Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021 Jul 5;13(7):1307.
doi: 10.3390/v13071307.

Antivirals against the Chikungunya Virus

Affiliations
Review

Antivirals against the Chikungunya Virus

Verena Battisti et al. Viruses. .

Abstract

Chikungunya virus (CHIKV) is a mosquito-transmitted alphavirus that has re-emerged in recent decades, causing large-scale epidemics in many parts of the world. CHIKV infection leads to a febrile disease known as chikungunya fever (CHIKF), which is characterised by severe joint pain and myalgia. As many patients develop a painful chronic stage and neither antiviral drugs nor vaccines are available, the development of a potent CHIKV inhibiting drug is crucial for CHIKF treatment. A comprehensive summary of current antiviral research and development of small-molecule inhibitor against CHIKV is presented in this review. We highlight different approaches used for the identification of such compounds and further discuss the identification and application of promising viral and host targets.

Keywords: Chikungunya virus; alphavirus; antiviral drug development; antiviral therapy; direct-acting antivirals; host-directed antivirals; in silico screening; in vivo validation.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Chemical structure of virus-targeting compounds. Inhibitors of viral entry and membrane fusion: arbidol, IIc, suramin, epigallocatechin gallate, bis(benzofuran-thiazolidone) 3g, and LQM334. Inhibitor of the viral capsid protease: picolinic acid, mandelic acid, ethyl 3-aminobenzoate, P1, P4-di(adenosine-5′) tetraphosphate, eptifibatide acetate, and paromomycin sulphate. Inhibitor of 6K Protein: amantadine.
Figure 2
Figure 2
Chemical structure of virus-targeting compounds. Inhibitors of nsP1: MADTP, CHVB, lobaric acid, 6′-β-fluoro-homoaristeromycin, 6′-fluoro-homoneplanocin A, and 5-iodotubercidin. Inhibitor of nsP2: compound 25, compound 8, MBZM-N-IBT, MIBT, thiazolidin-4-one, ID1452-2, telmisartan, novobiocin, and nelfinavir. Inhibitor of nsP4: favipiravir, β-D-N4-Hydroxycytidine, sofosbuvir, and compound-A.
Figure 3
Figure 3
Chemical structure of selected host-targeting compounds. Inhibitor of the viral entry and membrane fusion: chloroquine, hydroxychloroquine, obatoclax, niclosamide, nitazoxanide, and 5-(N-ethyl-N-isopropyl)amiloride. Inhibitor of the lipid pathway: orlistat, cerulenin, CAY10566, tivozanib, pimozide, 5-tetradecyloxy-2-furoic acid, imipramine, U18999A, and LXR-623. Inhibitor of the pyrimidine and purine synthesis: ribavirin, merimepodip, mycophenolic acid, 6-azauridine, DD264, antimycin A1a, RYL-634, and atovaquone.
Figure 4
Figure 4
Chemical structure of selected host-targeting compounds. Inhibitor of the protein synthesis: halofuginone, harringtonine, sorafenib, sylvestrol, bortezomib, and SR9009. Inhibitor of cellular proteins: tenovin-1, sodium phenylbutyrate, sirtinol, geldanamycin, HS-10, SNX-2112, HA15, 16F16, PACMA31, and auranofin. Inhibitor of cellular enzymes: amodiaquine, desethyl-amodiaquine, aristeromycin, dasatinib, Torin 1, CND3514, berberine, miltefosine, prostatin, isothiazolo[4,3-b]pyridine, difluoromethylornithine, and DENSpm.
Figure 5
Figure 5
Chemical structure of selected host-targeting compounds. Inhibitors of cellular receptors: oubain, digoxin, lanatoside C, DIDS, 9-ACA, NPPB, 5-nonyloxytryptamine, and methiothepin mesylate. Immunomodulatory agents: tilorone, C11, G10, and AV-C.
Figure 6
Figure 6
Chemical structure of anti-CHIKV compounds without known target.

References

    1. Robinson M.C. An epidemic of virus disease in Southern Province, Tanganyika Territory, in 1952-53. I. Clinical features. Trans. R. Soc. Trop. Med. Hyg. 1955;49:28–32. doi: 10.1016/0035-9203(55)90080-8. - DOI - PubMed
    1. Chretien J.P., Anyamba A., Bedno S.A., Breiman R.F., Sang R., Sergon K., Powers A.M., Onyango C.O., Small J., Tucker C.J., et al. Drought-associated chikungunya emergence along coastal East Africa. Am. J. Trop. Med. Hyg. 2007;76:405–407. doi: 10.4269/ajtmh.2007.76.405. - DOI - PubMed
    1. Vazeille M., Moutailler S., Coudrier D., Rousseaux C., Khun H., Huerre M., Thiria J., Bastien Dehecq J.-S., Fontenille D., Schuffenecker I., et al. Two Chikungunya Isolates from Two Chikungunya Isolates from the Outbreak of La Reunion (Indian Ocean) Exhibit Different Patterns of Infection in the Mosquito, Aedes albopictus. PLoS ONE. 2007;2:e1168. doi: 10.1371/journal.pone.0001168. - DOI - PMC - PubMed
    1. Cassadou S., Boucau S., Petit-Sinturel M., Huc P., Leparc-Goffart I., Ledrans M. Emergence of chikungunya fever on the French side of Saint Martin island, October to December 2013. Eurosurveillance. 2014;19:20752. doi: 10.2807/1560-7917.ES2014.19.13.20752. - DOI - PubMed
    1. Zeller H., Van Bortel W., Sudre B. Chikungunya: Its History in Africa and Asia and Its Spread to New Regions in 2013–2014. J. Infect. Dis. 2015;214:436–440. doi: 10.1093/infdis/jiw391. - DOI - PubMed

Publication types

Substances