Molecular epidemiology of noroviruses associated with acute sporadic gastroenteritis in children: Global distribution of genogroups, genotypes and GII.4 variants

Tran, Thomas; Trainor, Eamonn; Nakagomi, Toyoko; Cunliffe, Nigel A.; Nakagomi, Osamu

doi:10.1016/j.jcv.2012.11.011

Cited by 236 publications

(173 citation statements)

References 126 publications

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“…In Brazil, GII.4 NoV is most frequently reported from emergency departments [5,6,29,30]. The presence of a variety of genotypes in Sergipe and the periodic shift of GII.4 variants (i.e., GII.4 New-Orleans_2009 and GII.4 Sydney_2012) reflects the emergence worldwide of GII.4 variants [29,[31][32][33][34][35][36], confirming that the NoV genotypes have a wide geographical distribution. The increased detection of GII.4 could be explained by GII.4 theoretically causing more severe disease than other genotypes [31,37], but GII.4 diarrhoea severity in our patients was similar to other genotypes and we do not have evidence of an increased severity.…”

Section: Discussionmentioning

confidence: 93%

Acute norovirus gastroenteritis in children in a highly rotavirus-vaccinated population in Northeast Brazil

Santos

Gurgel

Cavalcante

et al. 2017

Journal of Clinical Virology

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Running title: Norovirus diarrhoea in children in BrazilWord count: Abstract: 199. Manuscript: 2255. Highlights Gastroenteritis is one of the most important causes of morbidity and mortality in children.  Noroviruses are a leading cause of sporadic cases and outbreaks of acute gastroenteritis.  Norovirus annual detection rates increased over the study period.  The detection of norovirus was higher among young children. AbstractBackground: Gastroenteritis is one of the most important causes of morbidity and mortality

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Section: Discussionmentioning

confidence: 93%

Acute norovirus gastroenteritis in children in a highly rotavirus-vaccinated population in Northeast Brazil

Santos

Gurgel

Cavalcante

et al. 2017

Journal of Clinical Virology

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“…A study from Alberta, Canada, showed that GI NoVs were responsible for ϳ37% of all NoV infections from late 2012 to early 2013, with the majority being caused by GI.6 and GI. 7. This was an ϳ15-fold-higher prevalence than in 2010 (12).…”

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confidence: 79%

Structural Analysis of Determinants of Histo-Blood Group Antigen Binding Specificity in Genogroup I Noroviruses

Shanker

Czakó

Sankaran

et al. 2014

J Virol

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Human noroviruses (NoVs) cause acute epidemic gastroenteritis. Susceptibility to the majority of NoV infections is determined by genetically controlled secretor-dependent expression of histo-blood group antigens (HBGAs), which are also critical for NoV attachment to host cells. Human NoVs are classified into two major genogroups (genogroup I [GI] and GII), with each genogroup further divided into several genotypes. GII NoVs are more prevalent and exhibit periodic emergence of new variants, suggested to be driven by altered HBGA binding specificities and antigenic drift. Recent epidemiological studies show increased activity among GI NoVs, with some members showing the ability to bind nonsecretor HBGAs. NoVs bind HBGAs through the protruding (P) domain of the major capsid protein VP1. GI NoVs, similar to GII, exhibit significant sequence variations in the P domain; it is unclear how these variations affect HBGA binding specificities. To understand the determinants of possible strainspecific HBGA binding among GI NoVs, we determined the structure of the P domain of a GI.7 clinical isolate and compared it to the previously determined P domain structures of GI.1 and GI.2 strains. Our crystallographic studies revealed significant structural differences, particularly in the loop regions of the GI.7 P domain, altering its surface topography and electrostatic landscape and potentially indicating antigenic variation. The GI.7 strain bound to H-and A-type, Lewis secretor, and Lewis nonsecretor families of HBGAs, allowing us to further elucidate the structural determinants of nonsecretor HBGA binding among GI NoVs and to infer several contrasting and generalizable features of HBGA binding in the GI NoVs. IMPORTANCEHuman noroviruses (NoVs) cause acute epidemic gastroenteritis. Recent epidemiological studies have shown increased prevalence of genogroup I (GI) NoVs. Although secretor-positive status is strongly correlated with NoV infection, cases of NoV infection associated with secretor-negative individuals are reported. Biochemical studies have shown that GI NoVs exhibit genotypedependent binding to nonsecretor histo-blood group antigens (HBGAs). From our crystallographic studies of a GI.7 NoV, in comparison with previous studies on GI.1 and GI.2 NoVs, we show that genotypic differences translate to extensive structural changes in the loop regions that significantly alter the surface topography and electrostatic landscape of the P domain; these features may be indicative of antigenic variations contributing to serotypic differentiation in GI NoVs and also differential modulation of the HBGA binding characteristics. A significant finding is that the threshold length and the structure of one of the loops are critical determinants in the binding of GI NoVs to nonsecretor HBGAs.

