Gregory S., David W. Green, and Jolanta A. Watson. "Observations supporting parental care by a viviparous reptile: aggressive behaviour against predators demonstrated by Cunningham’s skinks." Australian Journal of Zoology 67, no. 3 (2019): 180. http://dx.doi.org/10.1071/zo20024.

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Most reptiles exhibit no parental care and aggressive behaviour towards heterospecific predators has rarely been recorded in the natural environment. Several species of the subfamily Egerniinae are amongst the most highly social of all squamate reptiles, exhibiting stable social aggregations and high levels of long-term social and genetic monogamy. We have examined Cunningham’s skinks, Egernia cunninghami, over a three-year period during late January and early February (total 32 days) in the alpine region of New South Wales using video and thermal imaging. Four birthing sessions were witnessed during our field studies of social aggregations of skinks. Our observations monitored skink encounters, in the presence of offspring, with an eastern brown snake, Pseudonaja textilis (two separate encounters, one recorded by video/imaging) and 12 encounters with the Australian magpie, Gymnorhina tibicen. All events were associated with aggressive chasing and/or attack by adult skinks. The first snake encounter involved the active targeting of a recently born juvenile with the mother of the juvenile attacking the snake (running towards the snake, biting and remaining attached for several seconds). The second encounter (the following year) comprised two adult skinks attacking and biting a snake, Pseudonaja textilis. All magpie encounters resulted in chases by adult skinks.

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7

Whitaker, P. B., K. Ellis, and R. Shine. "The defensive strike of the Eastern Brownsnake, Pseudonaja textilis (Elapidae)." Functional Ecology 14, no. 1 (February 2000): 25–31. http://dx.doi.org/10.1046/j.1365-2435.2000.00385.x.

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8

Willmott, N., P. Gaffney, P. Masci, and A. Whitaker. "A novel serine protease inhibitor from the Australian brown snake, Pseudonaja textilis textilis: Inhibition kinetics." Fibrinolysis 9, no. 1 (January 1995): 1–8. http://dx.doi.org/10.1016/s0268-9499(08)80040-9.

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9

GONG, NanLing, Arunmozhiarasi ARMUGAM, Peter MIRTSCHIN, and Kandiah JEYASEELAN. "Cloning and characterization of the pseudonajatoxin b precursor." Biochemical Journal 358, no. 3 (September 10, 2001): 647–56. http://dx.doi.org/10.1042/bj3580647.

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An Australian common brown snake, Pseudonaja textilis, is known to contain highly lethal neurotoxins. Among them, a long-chain α-neurotoxin, pseudonajatoxin b, has been identified. In this report, while presenting evidence for the presence of at least four such long-chain α-neurotoxins in the venom of P. textilis, we describe the characteristics of both the mRNA and the gene responsible for the synthesis of these neurotoxins. A precursor toxin synthesized from the gene has been identified as being capable of producing the isoforms possibly by post-translational modifications at its C-terminal end. Recombinant toxins corresponding to the precursor and its product have been found to possess similar binding affinities for muscular acetylcholine receptors (IC50 = 3×10−8 M) and a lethality, LD50, of 0.15μg/g in mice.

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10

Tibballs, J., S. Sutherland, and S. Kerr. "Studies on Australian Snake Venoms. Part 1: The Haemodynamic Effects of Brown Snake (Pseudonaja) Species in the Dog." Anaesthesia and Intensive Care 17, no. 4 (November 1989): 466–69. http://dx.doi.org/10.1177/0310057x8901700412.

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The haemodynanic effects of Brown Snake (Pseudonaja) species (textilis, nuchalis, affinis) were investigated in anaesthetised, mechanically ventilated dogs. Blood pressure decreased to minimal levels five minutes after intravenous envenomation. Hypotension was accompanied by significant decrements in cardiac output and stroke volume and a rise in peripheral vascular resistance. Heart rate increased transiently during 0.5-2.0 minutes after envenomation but had declined below resting levels five minutes after envenomation. No statistically significant change was recorded in central venous pressure. Depression of myocardial contractility is postulated as the mechanism of venom induced hypotension.

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11

Birrell, Geoff W., Stephen Earl, Paul P. Masci, John de Jersey, Tristan P. Wallis, Jeffrey J. Gorman, and Martin F. Lavin. "Molecular Diversity in Venom from the Australian Brown Snake,Pseudonaja textilis." Molecular & Cellular Proteomics 5, no. 2 (November 10, 2005): 379–89. http://dx.doi.org/10.1074/mcp.m500270-mcp200.

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12

Henderson, Alan, Lee N. Baldwin, and Christopher May. "Fatal Brown Snake (Pseudonaja textilis) Envenomation Despite the use of Antivenom." Medical Journal of Australia 158, no. 10 (May 1993): 709–10. http://dx.doi.org/10.5694/j.1326-5377.1993.tb121923.x.

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13

Masci, P. P., A. N. Whitaker, L. G. Sparrow, J. de Jersey, D. J. Winzor, D. J. Watters, M. F. Lavin, and P. J. Gaffney. "Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model." Blood Coagulation and Fibrinolysis 11, no. 4 (June 2000): 385–93. http://dx.doi.org/10.1097/00001721-200006000-00011.

