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Table 10 Antiviral activity of propolis water, ethanol and hydroalcholic extracts (WE, EE and HAE, respectively) and isolated compounds

From: Propolis: An update on its chemistry and pharmacological applications

Extract/Compound

Concentration /Dose

Test system

Results/Mechanisms

References

WE and EE

0–120 pfu (%)

HSV-1 on RC-37 cells

Affects viral infection cycle

[294]

WE and EE

0.00005–0.005 pfu (%)

HSV-2 on cells RC-37

Inhibition of HSV-2 plaque formation (IC50 0.0005% and 0.0004%, respectively)

[295]

0.5% WE

_

Rat and rabbit infected with HSV-1

50% inhibition of HSV infection

[296]

Mexican EE

250 µg/mL

Canine distemper virus

Inhibition of the virus nucleoprotein gene expression

[297]

5% HAE

_

Influenza virus in mice

Prevents influenza viral proliferation

[298]

Brazilian EE

50–100 µg/mL

HRV-2, HRV-3, and HRV-4 in HeLa cells

Block virus entrance into the cells, avoiding virus destruction and replication

[299]

Galangin, kaempferol, quercetin

0.05–1.0 µM

HSV-1

Reduce the viral titer by 2log10

[300]

3-methyl-but-2- enyl caffeate

6.25, 12.5, 25 and 50 µg/mL

HSV-1

Reduce the viral titer by 3log10 and viral DNA synthesis by 32-fold

[301]

CAPE

5 µM

HTLV-1

Inhibits NF-kB activation during in vitro infection

[454]

Green propolis EE

5 mg

Suid herpesvirus type 1 (SuHV-1)

Increases humoral and cellular response in mice immunized with SuHV-1

[455]

Quercetin

5–25 µM

50 µM

1–50 µM

Rhinovirus (RV)

Hepatitis C virus (HCV)

Hepatitis B virus (HBV)

Inhibits rhinovirus replication in vitro and in vivo; Prevents up-regulation of diacylglycerol acyltransferase

(DGAT) required for HCV replication in vitro; Decreases heat shock proteins and HBV transcription levels in vitro

[456]

[457]

[458]

Caffeic acid

IC50 = 3.9 µM—100 mg/kg b.w. per os;

4 mM

IC50 = 7.2 and 8.5 µM on NA1 and NA2, respectively

HBV

Influenza A virus (IAV)

IAV

Inhibits HBV-DNA replication in vitro and in vivo; Inhibits replication IAV in vitro;

Inhibits IAV activity through

neuraminidases (NA) in vitro

[277]

[459]

[460]

Rutin

Binding energy -8.97 kcal/mol (in silico)

SARS-CoV-2

Inhibitory potential on ACE2

[302]

Anatolia propolis EE, hesperetin (HE), pinocembrin (PI), CAPE

IC50 = 0.57–1.14 µL, 16.88 mM, 29.53 mM, 79.09 mM; Binding energy to spike S1 protein: -7.28, -7.54, 7.17 respectively for HE, PI and CAPE

SARS-CoV-2

Binds spike S1 protein and ACE-2 receptor as both in vitro and

in silico studies

[303]

Optimized liposomal formula of propolis, rutin and CAPE

IC50 = 1.18 mM,

ICM score: -92.8 and -67.8 agaist 3CL protease; ICM score: -94.3 and -77.8 agaist S1 spike protein

SARS-CoV-2

Bind COVID-3CL protease and S1 spike protein; inhibit the viral replication

[304]

Glyasperin A and broussoflavonol F

Binding affinity -7.8 kcal/mol

SARS-CoV-2

Bind SARS-CoV-2 main protease

[305]

Withaferin-A, Withanone and CAPE

Binding affinity: -5.6, -4.3 and -6.20 kcal/mol, respectively

SARS-CoV-2

Bind transmembrane protease serine 2 (TMPRSS2) in molecular

docking studies

[306]

Withanone and CAPE

Binding affinity: -4.42 and -4.79 kcal/mol, respectively

SARS-CoV-2

Bind SARS-CoV-2 protease Mpro

[307]

3'-Methoxydaidzin (MD),

neoblavaisoflavone, methylophiopogonone A and genistin

Binding affinity: -7.7 for MD and -7.6 kcal/mol for other compounds against Mpro; -8.1, -8.2, -8.3, and -8.3 kcal/mol, respectively against spike protein S2

SARS-CoV-2

Bind main protease (Mpro) and spike protein subunit 2 (S2)

[308]

Glyasperin A, broussoflavonol F, sulabiroins A, (2S)-5,7-dihydroxy-4'-methoxy-8-prenylflavanone and isorhamnetin

Docking score of -10.8, -9.9, -9.5, -9.3 and -9.2 kcal/mol respectively

SARS-CoV-2

ACE-2 inhibitors

[309]

2,2-Dimethyl-8-prenylchromene, Artepillin C, 3-Prenyl cinnamic acid allyl ester, Isocupressic acid, 13C-symphyoreticulic acid, ellagic acid, syringic acid, caffeic acid phenethyl ester, p-coumaric acid, hesperetin, naringenin, kaempferol, quercetin, chrysin

Binding scores: -5.6—-7.8 kcal/mol against Mpro; -5.3—-6.4 kcal/mol against RdRp

SARS-CoV-2

Main protease (Mpro) and

RNA-dependent RNA polymerase (RdRp) enzymes

[310]