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ARS Home » Pacific West Area » Albany, California » Western Regional Research Center » Produce Safety and Microbiology Research » Research » Publications at this Location » Publication #191449


item Tian, Peng
item Bates, Anne
item Mandrell, Robert

Submitted to: Letters in Applied Microbiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/24/2006
Publication Date: 12/1/2006
Citation: Tian, P., Bates, A.H., Jensen, H., Mandrell, R.E. 2006. Norovirus binds to blood group a-like antigens in oyster gastrointestinal cells. Letters in Applied Microbiology. 43:645-651

Interpretive Summary: It has been estimated that human noroviruses (NV) cause 23 million cases of gastrointestinal disease in the United States annually, accounting for 50 to 67% of food-borne illness (Glass et al. 2001). Outbreaks of NV gastroenteritis are often associated with consumption of oysters contaminated with NV. Oyster could concentrate viral particles during their feeding process. However, no specific receptor specific binding of virus has been identified for viral accumulation in oysters. It has been shown that histo-blood group antigens (HBGA) on cells of human gastrointestinal (GI) tract functions as receptors for NV and mediates the entry of virus into these cells. We are wondering if HBGA present in oyster GI cells and mediate accumulation of NV in these cells. By using monoclonal antibodies against HBGA, we demonstrated that all oysters tested contain HBGA. The oyster GI homogenate could capture recombinant Norwalk virus like particles (rNVLP) very effectively in vitro by ELISA assay and in vivo by immuno-staining. The binding on oyster GI cells is co-localized with type A HBGA. Conclusion: Type A HBGA are present in oyster GI cells and responsible for specific binding and accumulation of rNVLP.

Technical Abstract: A set of HBGA specific monoclonal antibodies (MAbs) was used to determine the presence of corresponding HBGA in oyster GI cells. rNVLPs were applied to plate coated with oyster stomach and digestive diverticular (OSD) homogenate, and measured by ELISA assay using polyclonal antibodies against NV. Co-localization of HBGA and rNVLP binding on oyster OSD cells were determined by immuno-staining and analyzed in three-channel confocal microscopy. Results: All oyster samples tested contained type A HBGA in GI tissue measured by ELISA. rNVLP bound to plates coated with oyster OSD homogenate. The binding was inhibited when rNVLPs were pre-incubated with MAbs to type A HBGA, or samples contain free HBGA such as saliva from type A or type O individuals or porcine gastric mucin (PGM) that contains both type A and type O HBGA. Co-localization of rNVLP and type A HBGA, but not type B or type O HBGA, on GI epithelial cells was observed by using immuno-staining under three-channel confocal microscopy.