Affinities of human histo-blood group antigens for norovirus capsid protein complexes.
The binding profiles of many human noroviruses (huNoVs) for human histo-blood group antigens have been characterized. However, quantitative-binding data for these important virus-host interactions are lacking. Here, we report on the intrinsic (per binding site) affinities of HBGA oligosaccharides for the huNoV VA387 virus-like particles (VLPs) and the associated subviral P particles measured using electrospray ionization mass spectrometry. The affinities of 13 HBGA oligosaccharides, containing A, B and H epitopes, with variable sizes (disaccharide to tetrasaccharide) and different precursor chain types (types 1, 2, 3, 5 and 6), were measured for the P particle, while the affinities of the A and B trisaccharides and A and B type 6 tetrasaccharides for the VLP were determined. The intrinsic affinities of the HBGA oligosaccharides for the P particle range from 500 to 2300 M(-1), while those of the A and B trisaccharides and the A and B type 6 tetrasaccharides for the VLP range from 1000 to 4000 M(-1). Comparison of these binding data with those measured previously for the corresponding P dimer reveals that the HBGA oligosaccharides tested exhibit similar intrinsic affinities for the P dimer and P particle. The intrinsic affinities for the VLP are consistently higher than those measured for the P particle, but within a factor of three. While the cause of the subtle differences in HBGA oligosaccharide affinities for the P dimer and P particle and those for the VLP remains unknown, the present data support the use of P dimers or P particles as surrogates to the VLP for huNoV-receptor-binding studies.
Alberta Glycomics Centre, Department of Chemistry, University of Alberta, Edmonton, AB, Canada T6G 2G2.
Ling
L
Han
Alberta Glycomics Centre, Department of Chemistry, University of Alberta, Edmonton, AB, Canada T6G 2G2.
Elena N
EN
Kitova
Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Ming
M
Tan
Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Xi
X
Jiang
Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada V8W 3P6.
Benjamin
B
Pluvinage
Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada V8W 3P6.
Alisdair B
AB
Boraston
Alberta Glycomics Centre, Department of Chemistry, University of Alberta, Edmonton, AB, Canada T6G 2G2 john.klassen@ualberta.ca.
John S
JS
Klassen
D001789:Blood Group Antigens / Q000737:chemistry* / Q000502:physiology; D036022:Capsid Proteins / Q000737:chemistry* / Q000276:immunology; D006801:Humans; D029322:Norovirus / Q000276:immunology*; D009844:Oligosaccharides / Q000737:chemistry; D011485:Protein Binding; D014771:Virion / Q000276:immunology
D001789:Blood Group Antigens; D036022:Capsid Proteins; D009844:Oligosaccharides
affinities; antigen; electrospray ionization mass spectrometry; norovirus