Journal
VIRUSES-BASEL
Volume 13, Issue 10, Pages -Publisher
MDPI
DOI: 10.3390/v13102066
Keywords
human noroviruses; histo-blood group antigens; glycoconjugates; human intestinal enteroids/organoids; structure; host-virus interactions
Categories
Funding
- Public Health Service grants from the National Institutes of Health, Texas Medical Center Digestive Diseases Center [P01 AI 057788, T32 AI 055413, P30 DK 056338]
- Agriculture and Food Research Initiative competitive grant from the USDA National Institute of Food and Agriculture [2011-68003-30395]
- Robert Welch Foundation [Q1279]
- Naman Family Fund for Basic Research at Baylor College of Medicine
- Swedish Research Council [2017-00955]
- CPRIT [RP150578, RP170719]
- [HHSN2722017000381]
- Swedish Research Council [2017-00955] Funding Source: Swedish Research Council
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Recognition of cell-surface glycans is crucial for virus attachment to host cells. Studies on HuNoVs show that HBGA glycan structures are important for infection, and the antibody-mediated neutralization mechanism has been explored. The use of novel culture systems has confirmed the necessity of fucosylated HBGAs for HuNoV infection.
Recognition of cell-surface glycans is an important step in the attachment of several viruses to susceptible host cells. The molecular basis of glycan interactions and their functional consequences are well studied for human norovirus (HuNoV), an important gastrointestinal pathogen. Histo-blood group antigens (HBGAs), a family of fucosylated carbohydrate structures that are present on the cell surface, are utilized by HuNoVs to initially bind to cells. In this review, we describe the discovery of HBGAs as genetic susceptibility factors for HuNoV infection and review biochemical and structural studies investigating HuNoV binding to different HBGA glycans. Recently, human intestinal enteroids (HIEs) were developed as a laboratory cultivation system for HuNoV. We review how the use of this novel culture system has confirmed that fucosylated HBGAs are necessary and sufficient for infection by several HuNoV strains, describe mechanisms of antibody-mediated neutralization of infection that involve blocking of HuNoV binding to HBGAs, and discuss the potential for using the HIE model to answer unresolved questions on viral interactions with HBGAs and other glycans.
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