Synthesis and Evaluation of Biotinylated Bivalent HistoBlood Group Antigens for Capturing Human Noroviruses

Dhawane, Abasaheb N.; Diez‐Valcarce, Marta; Gurale, Bharat P.; Dinh, Hieu; Vinjé, Jan; Iyer, Suri S.

doi:10.1021/acs.bioconjchem.6b00226

Cited by 4 publications

(5 citation statements)

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“…The biological significance and clinical importance of ABH antigens have ensured that their synthesis continues to be of significant interest for decades since the pioneering studies accomplished by Lemieux and co-workers in the 1970s . In the new millennium, many different approaches have been explored for the synthesis of ABH antigens, such as chemical synthesis, − chemoenzymatic synthesis, enzymatic synthesis, − and whole-cell fermentation . Despite the numerous synthetic approaches reported so far, the collective synthesis of all 15 naturally occurring ABH antigens has only been achieved through elegant chemical synthesis by Lowary and co-workers recently. − The non-natural type V ABH antigens were also chemically synthesized by the Lowary group …”

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confidence: 99%

Diversity-Oriented Enzymatic Modular Assembly of ABO Histo-blood Group Antigens

Liu

Peng

et al. 2016

ACS Catal.

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Enzymatic synthesis of all 15 naturally occurring human ABH antigens was achieved using a diversityoriented enzymatic modular assembly (EMA) strategy. Three enzyme modules were developed, each one-pot multienzyme module comprises a glycosyltransferase and one or two corresponding sugar nucleotide generating enzyme(s). These multienzyme cascade processes provide an efficient and convenient platform for collective synthesis of all 15 ABH antigens in three operationally simple steps from five readily available disaccharide acceptors and three simple free sugars as donor precursors.

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confidence: 99%

Diversity-Oriented Enzymatic Modular Assembly of ABO Histo-blood Group Antigens

Liu

Peng

et al. 2016

ACS Catal.

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“…1. The synthesis of the H type I and III have been reported previously, and the synthesis of A and B will be reported elsewhere 9 . To assess the contribution of matrix and subject effects on the binding of SMV to HBGA ligands, bead-binding assays were conducted using a well-described stool and emesis collection from a previous SMV human challenge study 10 .…”

Section: Resultsmentioning

confidence: 99%

“…Development of HBGA-based norovirus detection assays has been hindered by a lack of assay reliability which could not be explained. In a previous study, examination of stool specimens collected from norovirus outbreaks that had similar titers of the same virus strain yielded dramatically different results when tested by HBGA binding assays 9 . To better understand this variability, stool samples from an SMV human challenge study were used to assess matrix and subject effects on virus recovery by synthetic HBGAs.…”

Section: Discussionmentioning

confidence: 98%

“…Histo-blood group antigens H-type I, H-type III, A, and B were synthesized with polyethylene glycol (PEG) linkers and biotin moieties for conjugation to streptavidin beads. The synthetic process was previously described in detail 9 . Biotinylated PEG and biotinylated galactose were also synthesized and used as negative controls.…”

Section: Methodsmentioning

confidence: 99%

“…In this study, synthetic HBGAs were assessed for their capacity to recover native GII.2 Snow Mountain Virus (SMV) from stool samples from infected subjects in a human challenge study as a first step towards the development of glycan-based diagnostics. These synthetic carbohydrates have previously been shown to bind GI.1 Norwalk virus VLPs and native Norwalk virus 9 . SMV VLPs are known to bind to H-type I carbohydrates, but not other HBGAs, such has H-type III, A, B, or the Lewis antigens 5 .…”

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Snow Mountain Virus recovery by synthetic human histo-blood group antigens is heavily influenced by matrix effects

