Submitted to: Letters in Applied Microbiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/1/2005
Publication Date: 7/1/2005
Citation: Tian, P., Brandl, M., Mandrell, R.E. 2005 Porcine stomach mucin binds to recombinant norovirus particles and competitively inhibits their binding to histo-blood group antigens and human intestine cells. Letters in Applied Microbiology.(41)315-320 Interpretive Summary: Farkas et al. (2005) recently reported the seroprevalence of NV in swine. 71% pig serum samples from the United States and 36% pig serum samples from Japan possessed antibodies against the swine norovirus SW918. More interesting, 63% of serum samples from pigs in the United States were positive for Norwalk virus (GGI) and 52% were positive for Hawaii virus (GGII). Their results indicated that NV infections are common among domestic pigs. The finding of seroprevalence of human NV in swine indicated it is possible that human NLV could enter into GI of swine and stimulate the immune response. Farkas et al also showed that the recombinant SW918 VLP did not bind to histo-blood group antigen (HBGA) in human saliva samples. However, it is not clear if human NV could bind to HBGAs from animal species. In this paper, we are testing if human NV could bind to HBGAs purified from porcine gastro-intestine (GI). We found that porcine gastric mucin (PGM) effectively binds to recombinant noroviral like particles (rNVLPs) and competitively inhibits their binding to human HBGA and human intestine cells. The present study is the first to identify the glycoprotein from an animal gastric mucosa could binds to human noroviruses and highlights the importance of further studies on NV infection as a possible zoonotic disease.
Technical Abstract: The saliva binding enzyme assays were used to determine the inhibition of PGM on rNVLP binding to HBGA. We found rNVLP to HBGA could be inhibited by PGM in a dose-depend pattern. The inhibition of binding of rNVLP to the HBGA could be observed in the presence of PGM as few as 2 ng per ml. rNVLP could be captured effectively by PGM coated on micro-titer plates and be detected by polyclonal antibodies against rNVLP. The binding of rNVLP to PGM could be inhibited effectively by HBGA in human saliva, Lewis b, Lewis d synthetic oligosaccharides, but not effectively by H3 HBGA, and not inhibited by mucin purified from bovine submaxillary glands. Pre-incubation of rNVLPs with PGM completed abolished their binding ability to human intestine cells.