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14

WILLIAMS, DAVID J., MARK O'SHEA, ROLAND L. DAGUERRE, CATHARINE E. POOK, WOLFGANG WÜSTER, CHRISTOPHER J. HAYDEN, JOHN D. MCVAY, et al. "Origin of the eastern brownsnake, Pseudonaja textilis (Dumeril, Bibron and Dumeril) (Serpentes: Elapidae: Hydrophiinae) in New Guinea: evidence of multiple dispersals from Australia, and comments on the status of Pseudonaja textilis pughi Hoser 2003." Zootaxa 1703, no. 1 (February 13, 2008): 47. http://dx.doi.org/10.11646/zootaxa.1703.1.3.

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Pseudonaja textilis is a widespread and common snake in eastern parts of Australia, but its distribution in New Guinea is poorly understood, and the origin of the New Guinea populations and its timing have been the subject of much speculation. Phylogenetic analysis of mitochondrial DNA sequences from three New Guinea populations of P. textilis indicates that New Guinea was colonised from two independent eastern and western migration routes most likely in the Pleistocene. One dispersal event from northern Queensland led to the populations in eastern New Guinea (Milne Bay, Oro and Central Provinces, Papua New Guinea), whereas another, from Arnhem Land to central southern New Guinea, led to the populations from the Merauke area, Indonesian Papua. The results are consistent with the effects of Pleistocene sea level changes on the physical geography of Australasia, and are thus suggestive of a natural rather than anthropogenic origin of the New Guinea populations. The taxonomic status of the New Guinean populations is discussed.

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15

Whitaker, P. B., and R. Shine. "Responses of free-ranging brownsnakes (Pseudonaja textilis : Elapidae) to encounters with humans." Wildlife Research 26, no. 5 (1999): 689. http://dx.doi.org/10.1071/wr98042.

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Eastern brownsnakes (Pseudonaja textilis) are large (to 2 m), slender, dangerously venomous elapid snakes that cause significant human mortality. We recorded the responses of free-ranging brownsnakes to 455 close encounters with a human observer, using 40 snakes implanted with miniature radio-transmitters, plus encounters with non-telemetered animals. Our study area (near Leeton in south-eastern Australia) is typical of many of the agricultural landscapes occupied by P. textilis. Contrary to public opinion, the snakes were rarely aggressive. About half of the encounters resulted in the snake retreating, and on most other occasions they relied on crypsis. Snakes advanced towards the observer on only 12 occasions (<3% of encounters) during initial approach, and only three of these advances were offensive. The snakes’ responses to an approach depended on the observer’s appearance (e.g. snakes were more likely to ignore an observer wearing light rather than dark shades of clothing) and behaviour (e.g. snakes were more likely to advance if approached rapidly, and touched immediately). Snakes were more likely to retreat if they were sub-adult rather than adult, if they were warm, or if they had been moving prior to an encounter. Weather conditions (air temperature, wind velocity and cloud cover) also influenced the snakes’ responses, as did season and time of day. The snakes’ response was relatively predictable from information on these factors, enabling us to suggest ways in which people can reduce the incidence of potentially fatal encounters with brownsnakes. ‘Snakes are first cowards, next bluffers, and last of all warriors’ (Pope 1958)

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16

Whitaker, P. B., and R. Shine. "When, where and why do people encounter Australian brownsnakes (Pseudonaja textilis : Elapidae)?" Wildlife Research 26, no. 5 (1999): 675. http://dx.doi.org/10.1071/wr98043.

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Encounters between humans and dangerously venomous snakes put both participants at serious risk, so the determinants of such encounters warrant attention. Pseudonaja textilis is a large fast-moving elapid snake responsible for most snakebite fatalities in Australia. As part of a broad ecological study of this species in agricultural land near Leeton, New South Wales, we set out to identify factors influencing the probability that a human walking in farmland would come into close proximity to a brownsnake. Over a three-year period, we walked regular transects to quantify the number and rate of snake encounters, and the proportion of snakes above ground that could be seen. The rate of encounters depended upon a series of factors, including season, time of day, habitat type, weather conditions (wind and air temperature) and shade (light v. dark) of the observers’ clothing. Interactions between factors were also important: for example, the effect of air temperature on encounter probability differed with season and snake gender, and the effect of the observers’ shade of clothing differed with cloud cover. Remarkably, even a highly-experienced observer actually saw <25% of the telemetrically monitored snakes that were known to be active (i.e. above ground) nearby. This result reflects the snakes’ ability to evade people and to escape detection, even in the flat and sparsely vegetated study area. The proportion of snakes that were visible was influenced by the same kinds of factors as described above. Most of the factors biasing encounter rates are readily interpretable from information on other facets of the species’ ecology, and knowledge of these factors may facilitate safer coexistence between snakes and people.

