Abstract
Foot-and-mouth disease (FMD), an acute, violent, infectious disease of cloven-hoofed animals, remains widespread in most parts of the world. It can lead to a major plague of livestock and an economical catastrophe. Structural studies of FMD virus (FMDV) have greatly contributed to our understanding of the virus life cycle and provided new horizons for the control and eradication of FMDV. To examine host-FMDV interactions and viral pathogenesis from a structural perspective, the structures of viral structural and non-structural proteins are reviewed in the context of their relevance for virus assembly and dissociation, formation of capsid-like particles and virus-receptor complexes, and viral penetration and uncoating. Moreover, possibilities for devising novel antiviral treatments are discussed.
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Abbreviations
- FMDV:
-
Foot-and-mouth disease virus
- UTR:
-
Untranslated region
- ORF:
-
Open reading frame
- HS:
-
Heparan sulfate
- CTE:
-
C-terminal extension
- HRV:
-
Human rhinovirus
- RTP:
-
Ribavirin triphosphate
- PK:
-
Pseudoknot
- cre :
-
Cis-acting element replication element
- IRES:
-
Internal ribosome entry site
- HSPGs:
-
Heparan sulfate proteoglycans
- ICAM-1:
-
Intercellular adhesion molecule 1
- MIDAS:
-
Metal ion-dependent adsorption site
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Acknowledgments
This research was supported by grants from the National Science and Technology Support Program (2013BAD12B00), International Science & Technology Cooperation Program of China (2014DFA31890), the Fundamental Research Funds for the Chinese Academy of Agricultural Sciences (2013ZL035), Gansu Provincial Sci. & Tech. Department (No. 1102NKDA033; No. 1102NKDA034; No. 1104WCGA185), and National Natural Science Foundation of China (No. 31100688; No. 31101838).
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The authors declare that they have no competing interest.
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Han, SC., Guo, HC. & Sun, SQ. Three-dimensional structure of foot-and-mouth disease virus and its biological functions. Arch Virol 160, 1–16 (2015). https://doi.org/10.1007/s00705-014-2278-x
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DOI: https://doi.org/10.1007/s00705-014-2278-x