Antiviral Activity of Carbobenzoxy Di- and Tripeptides on Measles Virus

Miller, F. A.; Dixon, Glen J.; Arnett, G.; Dice, J. R.; Rightsel, Wilton A.; Schabel, Frank M.; McLean, Ian W.

doi:10.1128/am.16.10.1489-1496.1968

Cited by 12 publications

(3 citation statements)

References 14 publications

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“…Chlorine dioxide and sodium hypochloride [80] Anti-mycoplasmal and anti-microbial peptides 2 -Amino-2 -Deoxyribofuranosyl Adenine (2-AA) [81] Mucroporin (optimized/attenuated) [82] Interferons IFNα [37] Others Inhibitors of cholesterol synthesis (W-7, cerulenin, mevinolin, miconazole, ketoconazole) [55] Carbobenzoxy-(di-or tri-) peptides [83] PPMO (anti-mRNA) [84] Pyrazino-Pyrazine derivate [85] PCG [86] ViroSAL (emulsion of short-chain caprylic acid) [87] Isoprinosine (inosine derivate) [88] Next to the viral polymerase, an important protein in the MV lifecycle is the fusion protein. The fusion of enveloped viruses with the host cell is a key step in their infectivity, and interference with this process can lead to highly effective antivirals.…”

Section: Disinfectantmentioning

confidence: 99%

“…Vero [36,37,40,59,65,68,73,74,77,88] Vero E6 [38] CV-1 [34,46] Vero-humanSLAM [48,57,59,65,80,99] CHO/SLAM [84] Hep-2 [76,83] B95a [47] BSC-1 [47] CK [85] MV Edmonston(-derived) Edmonston [46,47,59,65,73,80,[83][84][85] rMV-Edm [48] rMV-Edm-GFP [68] Schwarz [74] MV wild-type(-derived) MVi/Kansas.USA/43.00 [57,65] MVi/Alaska.USA/16.00 [48,99] MVi-Amsterdam.NET/49.97 [48] MVi/Ibadan.NIE/97/1 [48] CC [38] WTFb [47] Berkeley/83, Ibadan/97, Chicago1/89 [84] TN1994, Halonen, Bil, X-1108, SA, CC, Chicago-1 [46] Suguyama [36] Hep-2 adapted attenuated MeV …”

Section: Neutralization Assaymentioning

confidence: 99%

“…Vero [35,39,43,59,63,74,78,79] Vero E6 [82] Vero-humanSLAM [43,60,61,63] Hep-2 [83] HEL-R66 [81] MV Edmonston(-derived) Edmonston [39,43,74,79,[81][82][83] MV wild-type-derived Tanabe strain [78] Sugiyama [39] Toyoshima [39] rMV-IC323-eGFP [63] MV G954 [60,61] SSPE viruses Yamagata-1 [39,43,59] Hallé [35] (Chemiluminescent) complementationbased assay…”

Section: Sspe Virusesmentioning

confidence: 99%

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Repurposing an In Vitro Measles Virus Dissemination Assay for Screening of Antiviral Compounds

Schmitz

Lange

Gommers

et al. 2022

Viruses

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Measles virus (MV) is a highly contagious respiratory virus responsible for outbreaks associated with significant morbidity and mortality among children and young adults. Although safe and effective measles vaccines are available, the COVID-19 pandemic has resulted in vaccination coverage gaps that may lead to the resurgence of measles when restrictions are lifted. This puts individuals who cannot be vaccinated, such as young infants and immunocompromised individuals, at risk. Therapeutic interventions are complicated by the long incubation time of measles, resulting in a narrow treatment window. At present, the only available WHO-advised option is treatment with intravenous immunoglobulins, although this is not approved as standard of care. Antivirals against measles may contribute to intervention strategies to limit the impact of future outbreaks. Here, we review previously described antivirals and antiviral assays, evaluate the antiviral efficacy of a number of compounds to inhibit MV dissemination in vitro, and discuss potential application in specific target populations. We conclude that broadly reactive antivirals could strengthen existing intervention strategies to limit the impact of measles outbreaks.

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Section: Disinfectantmentioning

confidence: 99%

Section: Neutralization Assaymentioning

confidence: 99%

Section: Sspe Virusesmentioning

confidence: 99%

See 1 more Smart Citation

Repurposing an In Vitro Measles Virus Dissemination Assay for Screening of Antiviral Compounds

Schmitz

Lange

Gommers

et al. 2022

Viruses

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Inhibition of virus‐induced cell fusion by apolipoprotein A‐I and its amphipathic peptide analogs

Srinivas

Zheng

Owens

et al. 1991

J of Cellular Biochemistry

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Apolipoprotein A-I (apoA-I), the major protein component of serum high-density lipoproteins (HDL), was found to inhibit herpes simplex virus (HSV)-induced cell fusion at physiological (approximately 1 microM) concentrations, whereas HDL did not exert any inhibitory effect. Lipid-associating, synthetic amphipathic peptides corresponding to residues 1-33 (apoA-I[1-33]) or residues 66-120 (apoA-I[66-120]) of apoA-I, also inhibited HSV-induced cell fusion, whereas a peptide corresponding to residues 8-33 of apoA-I (apoA-I[8-33]), which fails to associate with lipids, did not exert any inhibitory effect. These results suggest that lipid binding may be a prerequisite for peptide-mediated fusion inhibition. Consistent with this idea, a series of lipid-binding 22-amino-acid-residue-long synthetic amphipathic peptides that correspond to the amphipathic helical domains of apoA-I (A-I consensus series), or 18-residue-long model amphipathic peptides (18A series), were found to exert variable levels of fusion-inhibitory activity. The extent of fusion-inhibitory activity did not correlate with hydrophobic moment, hydrophobicity of the nonpolar face, helix-forming ability, or lipid affinity of the different peptides. Peptides in which the nonpolar face was not interrupted by a charged residue displayed greater fusion-inhibitory activity. Also, the presence of positively charged residues at the polar-nonpolar interface was found to correlate with higher fusion-inhibitory activity.

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Membrane fusion-inhibiting peptides do not inhibit influenza virus fusion or the Ca(2+)-induced fusion of negatively charged vesicles.

Stegmann

1993

Journal of Biological Chemistry

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Antiviral Activity of Carbobenzoxy Di- and Tripeptides on Measles Virus

Cited by 12 publications

References 14 publications

Repurposing an In Vitro Measles Virus Dissemination Assay for Screening of Antiviral Compounds

Repurposing an In Vitro Measles Virus Dissemination Assay for Screening of Antiviral Compounds

Inhibition of virus‐induced cell fusion by apolipoprotein A‐I and its amphipathic peptide analogs

Membrane fusion-inhibiting peptides do not inhibit influenza virus fusion or the Ca(2+)-induced fusion of negatively charged vesicles.

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