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17

Lechtenberg, Bernhard C., Thomas A. Murray-Rust, Daniel J. D. Johnson, Ty E. Adams, Sriram Krishnaswamy, Rodney M. Camire, and James A. Huntington. "Crystal structure of the prothrombinase complex from the venom of Pseudonaja textilis." Blood 122, no. 16 (October 17, 2013): 2777–83. http://dx.doi.org/10.1182/blood-2013-06-511733.

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18

Masci, P. P., P. J. Mirtschin, T. N. Nias, R. K. Turnbull, T. R. Kuchel, and A. N. Whitaker. "Brown Snakes (Pseudonaja Genus): Venom Yields, Prothrombin Activator Neutralization and Implications Affecting Antivenom Usage." Anaesthesia and Intensive Care 26, no. 3 (June 1998): 276–81. http://dx.doi.org/10.1177/0310057x9802600308.

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The recent high prevalence of fatal bites by Brown snakes (Pseudonaja genus) has led to this study of venom yields from 66 brown snake milkings over 15 months. The amount of venom obtained from all species was higher than reported previously. Electrophoretic and Western blotting analyses of their venoms showed significantly lower avidity of Brown snake antivenom (BS-AV) for the prothrombin activator (PA) component (190 kD) than for other venom components, including the neurotoxins. The LD50 of P. inframacula has been determined for the first time. SDS-PAGE (sodium dodecyl sulphate-polyacrylamide gel electrophoresis) and Western blotting studies have shown that the Pseudonaja venoms contained proportionately more PA component than venoms of the Taipan (Oxyuranus scutellatus) or the Fierce snake (O. microlepidotus). Neutralization of the prothrombin activator of the Common Brown snake (P. textilis) (Pt-PA) by BS-AV was found to be time dependent and 40% remained unneutralized after 30 minutes incubation. Adult rats administered quantities of Pt-PA (IV) died with acute disseminated intravascular coagulation. Rats were made resistant to Pt-PA by preheparinization or by induction of tolerance to increasing quantities of Pt-PA. There is no evidence that Pt-PA has intrinsic toxicity apart from being a procoagulant. The improvement of BS-AV by addressing its deficiencies should be canvassed.

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19

Chaisakul, Janeyuth, Geoffrey K. Isbister, Sanjaya Kuruppu, Nicki Konstantakopoulos, and Wayne C. Hodgson. "An examination of cardiovascular collapse induced by eastern brown snake (Pseudonaja textilis) venom." Toxicology Letters 221, no. 3 (August 2013): 205–11. http://dx.doi.org/10.1016/j.toxlet.2013.06.235.

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20

Whitaker, P. B., and R. Shine. "THERMAL BIOLOGY AND ACTIVITY PATTERNS OF THE EASTERN BROWNSNAKE (PSEUDONAJA TEXTILIS): A RADIOTELEMETRIC STUDY." Herpetologica 58, no. 4 (December 2002): 436–52. http://dx.doi.org/10.1655/0018-0831(2002)058[0436:tbaapo]2.0.co;2.

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21

WHITE, J., and V. WILLIAMS. "Severe envenomation with convulsion following multiple bites by a common brown snake, Pseudonaja textilis." Journal of Paediatrics and Child Health 25, no. 2 (April 1989): 109–11. http://dx.doi.org/10.1111/j.1440-1754.1989.tb01430.x.

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22

Chaisakul, Janeyuth, Geoffrey K. Isbister, Margaret A. O'Leary, Helena C. Parkington, A. Ian Smith, Wayne C. Hodgson, and Sanjaya Kuruppu. "Prothrombin activator-like toxin appears to mediate cardiovascular collapse following envenoming by Pseudonaja textilis." Toxicon 102 (August 2015): 48–54. http://dx.doi.org/10.1016/j.toxicon.2015.05.001.

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23

Rehorek, Susan J., Mimi Halpern, Bruce T. Firth, and Mark N. Hutchinson. "The Harderian gland of two species of snakes: Pseudonaja textilis (Elapidae) and Thamnophis sirtalis (Colubridae)." Canadian Journal of Zoology 81, no. 3 (March 1, 2003): 357–63. http://dx.doi.org/10.1139/z03-014.

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The reptilian Harderian gland is a poorly understood cephalic structure. Despite the recent assertion that in snakes it may function as part of the vomeronasal system, the Harderian gland has been described in few snake species. In this study we examined the gross anatomy, histology, and ultrastructure of the Harderian gland of two different advanced snake species (Colubroidea): Pseudonaja textilis (Elapidae) and Thamnophis sirtalis (Colubridae). In both species the Harderian gland is a large serous gland whose secretions pass directly into the vomeronasal organ via the nasolacrimal duct. Contrary to previous publications, the Harderian gland in both species studied possesses a specific duct system lined by mucous cells. However, the Harderian glands of these two species differ in shape, the histochemical nature of these mucous secretions, and the ultrastructure of the serous granules. In conclusion, though the Harderian glands of snakes are remarkably conserved morphologically, there is some interspecific variation.

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24

Mirtschin, P. J., R. Shine, T. J. Nias, N. L. Dunstan, B. J. Hough, and M. Mirtschin. "Influences on venom yield in Australian tigersnakes (Notechis scutatus) and brownsnakes (Pseudonaja textilis: Elapidae, Serpentes)." Toxicon 40, no. 11 (November 2002): 1581–92. http://dx.doi.org/10.1016/s0041-0101(02)00175-7.

