- The Washington Times - Wednesday, January 28, 2004

Leading scientists believe that sugar-coated proteins (called glycoproteins) will soon assist in the treatment of everything from bacterial infections to inflammation.

Pharmaceutical manufacturers have long been interested in developing therapies with sugars attached. However, cells use many different sugars, and arrays of them must be stacked in precise order and then attached to proteins in particular places to be effective. Several companies have succeeded in producing products like the antibiotic vancomycin and imiglucerase, an enzyme used in treating Gaucher’s disease. Other companies have sugar-based antibiotics, anti-inflammatories and even anti-cancer therapies in development.

However, the production of glycoproteins has proved difficult. They are typically made by inserting genes into mammalian cells and then collecting the products. However, that method takes weeks and only yields small amounts of impure product. The mammalian cells used in the manufacture of such medicines may also host viruses. Preventing contamination by such pathogens is not easy.

Last year, a research group led by Tillman U. Gerngross announced that they had discovered a way to set up a sugar-complex assembly line in yeast. Yeast cells — which have long been used to produce products like beer and bread — are similar to human cells and so contain the basic manufacturing machinery required. However, that cellular assembly line had to be altered in several significant ways. In addition to deleting many yeast genes, the Gerngross group inserted numerous human genes and also added enzymes from several different creatures, such as rats and worms.

To the surprise of almost everyone, the technique worked better than expected. The modified yeast not only survived, it also produced nearly pure glycoproteins. While several other problems must be worked out, the technique shows significant commercial potential, since it would reduce manufacturing times to days and permit industrial-scale production.

The assembly-line manufacture of glycoproteins seems just the beginning. Proteins can be modified in a vast variety of other ways after being built, which significantly alters their function. Scientists are slowly learning how to mimic those changes. Policy-makers and consumers should stay tuned. Sweet medicines are not far away.

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