In recent years, bacterial resistance to glycopeptide antibiotics has been steadily increasing; therefore, treatment options for bacterial infections are becoming few. Structural information about glycopeptide antibiotics could indicate how they recognize their targets and thus will be useful in the design of new treatments. As crystallographic studies of the bacterial cell wall peptide in complex with the antibiotic have proven difficult, a macromolecular tool was needed to aid these studies. This tool consists of a readily crystallized protein fused to the cell wall mimetic. The distance between these two components was varied by a linker, thereby increasing the probability that crystallization will occur. Sequence- and ligation-independent cloning and native protein ligation were used to develop this macromolecular tool. The structural interactions identified from the use of this tool to co-crystallize glycopeptide antibiotics with their substrates will be used to develop a new generation of therapeutics.

Development of a macromolecular tool to study the interaction of glycopeptide antibiotics with the bacterial cell wall

239th National Meeting (2010)

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