Glycan recognition in globally dominant human rotaviruses

Hu, Liya; Sankaran, Banumathi; Laucirica, Daniel R.; Patil, Ketki; Salmen, Wilhelm; Ferreon, Allan Chris M.; Tsoi, Phoebe S.; Lasanajak, Yi; Smith, David F.; Ramani, Sasirekha; Atmar, Robert L.; Estes, Mary K.; Ferreon, Josephine C.; Prasad, B. V. Venkataram

doi:10.1038/s41467-018-05098-4

Cited by 70 publications

(95 citation statements)

References 64 publications

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“…Structural-based sequence alignment of P [19], P [6], P [4] and P [8] showed that they have high levels of amino acid conservation. From the recent crystallization studies, it was found that P [19], P [6], and P [4] employed the βα binding domain to accommodate H type 1 ligand LNFP I [35,36], which is in agreement with our NMR-driven HADDOCK results. Previous homology modeling results suggested that the addition of Lewis fucose via α1,4-linkage to the O4 atom of the GlcNAc residue could cause a binding clash if P [8] used the same binding interface as P[4] [36].…”

Section: Discussionsupporting

confidence: 88%

“…From the recent crystallization studies, it was found that P [19], P [6], and P [4] employed the βα binding domain to accommodate H type 1 ligand LNFP I [35,36], which is in agreement with our NMR-driven HADDOCK results. Previous homology modeling results suggested that the addition of Lewis fucose via α1,4-linkage to the O4 atom of the GlcNAc residue could cause a binding clash if P [8] used the same binding interface as P[4] [36]. Our structural studies presented here resolve this perceived conflict, showing that P [8] accommodates the Le b -containing ligands by shifting to a new binding site, namely the  binding domain.…”

Section: Discussionsupporting

confidence: 88%

“…P [19] RVs exhibit binding specificities to mucin core 2 and type 1 HBGA precursors, indicating that P [19] genotype may be positioned at an early evolutionary stage starting from a common P[I] ancestor. Recently, the apo crystal structure of porcine P [6] strain (z84) and human P [6] strain (RV3) have been reported, both demonstrating a galectin-like fold as reported for P [19] [36,46]. P [6] RVs are commonly found to infect animals (porcine), neonates and young infants [47,48].…”

Section: Our Data Also Provide Clues About the Evolution Of P[ii] Rvsmentioning

confidence: 84%

“…A significant advance in understanding the molecular basis of HBGA-VP8* interactions was achieved through nuclear magnetic resonance and crystallographic studies of P [19] binding to type 1 HBGA, which led to the discovery of a completely new glycan binding site composed of the N-terminal α-helix and the β-sheet containing βB, βI, βJ, βK stands [25,35]. During preparation of the manuscript, P [4] and P [6] VP8* were found to interact with H-type 1 HBGA using the same binding pocket formed by a β-sheet and the N-terminal α-helix [36].…”

Section: Introductionmentioning

confidence: 99%

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Molecular basis of P[6] and P[8] major human rotavirus VP8* domain interactions with histo-blood group antigens

Yang

Tan

et al. 2019

Preprint

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Initial cell attachment of rotavirus (RV) to specific cell surface glycans, which is the essential first step in RV infection, is mediated by the VP8* domain of the spike protein VP4. Recently, human histo-blood group antigens (HBGAs) have been identified as ligands or receptors for human RV strains. RV strains in the P[4] and P[8] genotypes of the P[II] genogroup share common recognition of the Lewis b and H type 1 antigens, while P[6], which is one of the other genotypes in P[II], only recognizes the H type 1 antigen. The molecular basis of receptor recognition by the major human P[8] RVs remains unknown due to lack of experimental structural information. Here, we used nuclear magnetic resonance (NMR) titration experiments and NMRderived high ambiguity driven docking (HADDOCK) methods to elucidate the molecular basis for P[8] VP8* recognition of the Le b and type 1 HBGAs and for P[6] recognition of H type 1 HBGAs. Unlike P[6] VP8* that recognizes H type 1 HGBAs in a binding surface composed of an α-helix and a β-sheet, referred as "βα binding domain", the P[8] VP8* binds the type 1 HBGAs requiring the presence of the Lewis epitope in a previously undescribed pocket formed by two β-sheets, referred as "β binding domain". The observation that P[6] and P[8] VP8* domains recognize different glycan structures at distinct binding sites supports the hypothesis that RV evolution is driven, at least in part, by selective pressure driven adaptation to HBGA structural diversity of their natural hosts living in the world. Recognition of the role that HBGAs play in driving RV evolution is essential to understanding RV diversity, host ranges, disease burden and zoonosis and to developing strategies to improve vaccines against RV infections.

