Certain natural hazards attach to the otherwise pleasant business of going bush to commune with nature in the great southern land - deadly spiders, snakes and crocodiles lie in wait for the unsuspecting bushwalker.

And Australia has the world's deadliest tick, a nasty bushwhacker, Ixodes holocyclus, the bane of pet owners and veterinarians along a great arc of the eastern coast, from the Iron Range in far north Queensland, to Lakes Entrance in eastern Victoria.

The tick's natural host is the bandicoot, but it also takes a toll on cats, dogs, foals and calves. Around five days after it attaches and begins to feed on its host's blood, the tick begins secreting a potent neurotoxin in its saliva.

Some 24 hours after the venom enters its bloodstream, the animal becomes lethargic and exhibits paralysis of its rear limbs. Vomiting and unconsciousness follow, and if the tick is not detected and removed, death can occur within 48 hours.

There's a dog-serum anti-venom, but no vaccine. Developing a vaccine against any external parasite is one of immunology's major challenges.

Matt Padula has spent seven years on a part-time PhD, looking for suitable antigens for a tick vaccine since 2000. Padula is also a full-time technical specialist at the Proteomics Technology Centre of Excellence at the University of Technology, Sydney (UTS) which provides technical advice to researchers around Australia with proteomics problems.

The tick's neurotoxin seemed an ideal target, and Padula spent five years investigating its potential as a key antigen for a vaccine.

But two years ago, Dr Ben Herbert, a founder both of Sydney company Proteome Systems and the Australian Proteome Analysis Facility, joined UTS as director of the centre.

"He suggested that, rather than trying to stop something that occurs five days after the tick begins to feed, we should be hunting vaccine targets that stop the tick feeding in the first place," Padula says.

"Essentially what I've been trying to do since then is to fractionate whole male and female ticks, and see what proteins we get on our 2-D gels."

Like other ticks, I holocyclus secretes proteins in its saliva that suppress the host species' immune response - otherwise the host could begin making antibodies against the tick's proteins, with potentially lethal results.

Reasoning that protease enzymes were likely to be involved in neutralising the host's immune response, Padula and his colleagues devised a way of exploiting the high biochemical energy present in enzyme reactions to activate a fluorescence reaction, so that any spot containing an enzyme would show up in their 2-D gels.

They purified other proteins via affinity chromatography and Western blotting, using commercial anti-tick dog serum, and several litres of serum from a human subject who had developed a hyperallergic reaction to tick bites.

The anti-tick antibodies in the sera would bind their corresponding antigens, and could then be eluted and run through a mass spectrometer to determine their mass and peptide sequence.