Kirby

Kienast

Aldeco

et al. 2020

Sci Rep

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Noroviruses are known to bind to histo-blood group antigens (HBGAs) and the specific binding patterns depend on the virus genotype. However, the development of point-of-care diagnostic assays based on this binding has been challenging due to low assay sensitivity. This study utilized a well-defined stool collection from a GII.2 Snow Mountain Virus (SMV) human challenge study to investigate virus recovery from stool and emesis samples using HBGA-coated beads. SMV was recovered from H type III-coated beads for 13 stool specimens out of 27 SMV-positive specimens tested. After adjusting for non-specific binding to PEG-coated beads, the mean percent recovery by H type III-coated beads was 308.11% +/− 861.61. Recovery by H type III ligands was subject-specific and weakly correlated with stool consistency. input virus titer was not correlated with SMV recovery. the results suggest that the generally low virus recovery we observed may be due to bead saturation or hindrance by existing glycans in the matrix that precluded the virus from being captured by the synthetic glycans. These results indicate a strong role for subject-specific and matrix effects in HBGA binding by SMV. Further investigation of the nature of this interference is needed to facilitate development of high sensitivity diagnostic assays.Noroviruses are a major cause of gastroenteritis worldwide in all age groups 1 . In the United States, it is estimated to cause 58% of all foodborne illnesses 2 . The illness is generally limited and resolves without medical intervention, however, severe outcomes and deaths do occur 3 . Three norovirus genogroups are known to cause illness in humans: GI, GII, and GIV. GII viruses are the most common, specifically GII.4, which is the genotype responsible for cyclic norovirus pandemics 4 . In vitro studies have shown that noroviruses bind to histo-blood group antigens (HBGAs), which comprise the ABO, Lewis, and secretor phenotypes 5 . HBGAs are thought to be the primary receptors for the virus, and the pattern of binding to specific HBGAs varies by genotype.In clinical practice, norovirus illness is generally diagnosed without a laboratory test due to the lack of clinically useful diagnostics 6 . The gold standard diagnostic is reverse transcription-polymerase chain reaction (RT-PCR), which detects the viral RNA. For accurate genotype identification, RT-PCR is followed by amplicon sequencing. While RT-PCR is sensitive and specific, the fairly long turnaround time limits its utility for an illness where duration is measured in hours. Other antibody-based diagnostics are available, but their sensitivities are much lower than RT-PCR. Currently, there exists an unmet need to develop point of care diagnostics to detect norovirus in a variety of settings as early detection and isolation of the infected person would decrease the spread of the virus.Until recently, noroviruses could not be cultured in the laboratory 7 , which limited diagnostic development to the use of recombinant capsid protein that formed virus-like particles (V...

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Synthesis and Evaluation of Biotinylated Bivalent HistoBlood Group Antigens for Capturing Human Noroviruses

Dhawane

Diez‐Valcarce²,

Gurale

et al. 2018

The FASEB Journal

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Glycosylation reactions were performed under argon with solvents dried using a solvent purification system Innovative Technology. All chemical reagents were of analytical grade, used as supplied without further purification unless indicated. The acidic ion exchange resin used was Amberlite ® IR 120 (H + ) resin. Analytical thin layer chromatography (TLC) was performed on silica gel 230-400 mesh (Sicicycle). Plates were visualized under UV light, and/or by staining with acidic CeH8Mo3N2O12 followed by heating. Column chromatography was performed on silica gel (230-400 mesh). 1 H and 13 C NMR spectra were recorded on Bruker 400MHz spectrometer. Chemical shifts are reported in δ (ppm) units using 13 C and residual 1 H signals from deuterated solvents as references. Spectra were analyzed with MestreNova ® (Mestrelab Research). Electrospray ionization mass spectra were recorded on a Micromass Q \T 2 (Waters) and data were analyzed with MassLynx ® 4.0 (Waters) software. Reported yields refer to spectroscopically and chromatographically pure compounds that were dried under high vacuum (10 -2 mbar) before analytical characterization, unless otherwise specified.

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Synthesis and Evaluation of Biotinylated Bivalent HistoBlood Group Antigens for Capturing Human Noroviruses

Cited by 4 publications

References 34 publications

Diversity-Oriented Enzymatic Modular Assembly of ABO Histo-blood Group Antigens

Diversity-Oriented Enzymatic Modular Assembly of ABO Histo-blood Group Antigens

Snow Mountain Virus recovery by synthetic human histo-blood group antigens is heavily influenced by matrix effects

Synthesis and Evaluation of Biotinylated Bivalent HistoBlood Group Antigens for Capturing Human Noroviruses

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