Conserved transmembrane glycine residues in the Shigella flexneri polysaccharide co-polymerase protein WzzB influence protein-protein interactions
Magdalene Papadopoulos, Ngoc Hoa Tran Elizabeth, Gerald Laurence Murray, Renato Morona
Microbiology | MICROBIOLOGY SOC | Published : 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. Both proteins share >70 % overall sequence identity and contain two transmembrane (TM1 and TM2) region..View full abstract
Awarded by National Health and Medical Research Council (NHMRC) of Australia
This study was supported by a Program Grant (#565526) from the National Health and Medical Research Council (NHMRC) of Australia to R. M.