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25

Stocker, Kurt, Helena Hauer, Christian Müller, and Douglas A. Triplett. "Isolation and characterization of TextarinR, a prothrombin activator from eastern brown snake (Pseudonaja textilis) venom." Toxicon 32, no. 10 (October 1994): 1227–36. http://dx.doi.org/10.1016/0041-0101(94)90352-2.

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26

Williams, V., and J. White. "Characteristics of the procoagulant front the venom of the Australian common brown snake (Pseudonaja textilis)." Toxicon 33, no. 3 (March 1995): 257. http://dx.doi.org/10.1016/0041-0101(95)99233-s.

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27

Schreuder, Mark, Geraldine Poenou, Viola J. F. Strijbis, Ka Lei Cheung, Pieter H. Reitsma, and Mettine H. A. Bos. "Evolutionary Adaptations in Pseudonaja Textilis Venom Factor X Induce Zymogen Activity and Resistance to the Intrinsic Tenase Complex." Thrombosis and Haemostasis 120, no. 11 (August 20, 2020): 1512–23. http://dx.doi.org/10.1055/s-0040-1715441.

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AbstractThe venom of the Australian snake Pseudonaja textilis comprises powerful prothrombin activators consisting of factor X (v-ptFX)- and factor V-like proteins. While all vertebrate liver-expressed factor X (FX) homologs, including that of P. textilis, comprise an activation peptide of approximately 45 to 65 residues, the activation peptide of v-ptFX is significantly shortened to 27 residues. In this study, we demonstrate that exchanging the human FX activation peptide for the snake venom ortholog impedes proteolytic cleavage by the intrinsic factor VIIIa–factor IXa tenase complex. Furthermore, our findings indicate that the human FX activation peptide comprises an essential binding site for the intrinsic tenase complex. Conversely, incorporation of FX into the extrinsic tissue factor–factor VIIa tenase complex is completely dependent on exosite-mediated interactions. Remarkably, the shortened activation peptide allows for factor V-dependent prothrombin conversion while in the zymogen state. This indicates that the active site of FX molecules comprising the v-ptFX activation peptide partially matures upon assembly into a premature prothrombinase complex. Taken together, the shortened activation peptide is one of the remarkable characteristics of v-ptFX that has been modified from its original form, thereby transforming FX into a powerful procoagulant protein. Moreover, these results shed new light on the structural requirements for serine protease activation and indicate that catalytic activity can be obtained without formation of the characteristic Ile16–Asp194 salt bridge via modification of the activation peptide.

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28

Whitaker, Patrick Brian, and Richard Shine. "A RADIOTELEMETRIC STUDY OF MOVEMENTS AND SHELTER-SITE SELECTION BY FREE-RANGING BROWNSNAKES (PSEUDONAJA TEXTILIS, ELAPIDAE)." Herpetological Monographs 17, no. 1 (2003): 130. http://dx.doi.org/10.1655/0733-1347(2003)017[0130:arsoma]2.0.co;2.

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29

Minh Le, Thi Nguyet, Md Abu Reza, Sanjay Swarup, and R. Manjunatha Kini. "Gene duplication of coagulation factor V and origin of venom prothrombin activator in Pseudonaja textilis snake." Thrombosis and Haemostasis 93, no. 03 (2005): 420–29. http://dx.doi.org/10.1160/th04-11-0707.

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SummaryThe origin and evolution of venom toxins is a mystery that has evoked much interest. We have recently shown that pseutarin C, a prothrombin activator from Pseudonaja textilis venom, is structurally and functionally similar to mammalian coagulation factor Xa – factor Va complex. Its catalytic subunit is homologous to factor Xa while the nonenzymatic subunit is homologous to factor Va. P.textilis therefore has two parallel prothrombin activator systems: one expressed in its venom gland as a toxin and the other expressed in its liver and released into its plasma as a haemostatic factor. Here we report the complete amino acid sequence of factor V (FV) from its liver determined by cDNA cloning and sequencing. The liver FV shows 96% identity to pseutarin C nonenzymatic subunit. Most of the functional sites involved in its interaction with factor Xa and prothrombin are conserved. However, many potential sites of post-translational modifications and one critical cleavage site for activated protein C are different. The absence of the latter cleavage site makes pseutarin C nonenzymatic subunit resistant to inactivation and enhances its potential as an excellent toxin. By PCR and real-time quantitative analysis, we show that pseutarin C nonenzymatic subunit gene is expressed specifically in the venom gland at ~280 fold higher than that of FV gene in liver. These two are thus encoded by two separate genes that express in a highly tissue-specific manner. Our results imply that the gene encoding pseutarin C nonenzymatic subunit was derived by the duplication of plasma FV gene and they have evolved to perform distinct functions.

