Publications by Gerald Laurence Murray

Publications by authors named "Gerald Laurence Murray"

Page 1 of 1

Conserved transmembrane glycine residues in the Shigella flexneri polysaccharide co-polymerase protein WzzB influence protein-protein interactions.

Magdalene Papadopoulos Elizabeth Ngoc Hoa Tran Gerald Laurence Murray Renato Morona

Microbiology (Reading)

June 2016

The O antigen (Oag) component of lipopolysaccharides (LPS) is crucial for virulence and Oag chain-length regulation is controlled by the polysaccharide co-polymerase class 1 (PCP1) proteins. Crystal structure analyses indicate that structural conservation among PCP1 proteins is highly maintained, however the mechanism of Oag modal-chain-length control remains to be fully elucidated. Shigella flexneri PCP1 protein WzzBSF confers a modal-chain length of 10-17 Oag repeat units (RUs), whereas the Salmonella enterica Typhimurium PCP1 protein WzzBST confers a modal-chain length of ~16-28 Oag RUs.

View Article and Find Full Text PDF

- Gerald Laurence Murray's research focuses on the structural and functional analysis of polysaccharide co-polymerase proteins (PCP1) that play a critical role in the regulation of O antigen chain-length in lipopolysaccharides (LPS).
- One significant finding from his 2016 article highlights that conserved transmembrane glycine residues in the Shigella flexneri polysaccharide co-polymerase protein WzzB influence important protein-protein interactions that determine O antigen modal-chain-length.
- The study suggests that while there is structural conservation among PCP1 proteins, the precise mechanisms for regulating O antigen chain-length remain an area for further investigation, which could have implications for understanding bacterial virulence.

Publications by authors named "Gerald Laurence Murray"

Conserved transmembrane glycine residues in the Shigella flexneri polysaccharide co-polymerase protein WzzB influence protein-protein interactions.

Synopsis of recent research by authors named "Gerald Laurence Murray"