Inhibition of African swine fever virus in liquid and feed by medium-chain fatty acids and glycerol monolaurate.
African swine fever virus
Antiviral
Feed pathogen mitigation
MCFA
Medium-chain fatty acids
Monoglycerides
Journal
Journal of animal science and biotechnology
ISSN: 1674-9782
Titre abrégé: J Anim Sci Biotechnol
Pays: England
ID NLM: 101581293
Informations de publication
Date de publication:
08 Dec 2020
08 Dec 2020
Historique:
received:
07
06
2020
accepted:
08
10
2020
entrez:
9
12
2020
pubmed:
10
12
2020
medline:
10
12
2020
Statut:
epublish
Résumé
The ongoing African swine fever virus (ASFv) epidemic has had a major impact on pig production globally and biosecurity efforts to curb ASFv infectivity and transmission are a high priority. It has been recently identified that feed and feed ingredients, along with drinking water, can serve as transmission vehicles and might facilitate transboundary spread of ASFv. Thus, it is important to test the antiviral activity of regulatory compatible, antiviral feed additives that might inhibit ASFv infectivity in feed. One promising group of feed additive candidates includes medium-chain fatty acids (MCFA) and monoglyceride derivatives, which are known to disrupt the lipid membrane surrounding certain enveloped viruses and bacteria. The antiviral activities of selected MCFA, namely caprylic, capric, and lauric acids, and a related monoglyceride, glycerol monolaurate (GML), to inhibit ASFv in liquid and feed conditions were investigated and suitable compounds and inclusion rates were identified that might be useful for mitigating ASFv in feed environments. Antiviral assays showed that all tested MCFA and GML inhibit ASFv. GML was more potent than MCFA because it worked at a lower concentration and inhibited ASFv due to direct virucidal activity along with one or more other antiviral mechanisms. Dose-dependent feed experiments further showed that sufficiently high GML doses can significantly reduce ASFv infectivity in feed in a linear manner in periods as short as 30 min, as determined by infectious viral titer measurements. Enzyme-linked immunosorbent assay (ELISA) experiments revealed that GML treatment also hinders antibody recognition of the membrane-associated ASFv p72 structural protein, which likely relates to protein conformational changes arising from viral membrane disruption. Together, the findings in this study indicate that MCFA and GML inhibit ASFv in liquid conditions and that GML is also able to reduce ASFv infectivity in feed, which may help to curb disease transmission.
Sections du résumé
BACKGROUND
BACKGROUND
The ongoing African swine fever virus (ASFv) epidemic has had a major impact on pig production globally and biosecurity efforts to curb ASFv infectivity and transmission are a high priority. It has been recently identified that feed and feed ingredients, along with drinking water, can serve as transmission vehicles and might facilitate transboundary spread of ASFv. Thus, it is important to test the antiviral activity of regulatory compatible, antiviral feed additives that might inhibit ASFv infectivity in feed. One promising group of feed additive candidates includes medium-chain fatty acids (MCFA) and monoglyceride derivatives, which are known to disrupt the lipid membrane surrounding certain enveloped viruses and bacteria.
RESULTS
RESULTS
The antiviral activities of selected MCFA, namely caprylic, capric, and lauric acids, and a related monoglyceride, glycerol monolaurate (GML), to inhibit ASFv in liquid and feed conditions were investigated and suitable compounds and inclusion rates were identified that might be useful for mitigating ASFv in feed environments. Antiviral assays showed that all tested MCFA and GML inhibit ASFv. GML was more potent than MCFA because it worked at a lower concentration and inhibited ASFv due to direct virucidal activity along with one or more other antiviral mechanisms. Dose-dependent feed experiments further showed that sufficiently high GML doses can significantly reduce ASFv infectivity in feed in a linear manner in periods as short as 30 min, as determined by infectious viral titer measurements. Enzyme-linked immunosorbent assay (ELISA) experiments revealed that GML treatment also hinders antibody recognition of the membrane-associated ASFv p72 structural protein, which likely relates to protein conformational changes arising from viral membrane disruption.
CONCLUSION
CONCLUSIONS
Together, the findings in this study indicate that MCFA and GML inhibit ASFv in liquid conditions and that GML is also able to reduce ASFv infectivity in feed, which may help to curb disease transmission.
