First a few details. The initial contract asked me to spend two days a week for 12 weeks at the university and to write at least one article a week during that time for use as a press release or in the university magazine. The contract also left me free to write and interview people for radio about work in progress at the university as much as I liked.

Any journalist will appreciate that my first concern was whether there would be enough good stories. Normally, science journalists get their stories from journals, or press conferences or tip-offs from scattered contacts, and not by going around one university with a notebook.

A second concern was whether, if the stories were there, the scientists and engineers responsible for them would be prepared to let me write them up and to be interviewed. Scientists often cannot talk about their work before publishing it, and may be nervous of accidentally disclosing ideas which could lose them a patent. Engineers are especially wary of giving a good idea away to the opposition. These were reasonable fears. But in fact there turned out to be plenty of stories that did not run into any of the problems I had expected. In fact, since no journalist worth their salt can see a story without writing it, in my first term at Loughborough I wrote about 25. All of them were used in one way or another. I also interviewed about twenty people. Nearly all the interviews were broadcast.

To give an idea of the variety of the material, among other things I wrote about using lasers to measure stress on bridges, replacing surgical stitches with glue for heart surgery, transparent engine cylinders used to reveal what happens inside when fuel burns and the value of dragonflies as indicators of pollution. The stories appeared in journals and newspapers, including the Sunday Times, The Economist and (on one occasion) the Reader’s Digest, and were broadcast in programmes including Science in Action, Discovery, Global Concerns, Farming World and Health Matters.

The point of all this detail is that it convinced me and will (I hope) convince the reader that there ought to be more science writers in residence at British universities. At present there are very few. As a result, press releases from British universities, with a very few laudable exceptions (such as the new media briefs from Imperial College, London, and University College London), have very little science in them. Compare the situation in Britain with the norm in American and Canadian universities, virtually all of which employ full-time or part-time writers.

In Britain, by and large, we only hear about work in progress when something is published. Because of the intense competition to find a place in such science journals as Nature, this means that an awful lot of good, interesting and important work never gets near the public at all. Yet as I think my experience showed, if you put a nosy and moderately avaricious old hack down on a campus and let him or her snuffle around for a month or two, then up come the stories, and a lot of science and engineering ideas are communicated.

There is more to it than that, of course. I have run workshops intended to help people explain their work at lay level. I was surprised at just how much effect one day’s work of this kind had. I know media training is now in full swing in some government laboratories but I have the feeling that university scientists may be missing out on it. Many of them may see this as a cause for rejoicing. But if there is a perceived need for media training, then there may be a lot to be said for having it done by a familiar figure around the campus, with whom you or your friends or colleagues have built up a friendly relationship.

There’s also a reverse side to all this, which, if the idea of more science writers in residence really caught on, could be quite as important. That is the education of the writer. Unless journalists have PhDs they usually know very little about how universities work, and indeed little about what the working day of a scientist or engineer is like. Such things do not affect the main content of a story. But they can and perhaps should affect the way it is written, and where the emphasis is placed.

Much science writing can be rather colourless; just a brief résumé of how a piece of research has led to an improved treatment for disease or the discovery of a predicted fundamental particle, or whatever. In part, this is due to lack of space. Two or three hundred words are often all one has, and this doesn’t leave much room for colour. But perhaps it is also due to a lack of familiarity with the kind of world the story grew out of. Writers in residence could turn in livelier copy.

Having science writers (and broadcasters) in residence would considerably increase and enhance the coverage of science in the media. It would also enable writers and scientists to get to know each other much better, to their mutual advantage. It would subtly, but I believe substantially, improve the images that scientists and engineers and their professions present to the public.

Suppose a group of three neighbouring universities were to club together to fund a science writer for one academic year. The boost in the coverage of their research both nationally and locally would be substantial. So much so, perhaps, that other universities would follow suit, while the first writer moved on to a three-year contract.

Oh, and by the way, thank you Loughborough University of Technology. If other universities are as patient and as helpful, then being in residence won’t just be useful. It’ll be life-enhancing.