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30

Filippovich, Igor, Natasha Sorokina, Liam St Pierre, Simone Flight, John de Jersey, Naomi Perry, Paul P. Masci, and Martin F. Lavin. "Cloning and functional expression of venom prothrombin activator protease from Pseudonaja textilis with whole blood procoagulant activity." British Journal of Haematology 131, no. 2 (October 2005): 237–46. http://dx.doi.org/10.1111/j.1365-2141.2005.05744.x.

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31

Viala, Vincent Louis, Diana Hildebrand, Maria Trusch, Tamara Mieco Fucase, Juliana Mozer Sciani, Daniel Carvalho Pimenta, Raghuvir K. Arni, et al. "Venomics of the Australian eastern brown snake ( Pseudonaja textilis ): Detection of new venom proteins and splicing variants." Toxicon 107 (December 2015): 252–65. http://dx.doi.org/10.1016/j.toxicon.2015.06.005.

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32

Aird, Steven D., C. Russell Middaugh, and Ivan I. Kaiser. "Spectroscopic characterization of textilotoxin, a presynaptic neurotoxin from the venom of the australian eastern brown snake (Pseudonaja t. textilis)." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 997, no. 3 (August 1989): 219–23. http://dx.doi.org/10.1016/0167-4838(89)90190-8.

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33

Skejić, Jure, and Wayne C. Hodgson. "Population Divergence in Venom Bioactivities of Elapid Snake Pseudonaja textilis: Role of Procoagulant Proteins in Rapid Rodent Prey Incapacitation." PLoS ONE 8, no. 5 (May 14, 2013): e63988. http://dx.doi.org/10.1371/journal.pone.0063988.

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34

Bos, Mettine H. A., Michael Boltz, Liam St. Pierre, Paul P. Masci, John de Jersey, Martin F. Lavin, and Rodney M. Camire. "Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations." Blood 114, no. 3 (July 16, 2009): 686–92. http://dx.doi.org/10.1182/blood-2009-02-202663.

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Abstract Venomous snakes produce an array of toxic compounds, including procoagulants to defend themselves and incapacitate prey. The Australian snake Pseudonaja textilis has a venom-derived prothrombin activator homologous to coagulation factors V (FV) and Xa (FXa). Here we show that the FV component (pt-FV) has unique biologic properties that subvert the normal regulatory restraints intended to restrict an unregulated procoagulant response. Unlike human FV, recombinant pt-FV is constitutively active and does not require proteolytic processing to function. Sequence comparisons show that it has shed a large portion of the central B-domain, including residues that stabilize the inactive procofactor state. Remarkably, pt-FV functions in the absence of anionic membranes as it binds snake-FXa with high affinity in solution. Furthermore, despite cleavage in the heavy chain, pt-FV is functionally resistant to activated protein C, an anticoagulant. We speculate this stability is the result of noncovalent interactions and/or a unique disulfide bond in pt-FV linking the heavy and light chains. Taken together, these findings provide a biochemical rationale for the strong procoagulant nature of venom prothrombinase. Furthermore, they illustrate how regulatory mechanisms designed to limit the hemostatic response can be uncoupled to provide a sustained, disseminated procoagulant stimulus for use as a biologic toxin.

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35

Gilbert, Gary E., Valerie A. Novakovic, Randal J. Kaufman, Hongzhi Miao, and Steven W. Pipe. "Conservative mutations in the C2 domains of factor VIII and factor V alter phospholipid binding and cofactor activity." Blood 120, no. 9 (August 30, 2012): 1923–32. http://dx.doi.org/10.1182/blood-2012-01-408245.

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Abstract Factor VIII and factor V share structural homology and bind to phospholipid membranes via tandem, lectin-like C domains. Their respective C2 domains bind via 2 pairs of hydrophobic amino acids and an amphipathic cluster. In contrast, the factor V-like, homologous subunit (Pt-FV) of a prothrombin activator from Pseudonaja textilis venom is reported to function without membrane binding. We hypothesized that the distinct membrane-interactive amino acids of these proteins contribute to the differing membrane-dependent properties. We prepared mutants in which the C2 domain hydrophobic amino acid pairs were changed to the homologous residues of the other protein and a factor V mutant with 5 amino acids changed to those from Pt-FV (FVMTTS/Y). Factor VIII mutants were active on additional membrane sites and had altered apparent affinities for factor X. Some factor V mutants, including FVMTTS/Y, had increased membrane interaction and apparent membrane-independent activity that was the result of phospholipid retained during purification. Phospholipid-free FVMTTS/Y showed increased activity, particularly a 10-fold increase in activity on membranes lacking phosphatidylserine. The reduced phosphatidylserine requirement correlated to increased activity on resting and stimulated platelets. We hypothesize that altered membrane binding contributes to toxicity of Pt-FV.

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Rao, Veena, Sanjay Swarup, and Manjunatha Kini. "The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa." Thrombosis and Haemostasis 92, no. 09 (2004): 509–21. http://dx.doi.org/10.1160/th04-03-0144.

