부산대학교 도서관

Objective Research suggests human norovirus binding to histo-blood group antigen (HBGA)-like molecules on enteric bacteria may enhance viral pathogenesis; however, the properties of these bacterial ligands are not well known. Previous work identified, but did not characterize, seven norovirus-binding bacteria. To further examine this bacteria-virus binding interaction, enteric bacteria were analyzed via Western blot with anti-HBGA antibodies and lectins targeting HBGA-associated sugar components. Virus overlay assays using capsids from six different human norovirus strains further identified responsible ligands and strain dependent binding properties. Results Each bacterial species possessed varying degrees of HBGA-like activity, and lectin binding further elucidated potential sugar residues involved (N-acetyl-galactosamine, [alpha]-d-galactose or [alpha]-l-fucose). Both GI and GII norovirus capsids bound specific bacterial ligand sizes, and generally corresponded to anti-HBGA Western blot patterns. A 35-kDa band reacted with all HBGA antibodies, bound all six of the noroviruses tested, and had a high affinity for the lectins. Collectively, this work characterizes the varying carbohydrate residues potentially responsible for norovirus-bacteria interactions and provides a basis for future ligand identification. Keywords: Norovirus-bacteria interactions, Glycoprotein, HBGA, Lectin, Enteric
Author(s): Erin A. Almand[sup.1,4] , Matthew D. Moore[sup.2,3] and Lee-Ann Jaykus[sup.1,5] Introduction Human norovirus is the leading cause of viral gastroenteritis worldwide, yet there are still multiple questions related to [...]