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Section: Discussionsupporting

confidence: 88%

Section: Discussionsupporting

confidence: 88%

Section: Our Data Also Provide Clues About the Evolution Of P[ii] Rvsmentioning

confidence: 84%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Molecular basis of P[6] and P[8] major human rotavirus VP8* domain interactions with histo-blood group antigens

Yang

Tan

et al. 2019

Preprint

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“…P [19] genotype (a genotype that infects pigs and humans), belongs to the genogroup II and binds to the H antigen and to the mucin core 2 glycan 21 . In the same manner, P [4], P [6] and P [8] that also belong to the genogroup II, are able to recognize H type related antigens and the type I precursor 5,22 . Finally the P [11] genotype interacts with the H type II precursor molecule 18 .…”

Section: Discussionmentioning

confidence: 94%

Sero-epidemiological study of the rotavirus VP8* protein from different P genotypes in Valencia, Spain

Vila-Vicent

Gozalbo-Rovira

Rubio‐del‐Campo

et al. 2020

Sci Rep

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The aims of the present work were to determine the prevalence and titer of serum antibodies against several rotavirus VP8* proteins from different P genotypes in children and adults in Valencia, Spain; and to determine the role of the secretor status (FUT2 G428A polymorphism) in the antibody response. The VP8* protein from the P[4], P[6], P[8], P[9], P[11], P[14] and P[25] genotypes were produced in E. coli. These proteins were tested with 88 serum samples from children (n = 41, 3.5 years old in average) and from adults (n = 47, 58 years old in average) by ELISA. A subset of 55 samples were genotyped for the FUT2 G428A polymorphism and the antibody titers compared. The same subset of samples was also analysed by ELISA using whole rotavirus Wa particles (G1P[8]) as antigen. Ninety-three per cent of the samples were positive for at least one of the VP8* antigens. Differences in the IgG seroprevalence were found between children and adults for the P[4], P[8] and P[11] genotypes. Similarly, significant differences were found between adults and children in their antibody titers against the P[4], P[8], and P[11] VP8* genotypes, having the children higher antibody titers than adults. Interestingly, positive samples against rare genotypes such as P[11] (only in children), P[14] and P[25]were found. While no statistical differences in the antibody titers between secretors and non-secretors were found for any of the tested P genotypes studied, a higher statistic significant prevalence for the P[25] genotype was found in secretors compared to non-secretors. Significant differences in the antibody titers between secretors and non-secretors were found when the whole viral particles from the Wa rotavirus strain (G1P[8]) were used as the antigen.Rotaviruses are the leading etiologic agent of viral gastroenteritis in infants and young children worldwide 1 . Rotavirus contains segmented, double stranded RNA genome. The rotavirus protein VP7 makes up the outer capsid protein shell and VP4 forms the spikes that emanate through the outer capsid. VP7 is a glycoprotein that determines the G-type antigen while VP4 is a protease-sensitive protein that determines the P-type antigen 2 . The common rotavirus classification involves their genome composition and their serological reactivity, so the scientific community uses the VP7, VP4 and VP6 proteins to classify them. Rotaviruses are classified into 7 groups (A to G) based in the immunological reactivity of the VP6 (middle layer viral protein). Rotaviruses from the groups A to C have been isolated from humans but the most prevalent is the group A.The two outer capsid protein, VP7 and VP4, are used to classify rotavirus in G and P types (genotypes and/or serotypes). Nowadays we can count more than 36 different G-genotypes and 51 P-genotypes (https://rega.kuleuven.be/cev/viralmetagenomics/virus-classification/rcwg). The most prevalent genotypes in humans infections are G1P[8], G2P[4], G3P[8] and G4P [8]. More recently a classification using the eleven segments of the genome has been settled...

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Binding of Glycans to the SARS CoV‐2 Spike Protein, an Open Question: NMR Data on Binding Site Localization, Affinity, and Selectivity

Maass

Ssebyatika

Brückner

et al. 2022

Chemistry A European J

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We have used NMR experiments to explore binding of selected glycans and glycomimetics to the SARS CoV‑2 spike glycoprotein (S‑protein) and to its receptor binding domain (RBD). STD NMR experiments confirm binding of sialoglycans to the S‑protein of the prototypic Wuhan strain virus and yield dissociation constants in the mM range. The absence of STD effects for sialoglycans in the presence of the Omicron/BA.1 S‑protein reflects a loss of binding as a result of S‐protein evolution. Likewise, no STD effects are observed for the deletion mutant Δ 143‐145 of the Wuhan S‐protein, supporting localization of the binding site in the N‐terminal domain (NTD). The glycomimetics Oseltamivir and Zanamivir bind weakly to the S‑protein of both virus strains. Binding of blood group antigens to the Wuhan S‑protein cannot be confirmed by STD NMR. Using 1 H, 15 N TROSY HSQC based chemical shift perturbation (CSP) experiments we exclude binding of any of the ligands studied to the RBD of the Wuhan S‑protein. Our results put reported data on glycan binding into perspective and shed new light on the potential role of glycan‐binding to the S‐protein.

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Glycan recognition in globally dominant human rotaviruses

Cited by 70 publications

References 64 publications

Molecular basis of P[6] and P[8] major human rotavirus VP8* domain interactions with histo-blood group antigens

Molecular basis of P[6] and P[8] major human rotavirus VP8* domain interactions with histo-blood group antigens

Sero-epidemiological study of the rotavirus VP8* protein from different P genotypes in Valencia, Spain

Binding of Glycans to the SARS CoV‐2 Spike Protein, an Open Question: NMR Data on Binding Site Localization, Affinity, and Selectivity

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