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SummaryPseutarin C, a group C prothrombin activator from Pseudonaja textilis venom, is a large protein complex consisting of catalytic and nonenzymatic subunits, which are functionally similar to the mammalian FXa-FVa complex. Here, we present the complete cDNA sequence of the catalytic subunit of pseutarin C. The cDNA of the catalytic subunit encodes a protein of 449 amino acids, which includes a 22-residue signal peptide, 18-residue propeptide and a mature protein of 409 amino acids. The deduced amino acid sequence shows 74-83% identity to group D prothrombin activators from snake venom and ∼42% identity to mammalian FX and has identical domain structure. The precursor of the catalytic subunit of pseutarin C has several unique features. The activation peptide of the catalytic subunit of pseutarin C is significantly smaller (27 as compared to 52 residues in mammalian FX) and does not contain any glycosylation sites. Unlike coagulation FXa, Ser52 and Asn45 of the light and heavy chains are O- and N-glycosylated in pseutarin C catalytic subunit. There is a 12-residue insertion in pseutarin C catalytic subunit close to the region that is implicated in binding to FVa. This is the first sequence of the catalytic subunit of a group C prothrombin activator.

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REZA, M. A., T. N. MINH LE, S. SWARUP, and R. MANJUNATHA KINI. "Molecular evolution caught in action: gene duplication and evolution of molecular isoforms of prothrombin activators in Pseudonaja textilis (brown snake)." Journal of Thrombosis and Haemostasis 4, no. 6 (June 2006): 1346–53. http://dx.doi.org/10.1111/j.1538-7836.2006.01969.x.

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Williams, V., and J. White. "Variation in the composition of the venom from a single specimen of Pseudonaja textilis (common brown snake) over one year." Toxicon 30, no. 2 (February 1992): 202–6. http://dx.doi.org/10.1016/0041-0101(92)90473-i.

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Rao, Veena, and R. Kini. "Pseutarin C, a Prothrombin Activator from Pseudonaja textilis Venom: Its Structural and Functional Similarity to Mammalian Coagulation Factor Xa-Va Complex." Thrombosis and Haemostasis 88, no. 10 (2002): 611–19. http://dx.doi.org/10.1055/s-0037-1613264.

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SummarySeveral snake venoms contain procoagulant proteins that can activate prothrombin. We have purified pseutarin C, a prothrombin activator from the venom of the Australian brown snake (Pseudonaja textilis). It converts prothrombin to thrombin by cleaving both the peptide bonds Arg274 – Thr275 and Arg323 – Ile324, similar to mammalian factor Xa. It is a protein complex (∼250 Kd) consisting of an enzymatic and a nonenzymatic subunit. These subunits were separated by reverse phase HPLC and their interactions with bovine factor Xa and factor Va were studied. The enzymatic subunit of pseutarin C has a ∼13 fold higher affinity for bovine factor Va (K d of 11.4 nM for pseutarin C enzymatic subunit – bovine factor Va interaction as compared to a K d of 147.4 nM for the bovine factor Xa-Va interaction). The non-enzymatic component, however, was unable to activate bovine factor Xa. N-terminal sequence analysis of the catalytic subunit of pseutarin C showed ∼ 60% homology to mammalian factor Xa and ∼78% homology to trocarin, a group D prothrombin activator from Tropidechis carinatus venom. Structural information for the non-enzymatic subunit of pseutarin C was obtained by amino terminal sequencing of several internal peptides. The sequence data obtained indicates that the non-enzymatic subunit of pseutarin C has similar domain architecture like the mammalian factor Va and the overall homology is ∼55%. Thus pseutarin C is the first venom procoagulant protein that is structurally and functionally similar to mammalian factor Xa-Va complex.

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TYLER, Margaret I., Merlin E. H. HOWDEN, Ian SPENCE, and Donald BARNETT. "Pseudonajatoxin b: unusual amino acid sequence of a lethal neurotoxin from the venom of the Australian common brown snake, Pseudonaja textilis." European Journal of Biochemistry 166, no. 1 (July 1987): 139–43. http://dx.doi.org/10.1111/j.1432-1033.1987.tb13493.x.

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Leong, Oriana S., Andrew M. Padula, and Ellie Leister. "Severe acute pulmonary haemorrhage and haemoptysis in ten dogs following eastern brown snake (Pseudonaja textilis) envenomation: Clinical signs, treatment and outcomes." Toxicon 150 (August 2018): 188–94. http://dx.doi.org/10.1016/j.toxicon.2018.05.020.

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Tyler, Margaret I., Donal Barnett, Philip Nicholson, Ian Spence, and Merlin E. H. Howden. "Studies on the subunit structure of textilotoxin, a potent neurotoxin from the venom of the Australian common brown snake (Pseudonaja textilis)." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 915, no. 2 (September 1987): 210–16. http://dx.doi.org/10.1016/0167-4838(87)90302-5.

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Meier, J., and K. Stocker. "Isolation, characterization and diagnostic potential of texlarin, a prothrombin activator from the venom of the Australian eastern brown snake Pseudonaja textilis." Toxicon 33, no. 3 (March 1995): 257. http://dx.doi.org/10.1016/0041-0101(95)99232-r.

