Toxins Flashcards

1
Q

Venomous definition

A

Capable of producing poison in a highly developed gland or group of cells and can deliver the toxin (i.e. barbs, beaks, fangs or modified teeth, harpoons, nematocysts (cnidaria)

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2
Q

Poisonous definition

A

Contains tissues that are toxic – no mechanism to deliver the poison.

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3
Q

Venom Delivery - Penetrant

A

Barb is ejected at prey (this is occurs via stimulation of the cnidocil)
This fills cell with water causing the cell to turn inside out which causes expulsion of the barb
These barbs can only be used once
Once used the nematocyst is sent back to the gastrovascular cavity for digestion and replaced by a nematoblast

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4
Q

Venom Delivery - Stenotele

A

Barb is released along with a long tube to wrap around prey:
The triggered capsule, which is ejected from the cell, discharges its tubular content (shaft, stylets and tubule) by a process of evagination.
In doing so the three joined stylets punch a hole into the cuticle of the prey through which the long evaginating tubule penetrates into the interior of the target

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5
Q

Cone Shells

A

fire expendable harpoon from proboscis

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6
Q

Snakes

A
around 20 proteins found in venom
Viperidae:
Long hollow fangs on a short maxillary bone, can be rotated independently (movable)
Elapidae (i.e. cobras):
Short, hollow, fixed fangs
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7
Q

Venoms

A
Contain proteins and peptides
Defence: highly conserved - localised pain
Predation: more variable/complex
can be pro/anti coagulant
developed in regard to specific diet
highly metabolic to produce
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8
Q

Spiders and scorpions

A

may inject more venom with increased resistance
E.g. some scorpions have a pre-venom used for defence
If the threat persists after pre-venom injection, or the scorpion is hunting they will inject their more expensive/ metabolically costly proteinaceous and enzymatic venom

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9
Q

Widow Spiders

A
o Venom:
Neurotoxic proteins
Proteolytic enzymes (lead to oedema (fluid retention) and swelling)
o Effects:
Muscle pain, cramps, tremor
Joint pain
Headache and dizziness
Oedema
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10
Q

Brown or Violin Spiders

A
o Venom:
Sphingomyelinase D
Phospholipase, hyaluronidase
Protease Esterase, Ribonuclease
Collagenase

o Effects:
Vascular damage and tissue necrosis
Lethality – intravascular hemolysis, thrombocytopenia
Hemoglobinuria leading to renal failure

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11
Q

Coagulation

A

Serpins are compounds that can inhibit serine proteases.
Some snake venoms cause coagulation, some cause anti-coagulation
Viperid species generally have hemotoxic and necrotizing effects causing tissue death (also some neurotoxins present in venom)
Elapid snakes tend to be predominantly neurotoxic effects

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12
Q

Snake Venom Metalloproteins

A

Affect blood clotting
Affect the permeability of blood molecules
Cleave parts of ECM (cleave integrin’s and cadherin’s) interfering whit how cells bind to each other
This leads to interruption of cell interaction and break down of blood vessels.
Haemostatic pressure is able to burst capillaries

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13
Q

Snake envenomation

A

Leads to inflammation and Oxidative stress

Viper envenomation tends to lead to tissue death

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14
Q

a - Neurotoxins

A

Elapids: cobra, Hydrophidae (sea snakes)
Inhibit nicotinic acetylcholine receptors at the neuromuscular junction
Alpha bungarotoxin (a-BTX) acts on the post synaptic cell leading to flaccid paralysis = can’t contract muscle (no breathing etc.)

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15
Q

Mongoose Resistance

A

Agile
Thick skinned
Resistance to a-neurotoxins (resistant to a-BTX)
This is a result of major substitutions in the ligand binding site (nAch receptors)
Mongoose nAchR (nicotine acetycholine receptor) does not bind a-BTX in vivo or in vitro

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16
Q

Captopril

A
Brazilian arrowhead (lancehead) viper
Causes circulatory shock (fall in BP)
17
Q

Bradykinin

A

Peptide found in captopril
Causes a drop in blood pressure
Broken down by ACE - same enzyme that converted Angiotensin I to Angiotensin II

18
Q

Development of Bradykinin drug

A

Only one form effective and long lasting which is found in venom:
Teprotide, Expensive, Only possible to administer orally
doesn’t inhibit ACE enough to become therapeutic drug