GlycoMIP and a Novel Peptidoglycan Structure in Lyme Disease

The bacterial cell wall is a unique glycomaterial composed of rigid glycans cross-linked by flexible peptides, aptly called peptidoglycan. Beyond its protective barrier function, the peptidoglycan architecture imposes biophysical limitations on cell shape, flexibility, and motility. Although alterations in the peptide chemistry occur, deviations from the glycan structure have not previously been reported. The GlycoMIP User Facility at Virginia Tech is supporting the work of Dr. Brandon Jutras, an Assistant Professor in the Department of Biochemistry at VT in characterizing a novel glycan in the cell wall of Borrelia burgdorferi, the causative agent of Lyme disease. The article entitled "The unusual cell wall of the Lyme disease spirochaete Borrelia burgdorferi is shaped by a tick sugar," is the first published effort by the Jutras Team utilizing GlycoMIP resources. This new glycan structure has led to a paradigm shift in our understanding of bacterial cell wall architecture. Inasmuch, the article is ranked in the top 5% of all science publications with similar publication dates. The findings described in the paper are important for understanding how glycan composition imparts dramatic biophysical changes in cell wall flexibility, elasticity and shape, which are ultimately reflected in bacterial motility and survival. The structures unique to the microbe can also be considered targets for detection and treatment. The novel materials are presently being purified using GlycoMIP resources to advance methods for pathogen detection.
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