HIV particles are spherical, with an outer protein coat and an inner
membrane surrounding the nucleic acid in the middle. Once HIV particles get
into the bloodstream, they fasten onto receptors on T cells and squeeze their
way into the cells. When inside, the membrane ruptures, the viral genes spill
out and p17 goes to work. It helps to integrate viral genes into the host
cell’s chromosomes (which makes retroviruses impossible to eradicate without
destroying the infected cell). And it organises the virus’s budding out of the
cells when it replicates.

Understandably p17 is a high-priority target for designers of anti-HIV
drugs. lain Campbell of the University of Oxford recently won the race to
solve the structure of p17, using nuclear magnetic resonance.

The molecule looks like four short lengths of coiled spring, helices of
assorted shapes and lengths, fastened together with bits of bent wire.

As a routine measure the Alan and Sue Kingsman sent this information to the
US National Laboratory at Brookhaven, where a database of all known protein
structures is kept, for the usual automated search for anything similar. The
search showed that three of the four coils are strikingly similar in the two
molecules, though there are also two significant differences in structure.

Is it just coincidence? The Kingsmans are noncommittal. But interestingly,
interferon was shown back in the 1970s to inhibit the replication of other
retroviruses. This could mean that gamma interferon has evolved to compete
with pl7, or vice versa. Interferon appeared to slow up the assembly of virus
particles, as might be expected if it was competing with p17.

The Kingsmans are now updating the experiments, to study the effects of
gamma interferon on cells infected with mouse leukaemia virus. Here the role
of p17 is played by a similar protein called pl5. If the interferon slows up
viral replication, that will support the idea that gamma interferon combats
retroviruses in general. The Oxford team are also overexpressing gamma
interferon in cells infected with HIV particles, to see what happens. The
results could encourage drug designers to go for something that could compete
with p17 more effectively than interferon, or that could boost its
effects.

A team led by Bill Boys of the University of Edinburgh, beat Genentech,
a Californian subsidiary of the pharmaceuticals company Hoffmann-la Roche,
and became the first to crystallise tissue factor and determine its structure.
Boys and his collaborators, among them Ted Tuddenham of the Clinical Sciences
Centre (CSC) at the Hammersmith Hospital in London and Karl Harlos of the
Oxford Centre for Molecular Sciences, are now working towards crystallising
the complex of tissue factor bound to Factor 7, in order to get the complete
structure of the complex.

Their work is likely to lead eventually to a new anticlotting drug for
people at risk of inappropriate blood clotting. Instead of starting the
healing of wounds this type of clotting contributes to the furring-up of
arteries, to strokes and coronary heart disease. ‘We can now use the structure
of the binding site on tissue factor to model a small molecule, a peptide
which will fit onto and attach itself strongly to the binding site on tissue
factor, and so block the binding of Factor 7. Such a drug should stop
the whole process of clot formation right at the start,’ says Boys. An
alternative approach, when the structure of the complete complex is known,
could be to design molecules to block Factor 7’s binding site.

Because a drug based on such a peptide would stop the clotting process
before it began, it would, the researchers hope, be more selective and have
fewer side effects than warfarin and other anticlotting drugs in use today.
With such a prize in view, it is not surprising that there was a close race.
Boys originally obtained cloned tissue factor from Genentechunder an agreement
which required him and Harlos to report their findings to Genentech. When
Genentech were told Boys had crystals, they mounted a crash programme to
catch up, and are now about to publish their version of the structure.

Meanwhile, Tuddenham is working at the CSC to clone tissue factor himself
for the British group. If they use their own tissue factor they will be
able to pursue the structure of the tissue factor-Factor 7 complex without
any obligation to report their findings to Hoffman and Genentech. The team
hopes to collaborate with a British pharmaceuticals company. Japanese pharmaceuticals
companies have already been on the phone since Boys and company published
their findings in Nature (vol 370, p 662).

Others in the field recognise the importance of the achievement. Tom
Meade, director of the MRC’s Epidemiology Unit at St Bartholomew’s Hospital
in London, who is working on the causes of thrombosis in arteries, says
that understanding the formation of the complex made when tissue factor
binds to Factor 7 is the key to controlling the clotting process. Getting
the structure of tissue factor is a major step forward. The next step will
be to see if this can lead to the development of drugs able to control clotting
without causing inadvertent bleeding.