DOPING IN SPORT
What the hell? There was no other way to react to the bizarre headlines that dropped in November last year.
“Tour de France rider tried to obtain marine worm haemoglobin for blood doping boost,” read Cycling News. “I never thought the next breakthrough in doping would be fishing worms,” wrote an op-ed from Cycling Weekly. More poetically: “Opening a can of worms” from the bike journalism project Escape Collective. It certainly had.
Any mention of doping in cycling probably sends fans into a nail-biting chatter as they remember the halcyon years of 1990s juicing.
This story, though, is something far odder. We're not just talking about blood from a human. Not even another mammalian species; we're climbing the ladder of Linnaean classification: Genus – Family – Order – Class (looking back at all our fellow mammals) – Phylum (saluting every animal with a backbone) – and up to Kingdom, where we neatly jump over to the annelids (the segmented worms) and scramble all the way back down to the genus Arenicola.
That's where oceanographer Franck Zal landed in the noughties, when he was based at the French national scientific research organisation CNRS and the Sorbonne University. His motivation wasn't juicing his favourite French pedallers. Instead, his research had identified potential applications for haemoglobin – that allimportant protein responsible for transporting oxygen to our tissues – extracted from a species of European lugworm (Arenicola marina).
Worm haemoglobin is far more potent than the haemoglobin humans possess, and Zal saw its promise as a therapeutic that could support the preservation of transplanted organs.
But that unnamed Tour de France athlete clearly saw the possibilities of harnessing worm blood to turbocharge his circulatory system for the big race.
To understand why the frontier of performance enhancement has athletes looking elsewhere in the animal kingdom, it's important to consider where these biological boosters come from, and what they do.
Power of the protein
Almost every vertebrate contains haemoglobin proteins in their red blood cells. Its job is vital: delivering oxygen to tissues through the blood. In mammals, haemoglobin consists of four subunits, each a long, folded chain of amino acids that determine the protein's properties and function. These subunits are each connected to a heme group: a ring of organic compounds that contain a single iron ion. This iron bindsWith four subunits, each haemoglobin can carry four oxygen molecules. Think of haemoglobin as a four-seater car. The car itself is the haemoglobin, its four seats the subunits, and the driver and their three mates are the oxygen molecules being transported to their destination.
