The Asian Lineage of Zika Virus: Transmission and Evolution in Asia and the Americas

Hu, Tao; Li, Juan; Carr, Michael J.; Duchêne, Sebastián; Shi, Weifeng

doi:10.1007/s12250-018-0078-2

Cited by 32 publications

(31 citation statements)

References 54 publications

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“…P [8] showed that they have high levels of amino acid conservation. From the recent X-ray crystallography studies, it was found that P [19], P [6], P [4], P [8] employed the βα binding site to accommodate H type 1 ligand LNFP I [35,36,39], which is consistent 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 PLOS PATHOGENS [8] used the same binding interface as P [4]/P [6]/P [19] [36].…”

Section: Plos Pathogenssupporting

confidence: 88%

“…W81 in the βB strand, W174 in the βJ strand, T184 and T185 in the βK strand, R209 in the βm-αA loop, and E212 in the αA helix (Fig 9 and Fig 10). These highly conserved key residues in the P[II] genogroup are consistent with the crystal structures showing that P[4]/P [6]/P [8]/P [19] in the P[II] genotype can bind the Lewis negative type 1 HBGAs in the βα site [35,36,38,39] (Fig 10A, 10B, 10C, 10D and 10E). On the other hand,…”

Section: Structural Conservation and Variations Within The Vp8 � Glycsupporting

confidence: 84%

“…Recently, the structural basis of human rotavirus P [8] in recognizing the H type 1 antigen (Fuc-α1,2-Gal-β1,3-GlcNAc) and its precursor lacto-N-biose (Gal-β1,3-GlcNAc) has been characterized by Gozalbo-Rovira et al [38], and lacto-N-fucopentaose 1 (Fucα1-2Galβ1-3GlcNAcβ1-3Galβ1-4Glc) by Sun et al [39]. Both groups demonstrated that different P [8] strains have different binding affinity to H type 1 antigen [38,39], indicating that the subtle amino acid changes within and outside the defined binding pocket between different P[8] VP8 � strains may explain their different affinities to HBGAs. In an attempt resolve the contradictory results concerning P[8] VP8 � recognition of Le b antigens, we used STD-based NMR experiments and HSQC-based NMR titration experiments to study the RV VP8 � -ligand interactions.…”

Section: Discussionmentioning

confidence: 99%

“…The crystal structure of an apo form of P [8] human RV (Wa-like) has been reported previously [37], and the crystal structures of P [8] in complex with the type 1 precursor and the H type 1 trisaccharide, as well as the P [8] in complex with LNFP I, have been reported recently [38,39]. However, structural data regarding P [8] recognition of Lewis b antigen is not currently available.…”

Section: Introductionmentioning

confidence: 97%

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Molecular basis of P[II] major human rotavirus VP8* domain recognition of histo-blood group antigens

Ahmed

Stuckert

et al. 2020

PLoS Pathog

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Initial cell attachment of rotavirus (RV) to specific cell surface glycan receptors, 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 receptors or attachment factors 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 (Le b) and H type 1 antigens, however, 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) spectroscopy-based titration experiments and NMR-derived high ambiguity driven docking (HADDOCK) methods to elucidate the molecular basis for P[8] VP8* recognition of the Le b (LNDFH I) and type 1 HBGAs. We also used X-ray crystallography to determine the molecular details underlying P[6] recognition of H type 1 HBGAs. Unlike P[6]/ P[19] VP8*s that recognize H type 1 HBGAs in a binding surface composed of an α-helix and a β-sheet, referred as the "βα binding site", the P[8] and P[4] VP8*s bind Le b HBGAs in a previously undescribed pocket formed by the edges of two β-sheets, referred to as the "ββ binding site". Importantly, the P[8] and P[4] VP8*s retain binding capability to non-Le b type 1 HBGAs using the βα binding site. The presence of two distinct binding sites for Le b and non-Le b HBGA glycans in the P[8] and P[4] VP8* domains suggests host-pathogen co-evolution under structural and functional adaptation of RV pathogens to host glycan polymorphisms. Assessment and understanding of the precise impact of this co-evolutionary process in determining RV host ranges and cross-species RV transmission should facilitate improved RV vaccine development and prediction of future RV strain emergence and epidemics.

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Section: Plos Pathogenssupporting

confidence: 88%

Section: Structural Conservation and Variations Within The Vp8 � Glycsupporting

confidence: 84%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

See 2 more Smart Citations

Molecular basis of P[II] major human rotavirus VP8* domain recognition of histo-blood group antigens

Ahmed

Stuckert

et al. 2020

PLoS Pathog

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“…Over the last decade the world has seen the emergence and re-emergence of a number of lethal viral infections, including the Zika virus [2], Ebola [3], Influenza and Middle East Respiratory Syndrome (MERS) [4,5]. It has been noted that the frequency of emergence of new pathogens is increasing, notably in relation to population density [6].…”

mentioning

confidence: 99%

Geography, global pandemics & air travel: Faster, fuller, further & more frequent

Houghton¹

2019

Journal of Infection and Public Health

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Characterization and phylogenetic analysis of a neurovirulent Zika virus isolated from Cambodia in 2019

Zhang

Guo

Yang

et al. 2022

Journal of Medical Virology

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The geographic range of Zika virus (ZIKV) has expanded from Asia to the Americas, leading to the 2015–2016 pandemic with enhanced neurovirulence. At present, ZIKV is continuously circulating in many Southeast Asian countries. Unfortunately, the persistent evolution of ZIKV in Southeast Asia and its influence on the biological characteristics of the virus remain incompletely understood. In this study, the in vitro and in vivo properties of a new ZIKV isolate obtained from Cambodia in 2019 (CAM/2019) were characterized and compared with those of the Cambodian strain (CAM/2010). Compared with CAM/2010, the CAM/2019 virus showed similar plaque morphology and growth curves in cell cultures and induced comparable viremia and organ viral loads profiles in both BALB/c and A129 (IFNAR1−/−) mice upon intraperitoneal (i.p.) inoculation. Remarkably, the CAM/2019 virus exhibited enhanced neurovirulence in neonatal mice compared with CAM/2010, with a 74‐fold reduction in the 50% lethal dose (LD50). Consistently, CAM/2019 produced higher viral loads in the brains of BALB/c neonatal mice than CAM/2010 did. Sequence alignment showed that the CAM/2019 virus has acquired 12 amino acid substitutions, several of which were found to be associated with neurovirulence. In particular, the CAM/2019 virus shared an A1204T substitution in NS2A with the Thai isolate SI‐BKK02 that was isolated from a microcephaly case. Taken together, our results indicate that a ZIKV strain isolated with specific mutations has emerged in Cambodia, highlighting the need for extensive molecular and disease surveillance in Cambodia and other Asian countries.

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The Asian Lineage of Zika Virus: Transmission and Evolution in Asia and the Americas

Cited by 32 publications

References 54 publications

Molecular basis of P[II] major human rotavirus VP8* domain recognition of histo-blood group antigens

Molecular basis of P[II] major human rotavirus VP8* domain recognition of histo-blood group antigens

Geography, global pandemics & air travel: Faster, fuller, further & more frequent

Characterization and phylogenetic analysis of a neurovirulent Zika virus isolated from Cambodia in 2019

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