Identifiants
pubmed: 33292608
doi: 10.1186/s40104-020-00517-3
pii: 10.1186/s40104-020-00517-3
pmc: PMC7722453
doi:
Types de publication
Journal Article
Langues
eng
Pagination
114Références
Biosystems. 2020 Oct;196:104184
pubmed: 32531420
J Virol Methods. 2003 Jan;107(1):53-61
pubmed: 12445938
J Phys Chem Lett. 2020 Jul 2;11(13):4951-4957
pubmed: 32478524
Arch Virol. 1986;88(3-4):285-92
pubmed: 3707358
J Anim Sci. 2020 Jan 1;98(1):
pubmed: 31758795
Transbound Emerg Dis. 2020 Jul 2;:
pubmed: 32613713
Antiviral Res. 2019 Jul;167:78-82
pubmed: 30991087
Emerg Infect Dis. 2019 Jul;25(7):1433-1435
pubmed: 31075078
Viruses. 2017 May 10;9(5):
pubmed: 28489063
Vet Microbiol. 2016 Mar 15;185:15-9
pubmed: 26931386
PLoS One. 2015 Nov 30;10(11):e0142889
pubmed: 26618713
Antiviral Res. 2018 Aug;156:128-137
pubmed: 29940214
Transbound Emerg Dis. 2020 Jul;67(4):1472-1484
pubmed: 32150785
Antimicrob Agents Chemother. 1972 Jul;2(1):23-8
pubmed: 4670656
Virology. 1993 Oct;196(2):596-602
pubmed: 7690502
Int J Mol Sci. 2018 Apr 08;19(4):
pubmed: 29642500
Transl Anim Sci. 2020 Feb 27;4(2):txaa024
pubmed: 32705023
J Food Prot. 2016 Apr;79(4):672-6
pubmed: 27052874
Antiviral Res. 2019 May;165:34-41
pubmed: 30836106
Biochemistry. 2006 Feb 21;45(7):2387-97
pubmed: 16475828
Langmuir. 2018 Nov 13;34(45):13745-13753
pubmed: 30343569
Langmuir. 2019 Mar 5;35(9):3568-3575
pubmed: 30720282
Langmuir. 2015 Sep 22;31(37):10223-32
pubmed: 26325618
Science. 2019 Nov 1;366(6465):640-644
pubmed: 31624094
Vet J. 2018 Mar;233:41-48
pubmed: 29486878
BMC Vet Res. 2014 Aug 05;10:176
pubmed: 25091641
Antimicrob Agents Chemother. 1987 Jan;31(1):27-31
pubmed: 3032090
Front Vet Sci. 2019 Aug 22;6:273
pubmed: 31508430
BMC Vet Res. 2016 Mar 12;12:51
pubmed: 26968372
Virus Res. 2019 Sep;270:197669
pubmed: 31325472
mBio. 2020 May 5;11(3):
pubmed: 32371599
Molecules. 2016 Mar 03;21(3):305
pubmed: 26950108
J Virol. 1996 Aug;70(8):5689-94
pubmed: 8764090
Emerg Infect Dis. 2019 May;25(5):891-897
pubmed: 30761988
Nature. 2009 Apr 23;458(7241):1034-8
pubmed: 19262509
Virol J. 2015 Dec 22;12:193
pubmed: 26689811
Vet Rec. 2019 Jun 8;184(23):713
pubmed: 31175249
Transbound Emerg Dis. 2014 Oct;61(5):397-410
pubmed: 25098383
BMC Vet Res. 2014 Sep 25;10:220
pubmed: 25253192
Transl Anim Sci. 2019 Nov 29;4(2):txz179
pubmed: 32289114
PLoS One. 2018 Mar 20;13(3):e0194509
pubmed: 29558524
J Biol Chem. 2020 Jan 10;295(2):348-362
pubmed: 31757809
Virus Res. 2013 Apr;173(1):29-41
pubmed: 23059353
Cell Host Microbe. 2019 Dec 11;26(6):836-843.e3
pubmed: 31787524
Porcine Health Manag. 2015 Jul 9;1:9
pubmed: 28405416
Transbound Emerg Dis. 2020 Nov;67(6):2365-2371
pubmed: 32359207
PLoS One. 2019 Apr 11;14(4):e0215227
pubmed: 30973929
Vet Med Sci. 2020 Aug;6(3):527-534
pubmed: 31854118
J Anim Sci Biotechnol. 2020 Apr 23;11:44
pubmed: 32337029
Res Vet Sci. 2016 Apr;105:28-30
pubmed: 27033903
Transbound Emerg Dis. 2020 May;67(3):1101-1112
pubmed: 31995852