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Journal of Virology, January 2003, p. 405-415, Vol. 77, No. 1
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.1.405-415.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Norwalk Virus-Like Particle Hemagglutination by Binding to H Histo-Blood Group Antigens

Anne M. Hutson,1 Robert L. Atmar,1,2 Donald M. Marcus,2,3 and Mary K. Estes1,2*

Departments of Molecular Virology and Microbiology,1 Medicine,2 Immunology, Baylor College of Medicine, Houston, Texas 770303

Received 5 July 2002/ Accepted 24 September 2002

Noroviruses are a major cause of epidemic acute nonbacterial gastroenteritis worldwide. Here we report our discovery that recombinant Norwalk virus virus-like particles (rNV VLPs) agglutinate red blood cells (RBCs). Since histo-blood group antigens are expressed on gut mucosa as well as RBCs, we used rNV VLP hemagglutination (HA) as a model system for studying NV attachment to cells in order to help identify a potential NV receptor(s). rNV VLP HA is dependent on low temperature (4°C) and acidic pH. Of the 13 species of RBCs tested, rNV VLPs hemagglutinated only chimpanzee and human RBCs. The rNV VLPs hemagglutinated all human type O (11 of 11), A (9 of 9), and AB (4 of 4) RBCs; however, few human type B RBC samples (4 of 14) were hemagglutinated. HA with periodate- and neuraminidase-treated RBCs indicated that rNV VLP binding was carbohydrate dependent and did not require sialic acid. The rNV VLPs did not hemagglutinate Bombay RBCs (zero of seven) that lack H type 2 antigen, and an anti-H type 2 antibody inhibited rNV VLP HA of human type O RBCs. These data indicated that the H type 2 antigen functions as the rNV VLP HA receptor on human type O RBCs. The rNV VLP HA was also inhibited by rNV VLP-specific monoclonal antibody 8812, an antibody that inhibits VLP binding to Caco-2 cells. Convalescent-phase sera from NV-infected individuals showed increased rNV VLP HA inhibition titers compared to prechallenge sera. In carbohydrate binding assays, the rNV VLPs bound to synthetic Lewis d (Led), Leb, H type 2, and Ley antigens, and these antigens also inhibited rNV VLP HA of human type O RBCs. Overall, our results indicate that carbohydrate antigens in the gut are a previously unrecognized factor in NV pathogenesis.

* Corresponding author. Mailing address: Department of Molecular Virology & Microbiology, Baylor College of Medicine, One Baylor Plaza BCM-385, Houston, TX 77030. Phone: (713) 798-3585. Fax: (713) 798-3586. E-mail: mestes{at}bcm.tmc.edu.

Journal of Virology, January 2003, p. 405-415, Vol. 77, No. 1
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.1.405-415.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.





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