A family of snakes in South and Central America have potentially fatal venom that can disrupt blood clotting and cause hemorrhage, strokes and kidney failure.
Researchers from the Laboratory of Applied Toxicology at the Instituto Butantan in Sao Paulo, Brazil and the University of New Hampshire studied the protein toxins in venom from the lancehead snakes, hoping to find the key to developing a more effective treatment to a bite.
They looked at a group of sugar molecules, called gylcans, found in a complex chain that can be attached to proteins.
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Vipers in Central and South America have venom that can disrupt blood clotting and cause hemorrhage, strokes and kidney failure and can be fatal. Pictured: A drop of venom being extracted from a lancehead snake
Most proteins in lancehead venom are modified with glycans, according to researcher Solange Serrano.
However, very little is known about the actual structure of the sugars in the snake venom.
Researchers were able to characterize the structure of 60 glycan chains in eight lancehead species’ venom.
Then, they were able to analyze them and break down each complex molecule to understand what sugars were present, and how they affected the venom.
They discovered that lancehead venom contains nearly 100 milligrams of protein per milliliter of liquid.
At this high of a concentration, protein solutions can to become very thick and sticky or form gels.
Researchers from the Laboratory of Applied Toxicology at the Instituto Butantan in Sao Paulo, Brazil and the University of New Hampshire studied the protein toxins in venom from the lancehead snakes, hoping to find the key to developing a more effective treatment to a bite
After analyzing the structures, the researchers found that an unusually high number contained sialic acid, a sugar with a negative charge.
‘Glycans containing sialic acid may help in venom solubility and increase toxin half-life,’ said Serrano.
The acid could also bind to host proteins called siglecs, which would then pull the toxic enzymes closer to target cells for greater effect, essentially causing more damage in the person receiving the bite.
With this research into basic structures of the venoms, scientists hope they can develop more efficient treatments for viper bites.
Inland taipan: Native to Australia, a bite from the inland – or western – taipan could paralyse you, stop your breathing and cause haemorrhaging.
Coastal taipan: The cousin of the inland taipan, this snake’s bites kill in more than 80 per cent of untreated cases.
King Cobra: Perhaps the most iconic snake, cobra venom will paralyse you and one bite can kill an elephant. It is native to India and south-east Asia.
Banded krait: Yet more paralysis-inducing venom from this resident of India and south-east Asia.
Saw-scaled viper: Found across Africa and Asia, this one is thought to be the biggest snake killer of humans. It is not the most venomous but bites most often.
‘The antivenoms do a reasonable job, but they are not so good at neutralizing the local effects of snakebite,’ including swelling, hemorrhage and necrosis, Serrano said.
Damage from bites could sometimes be severe enough that doctors needed to amputate bitten limbs.
The research may also have benefits for medicine and biotechnology, as some venom proteins have already been repurposed as medication.
Knowing more about how glycosylation affects each protein could change the way the venoms are used.
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