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Section: Importancementioning

confidence: 99%

“…Nevertheless, most human NoV infections are caused by genogroups GI and GII. Furthermore, in the last 2 decades, genotype GII.4 has been the causative agent of Ͼ95% of NoV gastroenteritis outbreaks, with globally distributed epidemic viral variants emerging every 2 to 3 years (11,12).NoVs are small nonenveloped viruses with a nonsegmented single-stranded positive-sense RNA genome, which encodes the viral structural and nonstructural proteins in three open reading frames (ORFs). ORF1 encodes the six nonstructural proteins, including the viral protease and the RNA-dependent RNA polymerase (RdRp), while ORF3 encodes a small basic protein, VP2, which interacts with VP1 and stabilizes the virion (13).…”

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confidence: 99%

“…The P domain can be further divided into two subdomains, P1 and P2 (14). The P1 subdomain forms the anchoring portion of the P dimer, connecting it to the S domain and promoting the stability of the viral particle, while the P2 subdomain is exposed on the surface of the capsid protein and is the most variable region of the virus (11). Both the main epitopes for immunorecognition and the histo-blood group antigen (HBGA) binding domains reside within this P2 subdomain.…”

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confidence: 99%

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Characterization of a Novel Conformational GII.4 Norovirus Epitope: Implications for Norovirus-Host Interactions

Carmona-Vicente

Vila-Vicent

Allen

et al. 2016

J Virol

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Human noroviruses (NoVs) are the main etiological agents of acute gastroenteritis worldwide. While NoVs are highly diverse (more than 30 genotypes have been detected in humans), during the last 40 years most outbreaks and epidemics have been caused by GII.4 genotype strains, raising questions about their persistence in the population. Among other potential explanations, immune evasion is considered to be a main driver of their success. In order to study antibody recognition and evasion in detail, we analyzed a conformational epitope recognized by a monoclonal antibody (3C3G3) by phage display, site-directed mutagenesis, and surface plasmon resonance. Our results show that the predicted epitope is composed of 11 amino acids within the P domain: P245, E247, I389, Q390, R397, R435, G443, Y444, P445, N446, and D448. Only two of them, R397 and D448, differ from the homologous variant (GII.4 Den-Haag_2006b) and from a previous variant (GII.4 VA387_1996) that is not recognized by the antibody. A double mutant derived from the VA387_1996 variant containing both changes, Q396R and N447D, is recognized by the 3C3G3 monoclonal antibody, confirming the participation of the two sites in the epitope recognized by the antibody. Furthermore, a single change, Q396R, is able to modify the histo-blood group antigen (HBGA) recognition pattern. These results provide evidence that the epitope recognized by the 3C3G3 antibody is involved in the virus-host interactions, both at the immunological and at the receptor levels. IMPORTANCEHuman noroviruses are the main cause of viral diarrhea worldwide in people of all ages. Noroviruses can infect individuals who had been previously exposed to the same or different norovirus genotypes. Norovirus genotype GII.4 has been reported to be most prevalent during the last 40 years. In the present study, we describe a novel viral epitope identified by a monoclonal antibody and located within the highly diverse P domain of the capsid protein. The evolution of this epitope along with sequential GII.4 variants has allowed noroviruses to evade previously elicited antibodies, thus explaining how the GII.4 genotype can persist over long periods, reinfecting the population. Our results also show that the epitope participates in the recognition of host receptors that have evolved over time, as well. N oroviruses (NoVs) are the predominant etiological agents of acute gastroenteritis worldwide, causing both outbreaks and sporadic cases (1-3). In many countries, NoVs have become the main cause of infantile gastroenteritis since the introduction of rotavirus vaccines (4-7), and they have also been recognized globally as the main cause of associated foodborne diseases (8,9).NoVs belong to the family Caliciviridae, and currently, they are classified into 6 genogroups (GI to GVI) (10) subdivided into more than 30 genotypes based on the capsid protein sequence diversity. Nevertheless, most human NoV infections are caused by genogroups GI and GII. Furthermore, in the last 2 decades, genotype GII.4 has been th...

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Molecular epidemiology of noroviruses associated with acute sporadic gastroenteritis in children: Global distribution of genogroups, genotypes and GII.4 variants

Cited by 236 publications

References 126 publications

Acute norovirus gastroenteritis in children in a highly rotavirus-vaccinated population in Northeast Brazil

Acute norovirus gastroenteritis in children in a highly rotavirus-vaccinated population in Northeast Brazil

Structural Analysis of Determinants of Histo-Blood Group Antigen Binding Specificity in Genogroup I Noroviruses

Characterization of a Novel Conformational GII.4 Norovirus Epitope: Implications for Norovirus-Host Interactions

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