The new information could lead to renewed interest in anti-infectives research from big pharmaceutical companies who have shied away from the area as new antibiotics tend to be reserved as last-line solutions for fear of generating resistance. This has held back peak sales leading to many large pharmaceutical firms cutting antibiotics research, with only ten drugs being approved since 1998.

Until the publication of the research in the latest issue of the journal Science, researchers had been struggling to determine the structure of the enzyme that helps build bacterial cell walls. The researchers managed to crystallise and solve the structure of the enzyme on its own and when bound to the animal antibiotic moenomycin.

The enzyme, PBP2, is common to all bacteria and the new structural information should speed up the design of new antibiotics, which are in constant demand as drug resistant strains, such as methicillin-resistant Staphylococcus aureus (MRSA), continue to develop. MRSA is a cause of much concern among hospital staff and patients and its resistance to both penicillin and amoxicillin has allowed the problem to grow to epidemic proportions.

"The cell wall has all the hallmarks of a great drug target, it is essential to the survival of all bacteria. The enzymes that create the cell wall are unique to bacteria. And it is accessible; you don't have to get the antibiotics into the cell," said Dr Natalie Strynadka, of the Howard Hughes Medical Institute (HHMI) at the University of British Columbia in Vancouver and the corresponding author of the article.

This is the first time a structure of one of the enzymes that removes sugar molecules from lipids and attaches them to other sugars has been solved. This sugar transfer is used in a wide range of biochemical reactions including allergic responses and cell signalling in cancer.

PBP2 has two main parts, one that assembles long sugar fibres and the other that binds them to proteins to form the bacteria's cell wall. This second step is targeted by penicillin and has been well studied.

"This enzyme is an awesome target for antibiotics, we have a totally new understanding of how the enzyme works and how a very good animal antibiotic inhibits the enzyme." said Strynadka.

While the human body poorly absorbs moenomycin, the new understanding of how it disrupts enzyme function should help the design of modified versions that are more suitable for human use.

The researchers believe that moenomycin mimics the sugar-lipid, lipid II, irreversibly binding with the enzyme, blocking its uptake of more sugar molecules.