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Journal of Virology, June 2005, p. 6714-6722, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6714-6722.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Norovirus and Histo-Blood Group Antigens: Demonstration of a Wide Spectrum of Strain Specificities and Classification of Two Major Binding Groups among Multiple Binding Patterns

Pengwei Huang,1 Tibor Farkas,1,2 Weiming Zhong,1 Ming Tan,1 Scott Thornton,3 Ardythe L. Morrow,1,2 and Xi Jiang1,2*

Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center,1 University of Cincinnati College of Medicine, Cincinnati, Ohio,2 Navy Environmental and Preventive Medicine Unit 6, Pearl Harbor, Hawaii3

Received 24 September 2004/ Accepted 15 January 2005

Noroviruses, an important cause of acute gastroenteritis, have been found to recognize human histo-blood group antigens (HBGAs) as receptors. Four strain-specific binding patterns to HBGAs have been described in our previous report. In this study, we have extended the binding patterns to seven based on 14 noroviruses examined. The oligosaccharide-based assays revealed additional epitopes that were not detected by the saliva-based assays. The seven patterns have been classified into two groups according to their interactions with three major epitopes (A/B, H, and Lewis) of human HBGAs: the A/B-binding group and the Lewis-binding group. Strains in the A/B binding group recognize the A and/or B and H antigens, but not the Lewis antigens, while strains in the Lewis-binding group react only to the Lewis and/or H antigens. This classification also resulted in a model of the norovirus/HBGA interaction. Phylogenetic analyses showed that strains with identical or closely related binding patterns tend to be clustered, but strains in both binding group can be found in both genogroups I and II. Our results suggest that noroviruses have a wide spectrum of host range and that human HBGAs play an important role in norovirus evolution. The high polymorphism of the human HBGA system, the involvement of multiple epitopes, and the typical protein/carbohydrate interaction between norovirus VLPs and HBGAs provide an explanation for the virus-ligand binding diversities.

* Corresponding author. Mailing address: Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, 3333 Burnet Avenue, Cincinnati, OH 45229-3039. Phone: (513) 636-0119. Fax: (513) 636-7655. E-mail: Jason.Jiang{at}cchmc.org.

Journal of Virology, June 2005, p. 6714-6722, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6714-6722.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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