Norovirus drug candidates that inhibit viral capsid attachment to human histo-blood group antigens

Ali, Eunüs S.; Rajapaksha, Harinda; Carr, Jillian M.; Petrovsky, Nikolai

doi:10.1016/j.antiviral.2016.07.006

Cited by 17 publications

(9 citation statements)

References 107 publications

(157 reference statements)

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“…Glycerol, tannic acid and panels of other molecules were identified with the purpose of disrupting norovirus binding ( Feng and Jiang, 2007 ; Zhang et al, 2012 ), and may have potential therapeutic application ( Table 1 ). However, discussion of therapeutics and antivirals for noroviruses is beyond the scope of this review, but interested readers are referred to other reviews ( Ali et al, 2016 ; Prasad et al, 2016 ; Deval et al, 2017 ).…”

Section: Simple Chemical Compounds That Bind Human Norovirusmentioning

confidence: 99%

Norovirus Binding to Ligands Beyond Histo-Blood Group Antigens

2017

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Histo-blood group antigens (HBGAs) are commonly accepted as the cellular receptors for human norovirus. However, some human noroviruses have been found not to bind any HBGA ligand, suggesting potential additional co-factors. Some ligands have been found to bind noroviruses and have the potential to be additional cellular receptors/attachment factors for human norovirus or inhibitors of the HBGA interaction. The studies identifying these mostly characterize different chemical, human, food, or bacterial components and their effect on norovirus binding and infection, although the mechanism of interaction is unknown in many cases. This review seeks to supplement the already well-covered HBGA-norovirus literature by covering non-HBGA human norovirus ligands and inhibitors to provide investigators with a more comprehensive view of norovirus ligands.

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Section: Simple Chemical Compounds That Bind Human Norovirusmentioning

confidence: 99%

Norovirus Binding to Ligands Beyond Histo-Blood Group Antigens

2017

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“…Since histo-blood group antigens (HBGA) have been shown to have close correlations with hNoV infection [ 7 , 8 ], the in vitro HBGA-binding block assay has been used in many studies to screen for anti-hNoV candidates [ 9 , 10 , 11 , 12 ]. As hNoV cultivation remains to be challenging, not many of the candidates have been further validated [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

Fucoidan But Not 2′-Fucosyllactose Inhibits Human Norovirus Replication in Zebrafish Larvae

Tan

Gorji

et al. 2021

Viruses

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Human noroviruses (hNoVs) cause heavy disease burden worldwide and there is no clinically approved vaccination or antiviral hitherto. In this study, with the use of a zebrafish larva in vivo platform, we investigated the anti-hNoV potentials of fucoidan (from brown algae Fucus vesiculosus) and 2′-Fucosyllactose (2′-FL). As a result, although both fucoidan and 2′-FL were able to block hNoV GII.4 virus-like particle (VLPs) from binding to type A saliva as expected, only fucoidan, but not 2′-FL, was able to inhibit the replication of hNoV GII.P16-GII.4 in zebrafish larvae, indicating the possible needs of higher molecular weights for fucosylated carbohydrates to exert anti-hNoV effect.

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“…Both viral and host factors can in principle serve as a launching pad for the discovery of anti-norovirus therapeutics [11–14,17–20]. Prominent viral targets that are particularly well-suited as targets for anti-noroviral drug development include the viral-encoded 3CL protease (3CLpro) and RNA dependent RNA polymerase (RdRp) because of the essential roles they play in viral replication [18].…”

Section: Introductionmentioning

confidence: 99%

Structure-based exploration and exploitation of the S4 subsite of norovirus 3CL protease in the design of potent and permeable inhibitors

Kankanamalage

Kim

Rathnayake

et al. 2017

European Journal of Medicinal Chemistry

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Human noroviruses are the primary cause of epidemic and sporadic acute gastroenteritis. The worldwide high morbidity and mortality associated with norovirus infections, particularly among the elderly, immunocompromised patients and children, constitute a serious public health concern. There are currently no approved human vaccines or norovirus-specific small-molecule therapeutics or prophylactics. Norovirus 3CL protease has recently emerged as a potential therapeutic target for the development of anti-norovirus agents. We hypothesized that the S4 subsite of the enzyme may provide an effective means of designing potent and cell permeable inhibitors of the enzyme. We report herein the structure-guided exploration and exploitation of the S4 subsite of norovirus 3CL protease in the design and synthesis of effective inhibitors of the protease.

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Norovirus drug candidates that inhibit viral capsid attachment to human histo-blood group antigens

Cited by 17 publications

References 107 publications

Norovirus Binding to Ligands Beyond Histo-Blood Group Antigens

Norovirus Binding to Ligands Beyond Histo-Blood Group Antigens

Fucoidan But Not 2′-Fucosyllactose Inhibits Human Norovirus Replication in Zebrafish Larvae

Structure-based exploration and exploitation of the S4 subsite of norovirus 3CL protease in the design of potent and permeable inhibitors

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