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Rao, Veena S., Sanjay Swarup, and R. Manjunatha Kini. "The nonenzymatic subunit of pseutarin C, a prothrombin activator from eastern brown snake (Pseudonaja textilis) venom, shows structural similarity to mammalian coagulation factor V." Blood 102, no. 4 (August 15, 2003): 1347–54. http://dx.doi.org/10.1182/blood-2002-12-3839.

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Abstract Pseutarin C is a group C prothrombin activator from the venom of the eastern brown snake Pseudonaja textilis. It is a multi-subunit protein complex consisting of catalytic and nonenzymatic subunits similar to coagulation factor Xa and factor Va, respectively. Here we describe the complete sequence of the nonenzymatic subunit. Based on the partial amino acid sequence of the nonenzymatic subunit, degenerate primers were designed. Using a “walking” strategy based on sequentially designed primers, we determined the complete cDNA sequence of the nonenzymatic subunit. The cDNA encodes a protein of 1461 amino acid residues, which includes a 30-residue signal peptide, a mature protein of 1430 amino acid residues, and a stop codon. cDNA blot analysis showed a single transcript of approximately 4.6 kb. The deduced amino acid sequence shows approximately 50% identity to mammalian factor V and by homology has a similar domain structure consisting of domains A1-A2-B-A3-C1-C2. Interestingly, the B domain of pseutarin C is shorter than that of mammalian factor V (FV). Although most of the proteolytic activation sites are conserved, 2 of 3 proteolytic sites cleaved by activated protein C are mutated, and thus activated protein C is not able to inactivate this procoagulant toxin. The predicted posttranslational modifications, including disulfide bonds, N-glycosylation, phosphorylation, and sulfation, in pseutarin C are significantly different compared with bovine factor V. Thus, our data demonstrate that the nonenzymatic subunit of group C prothrombin activators is structurally similar to mammalian FV.

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Norval, Gerrut, and Michael G. Gardner. "Predation by an Eastern Brownsnake, Pseudonaja textilis (Duméril, Bibron, and Duméril 1854), on a Mallee Black-backed Snake, Parasuta nigriceps (Günther 1863)." Reptiles & Amphibians 25, no. 2 (August 1, 2018): 134–36. http://dx.doi.org/10.17161/randa.v25i2.14269.

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Millers, Emma-Karin I., Manuela Trabi, Paul P. Masci, Martin F. Lavin, John de Jersey, and Luke W. Guddat. "Crystal structure of textilinin-1, a Kunitz-type serine protease inhibitor from the venom of the Australian common brown snake (Pseudonaja textilis)." FEBS Journal 276, no. 11 (June 2009): 3163–75. http://dx.doi.org/10.1111/j.1742-4658.2009.07034.x.

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Webster, C., M. Massaro, D. R. Michael, D. Bambrick, J. L. Riley, and D. G. Nimmo. "Native reptiles alter their foraging in the presence of the olfactory cues of invasive mammalian predators." Royal Society Open Science 5, no. 10 (October 2018): 180136. http://dx.doi.org/10.1098/rsos.180136.

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Invasive mammalian predators are linked to terrestrial vertebrate extinctions worldwide. Prey naïveté may explain the large impact invasive predators have on native prey; prey may fail to detect and react appropriately to the cues of novel predators, which results in high levels of depredation. In Australia, the feral cat ( Felis catus ) and the red fox ( Vulpes vulpes ) are implicated in more than 30 animal extinctions and the naïveté of native prey is often used to explain this high extinction rate. Reptiles are one group of animals that are heavily preyed upon by F. catus and V. vulpes . However, very few studies have examined whether reptiles are naive to their cues. In this study, we examine the ability of two native reptile species ( Morethia boulengeri and Christinus marmoratus ) to detect and distinguish between the chemical cues of two invasive predators ( V. vulpes and F. catus ) and three native predators (spotted-tailed quoll, Dasyurus maculatus; dingo, Canis lupus dingo ; eastern brown snake, Pseudonaja textilis ), as well as two non-predator controls (eastern grey kangaroo, Macropus giganteus and water). We conducted experiments to quantify the effects of predator scents on lizard foraging (the amount of food eaten) during 1 h trials within Y-maze arenas. We found both study species reduced the amount they consumed when exposed to predator scents—both native and invasive—indicating that these species are not naive to invasive predators. An evolved generalized predator-recognition system, rapid evolution or learned behaviour could each explain the lack of naïveté in some native Australian reptiles towards invasive predators.

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Gong, NanLing, Arunmozhiarasi Armugam, and Kandiah Jeyaseelan. "Molecular cloning, characterization and evolution of the gene encoding a new group of short-chain α-neurotoxins in an Australian elapid, Pseudonaja textilis." FEBS Letters 473, no. 3 (May 12, 2000): 303–10. http://dx.doi.org/10.1016/s0014-5793(00)01549-0.

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Novakovic, Valerie A., Hongzhi Miao, Steven Pipe, and Gary E. Gilbert. "Conservative Mutations in the Membrane-Binding Motif of Factor V C2 Domain to Residues of Pseudonaja Textilis Venom Factor V Confer Phosphatidylserine-Independent Activity." Blood 118, no. 21 (November 18, 2011): 2243. http://dx.doi.org/10.1182/blood.v118.21.2243.2243.

