Mapping Broadly Reactive Norovirus Genogroup I and II Monoclonal Antibodies

Crawford, Sue E.; Ajami, Nadim J.; Parker, Tracy Dewese; Kitamoto, Noritoshi; Natori, Katsuro; Takeda, Naokazu; Tanaka, Tomoyuki; Kou, Baijun; Atmar, Robert L.; Estes, Mary K.

doi:10.1128/cvi.00520-14

Cited by 17 publications

(16 citation statements)

References 54 publications

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“…This explains why the same genotype can produce successive pandemics. Moreover, the HPA-PAb is able to recognize the GI.1 VLPs but not the GI.1 P particles, supporting the idea that the cross-reactive epitopes between the two NoV genogroups are present only in the shell domain of VP1, which is not present in the P particles (31,32).…”

Section: Discussionsupporting

confidence: 51%

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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Section: Discussionsupporting

confidence: 51%

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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“…NV23, NV37, and NV3 recognized all of the VLPs evaluated by direct ELISA (Table 4), and these MAbs were shown by Crawford et al (26) to compete with each other in competition ELISAs. However, neither NV3 nor NV37 recognized VLPs in suspension by capture ELISA or SPR analysis, suggesting that the epitope(s) recognized by these MAbs is distinct from that recognized by NV23.…”

Section: Discussionmentioning

confidence: 99%

“…In the current study, we further characterized a panel of NoVspecific MAbs, many of which recognize common or overlapping linear epitopes in the C-terminal P1 domain of the virus capsid (see the accompanying paper by Crawford et al [26]). Several of the MAbs were unable to recognize VLPs in suspension, such as when assayed by SPR analysis or capture ELISA.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Cross-Reactive Norovirus-Specific Monoclonal Antibodies

Kou¹,

Crawford²,

Ajami³

et al. 2014

Clin. Vaccine Immunol.

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“…Multiple studies have reported cross‐reactive mAbs that can recognize strains from GI, GII, or both GI and GII. Epitope mapping studies indicate that cross‐reactive mAbs primarily target the S domain and P1 subdomain …”

Section: Introductionmentioning

confidence: 99%

“…Epitope mapping studies indicate that cross-reactive mAbs primarily target the S domain and P1 subdomain. [12][13][14][15][16] In this study, we successfully produced GI.7 and GII.2 VLPs and identified a mAb that exhibited wide-spectrum binding activities by immunizing mice with NoV VLPs derived from eight different genotypes. The immunization protocol by using multiple VLPs was based on the facts that NoV vaccine consisting of more than one genotype can induce the production of HBGAs blocking antibodies targeting genotypes not included in the vaccines, suggesting broadened immune responses.…”

mentioning

confidence: 99%

Characterization of a Norovirus‐specific monoclonal antibody that exhibits wide spectrum binding activities

Zheng

Wang

Liu

et al. 2018

Journal of Medical Virology

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Noroviruses (NoVs) are increasingly recognized as the leading cause of acute non-bacterial gastroenteritis worldwide. To screen for NoV-specific monoclonal antibodies (mAbs) with wide spectrum binding activities that could be used for the development of NoV-related detection reagents, we immunized mice with a combination of virus like particles (VLPs) derived from eight different genotypes (two from genogroup I and six from genogroup II), of which two (GI.7 and GII.2) were newly produced VLPs. Indirect enzyme-linked immunosorbent assay (ELISA) confirmed that two mAbs (8D8 and 10B11) bound to all eight major capsid proteins (VP1) with varied binding abilities. Epitope mapping using short peptides covering the N-terminal half of GII.3 VP1 indicated that the binding site of mAb 8D8 was located between amino acid 31 and 60. Multiple amino acid sequence alignment of VP1 suggested that this site harbors conservative sequences across all genogroups. Indirect and sandwich ELISA indicated that mAb 8D8 was unable bind intact VLPs. In summary, we successfully produced GI.7 and GII.2 VLPs using recombinant baculovirus expression system and a cross-reactive mAb by immunizing mice with eight different VLPs that might be useful in the studying and detecting NoVs.

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Mapping Broadly Reactive Norovirus Genogroup I and II Monoclonal Antibodies

Cited by 17 publications

References 54 publications

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

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

Characterization of Cross-Reactive Norovirus-Specific Monoclonal Antibodies

Characterization of a Norovirus‐specific monoclonal antibody that exhibits wide spectrum binding activities

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