Norovirus Capture with Histo-Blood Group Antigens Reveals Novel Virus-Ligand Interactions

Harrington, Patrick R.; Vinjé, Jan; Moe, Christine L.; Baric, Ralph S.

doi:10.1128/jvi.78.6.3035-3045.2004

Cited by 127 publications

(96 citation statements)

References 54 publications

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“…It was noted that all these binding activities were dose related but with a low OD value (below 1.0). In fact, the binding of HV to synthetic Le b also has been reported by others (6). Thus, we believe that these reactions are strain specific, not an artifact.…”

Section: Resultsmentioning

confidence: 60%

“…Strains MOH and BUDS have only one site for the A/B epitopes, and they bound to the A/B secretors only. Norwalk virus and C59 may recognize A but not B, while SMV may recognize B but not A (6). Similarly, in the Lewis binding group, Boxer may have a strong affinity to both Lewis and H epitopes and VA207 may have a strong affinity to the Lewis and a weak affinity to the H epitopes, while OIF recognizes only the Lewis epitope.…”

Section: Discussionmentioning

confidence: 99%

“…The binding specificity of noroviruses to HBGAs also has been suggested by a study using the recombinant capsid proteins expressed in Venezuelan equine encephalitis virus replicons, although fewer binding patterns with fewer strains of noroviruses were studied (5). Strain-specific binding of noroviruses to HBGAs has also been demonstrated using authentic virions in stool specimens of patients infected with noroviruses, and factors in human stools were found to be able to promote VLP binding of some strains to HBGAs (6).…”

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confidence: 95%

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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

Huang

Farkas

Zhong

et al. 2005

J Virol

373

465

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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-

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Section: Resultsmentioning

confidence: 60%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 95%

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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

Huang

Farkas

Zhong

et al. 2005

J Virol

373

465

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“…Whether strains of FCV associated with different types of disease use different receptors remains to be determined. In human noroviruses, different host expression of viral receptors belonging to the ABH histo-blood group family is associated with resistant to infection in some individuals [38,44,57]. Whether a similar mechanism operates for FCV is unknown although interestingly in the field, some cats do appear to be relatively resistant to infection despite between heavily exposed to challenge virus [14].…”

Section: Molecular Pathogenesismentioning

confidence: 99%

Feline calicivirus

et al. 2007

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-Feline calicivirus (FCV) is an important and highly prevalent pathogen of cats. It belongs to the family Caliciviridae which includes other significant pathogens of man and animals. As an RNA virus, high polymerase error rates convey upon FCV a high genome plasticity, and allow the virus to respond rapidly to environmental selection pressures. This makes the virus very adaptable and has important implications for clinical disease and its control. Being genetically diverse, FCV is associated with a range of clinical syndromes from inapparent infections to relatively mild oral and upper respiratory tract disease with or without acute lameness. More recently, highly virulent forms of the virus have emerged associated with a systemic infection that is frequently fatal. A proportion of FCV infected cats that recover from acute disease, remain persistently infected. In such cats, virus evolution is believed to help the virus to evade the host immune response. Such longterm carriers may only represent a minority of the feline population but are likely to be crucial to the epidemiology of the virus. Vaccination against FCV has been available for many years and has effectively reduced the incidence of clinical disease. However, the vaccines do not prevent infection and vaccinated cats can still become persistently infected. In addition, FCV strain variability means that not all strains are protected against equally. Much progress has been made in understanding the biology and pathogenesis of this important feline virus. Challenges for the future will necessarily focus on how to control the variability of this virus particularly in relation to emerging virulent strains and vaccination.

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“…Noroviruses recognize human histo-blood group antigens (HBGAs) as receptors, which are complex carbohydrates present on red blood cells and mucosal epithelium or as free antigens in biological fluids, such as saliva, milk, and intestinal contents (25,29). The recognition of HBGAs by noroviruses is strain specific, and eight distinct receptor-binding patterns have been identified (13,14,16,17,19,26). The linkage of norovirus binding to HBGAs with clinical infection has been demonstrated in human volunteer studies.…”

mentioning

confidence: 99%

The P Domain of Norovirus Capsid Protein Forms a Subviral Particle That Binds to Histo-Blood Group Antigen Receptors

Tan

Jiang

2005

J Virol

202

304

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Norovirus is the most important cause of nonbacterial acute gastroenteritis. We have shown previously that the isolated P domain containing the hinge forms a dimer and binds to histo-blood group antigen (HBGA) receptors with a low affinity (M. Tan, R. S. Hegde, and X. Jiang, J. Virol. 78:6233-6242, 2004). Here, we reported that the P domain of VA387 without the hinge forms a small particle with a significantly increased receptor binding affinity. An end-linked oligopeptide containing one or more cysteines promoted P-particle formation by forming intermolecular disulfide bridges. The binding sensitivity of the P particle to HBGAs was enhanced >700-fold compared to the P dimer, which was comparable to that of virus-like particles. The binding specificity of the P particle was further confirmed by strong binding to the Caco-2 cells, a human colon carcinoma cell line. This binding enhancement was observed in the P particles of both norovirus GI and GII strains. The P particle is estimated to contain 12 P dimers, in which the P2 subdomain builds up the outer layer, while the P1 subdomain forms the internal core. Taken together, our data indicate that the P domain is involved not only in dimerization but also in polymerization of the protein during the capsid assembling. The enhanced receptor binding of the P particle reflects the intrinsic feature of the viral capsid. The easy production of the P particle and its strong binding to HBGAs suggest that the P particle is useful in studying pathogenesis and morphogenesis of norovirus and candidates for antiviral or vaccine development.Norovirus, previously called Norwalk-like virus or small round structured virus, is the most important viral pathogen of epidemic acute gastroenteritis in both developed and developing countries (9, 10). Recent advances in understanding of norovirus-host interaction and the viral receptors have opened a new approach to study the host range and pathogenesis (18, 31). Noroviruses recognize human histo-blood group antigens (HBGAs) as receptors, which are complex carbohydrates present on red blood cells and mucosal epithelium or as free antigens in biological fluids, such as saliva, milk, and intestinal contents (25,29). The recognition of HBGAs by noroviruses is strain specific, and eight distinct receptor-binding patterns have been identified (13,14,16,17,19,26). The linkage of norovirus binding to HBGAs with clinical infection has been demonstrated in human volunteer studies. In the case of the prototype Norwalk virus (NV), for example, individuals of nonsecretors were naturally resistant to NV infection following the challenge (23). It seems logical to predict that each virus strain of the other binding patterns has its own host range defined by host blood type, although a recent human volunteer study of another norovirus, the Snow Mountain virus, did not reveal clear association between infection and host blood type (22).Norovirus belongs to the family Caliciviridae. It contains a positive-strand, polyadenylated RNA genome of ϳ7.7 kb that i...

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Norovirus Capture with Histo-Blood Group Antigens Reveals Novel Virus-Ligand Interactions

Cited by 127 publications

References 54 publications

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

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

Feline calicivirus

The P Domain of Norovirus Capsid Protein Forms a Subviral Particle That Binds to Histo-Blood Group Antigen Receptors

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