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Abstract Abstract 2243 Toxicity of venom from the eastern brown snake (Pseudonaja textilis) is related to a prothrombin activator protein complex (pseutarin C) that is homologous to the factor Va/factor Xa complex. A previous study has found that the factor V-homologous subunit of this protein (pt-fV) is constitutively active and does not require anionic membranes to function (Bos et al. 2010, Blood). We have previously found that conservative mutation of the amino acids on the hydrophobic membrane binding regions (called spikes) of factor V (W2063M/W2064F/S2117L) can produce increased prothrombinase activity, increased membrane binding affinity and apparent phospholipid-independent prothrombinase activity. However, the membrane-independent activity is caused by retention of phospholipid by factor V through the purification process. We hypothesized that the P.textilis venom-derived factor V has an increase in lipid affinity due to differences in the membrane-interactive spikes. Sequence alignment of the P.textilis venom-derived factor V with bovine and human factor V revealed 5 amino acids located in the putative membrane-binding region (four on spike 3 and one in a region targeted by a small-molecule inhibitor of membrane binding for both factor VIII and factor V) that differed in the venom-derived factor V versus the consensus sequence of mammalian factor V. A mutant factor V that incorporated these five mutations (L2116M, S2117T, S2118T, E2119S, and S2183Y) (factor VMTTS/Y) was expressed in COS cells. After purification utilizing ion exchange chromatography, factor VMTTS/Y showed phospholipid-independent activity that could be inhibited with phospholipase A2. Subsequently, factor VMTTS/Y was washed extensively with CHAPS during purification to prevent phospholipid from co-purifying. Activity was measured with a prothrombin time assay with plasma lacking factor V. Specific activity was 1183 units/mg vs. 676 units/mg for wild type human factor V. Steady state kinetics of the prothrombinase complex with factor VMTTS/Y were assessed with varying concentrations of phospholipid vesicles. In the presence of membranes containing excess phosphatidylserine (15:20:65 PS:PE:PC), factor VMTTS/Y (5 pM) showed 39% greater Vmax than wild type human factor V and 3-fold higher apparent membrane affinity. With limiting phosphatidylserine (2:20:78 PS:PE:PC), factor VMTTS/Y (10 pM) showed 64% greater Vmax and 2-fold higher apparent membrane affinity. Factor VMTTS/Y, purified with a CHAPS wash, did not show lipid-independent activity but did support prothrombinase activity on membranes lacking PS or other negatively charged lipid (20:80 PE:PC). On these vesicles factor VMTTS/Y (50 pM) had a Vmax that was 8-fold higher than wild type factor V (see figure). These data indicate that the apparent phospholipid-independent activity results from higher membrane affinity or from greater activity on minimal phospholipid retained by factor V during purification. They imply that toxicity of pseutarin C may result, in part, from procoagulant activity on cell membranes that do not support the mammalian prothrombinase complex. Furthermore, they indicate that the precise manner in which the C2 domain of factor V binds to a phospholipid membrane influences the Vmax of the prothrombinase complex. Disclosures: No relevant conflicts of interest to declare.

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Triplett, Douglas A., Kurt F. Stocker, Gail A. Unger, and Linda K. Barna. "The Textarin/Ecarin Ratio: A Confirmatory Test for Lupus Anticoagulants." Thrombosis and Haemostasis 70, no. 06 (1993): 0925–31. http://dx.doi.org/10.1055/s-0038-1649701.

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SummaryLupus anticoagulants (LA) are immunoglobulins (IgG, IgM, IgA or a mixture) which interfere with in vitro phospholipid (PL) dependent tests of coagulation (e.g. APTT, KCT, dilute Russell Viper Venom Time). LA are heterogeneous; consequently, the laboratory diagnosis is difficult and relies on multiple tests. We have developed a sensitive and relatively specific confirmatory test system based on fractions of two snake venoms. Textarin®, a protein fraction of Pseudonaja textilis venom (Australian Eastern brown snake), activates prothrombin in the presence of PL, factor V and calcium ions. Ecarin, a protein fraction of Echis carinatus venom, will activate prothrombin in the absence of any cofactors. The activation of prothrombin by Textarin yields thrombin while Ecarin yields meizothrombin. In the presence of LA, the Textarin time is prolonged and the Ecarin time is unaffected. The test results are reported as a ratio of Textarin/Ecarin times (abnormal greater than 1.3). We have evaluated this test system in the following patient populations: LA positive, therapeutically heparinized, stable oral anticoagulated, liver disease, routine preoperative, anticardiolipin antibody positive LA negative, hemophilia A, various other hereditary factor deficiencies or dysfunctional proteins, and specific inhibitors of factor V and factor VTII. The LA positive patients represented a mixed population of autoimmune disease, drug-induced and post-infectious states. Our findings indicate the sensitivity of the Textarin/Ecarin system in the confirmation of LA. In order to use the test system most effectively, it is recommended to incorporate poly-brene with Textarin when evaluating heparinized samples. Factor V deficiency and specific inhibitors of factor V yielded, in some instances, false positive results.

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