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Title: Foot-and-Mouth Disease (FMD) Virus 3C Protease Mutant L127P: Implications for FMD Vaccine Development

Journal Article · · Journal of Virology
DOI:https://doi.org/10.1128/jvi.00924-17· OSTI ID:1626072
 [1];  [2];  [2];  [3];  [4];  [3];  [3];  [5];  [4];  [6];  [5];  [5]
  1. US Dept. of Homeland Security (DHS), Greenport, NY (United States). Plum Island Animal Disease Center; Leidos, Inc., Greenport, NY (United States). Plum Island Animal Disease Center; Oak Ridge Inst. for Science and Education (ORISE), Oak Ridge, TN (United States). Plum Island Animal Disease Center Research Participation Program
  2. Leidos, Inc., Greenport, NY (United States). Plum Island Animal Disease Center; Oak Ridge Inst. for Science and Education (ORISE), Oak Ridge, TN (United States). Plum Island Animal Disease Center Research Participation Program
  3. Leidos, Inc., Greenport, NY (United States). Plum Island Animal Disease Center
  4. Oak Ridge Inst. for Science and Education (ORISE), Oak Ridge, TN (United States). Plum Island Animal Disease Center Research Participation Program
  5. US Dept. of Homeland Security (DHS), Greenport, NY (United States). Plum Island Animal Disease Center;
  6. Leidos, Inc., Greenport, NY (United States). Plum Island Animal Disease Center;

The foot-and-mouth disease virus (FMDV) afflicts livestock in more than 80 countries, limiting food production and global trade. Production of foot-and-mouth disease (FMD) vaccines requires cytosolic expression of the FMDV 3C protease to cleave the P1 polyprotein into mature capsid proteins, but the FMDV 3C protease is toxic to host cells. To identify less-toxic isoforms of the FMDV 3C protease, we screened 3C mutants for increased transgene output in comparison to wild-type 3C using aGaussialuciferase reporter system. The novel point mutation 3C(L127P) increased yields of recombinant FMDV subunit proteins in mammalian and bacterial cells expressing P1-3C transgenes and retained the ability to process P1 polyproteins from multiple FMDV serotypes. The 3C(L127P) mutant produced crystalline arrays of FMDV-like particles in mammalian and bacterial cells, potentially providing a practical method of rapid, inexpensive FMD vaccine production in bacteria.

Research Organization:
Oak Ridge Associated Univ., Oak Ridge, TN (United States)
Sponsoring Organization:
USDOE
Grant/Contract Number:
AC05-06OR23100; HSHQDC-14-F-00035; HSHQPM-14-X00001
OSTI ID:
1626072
Journal Information:
Journal of Virology, Vol. 91, Issue 22; ISSN 0022-538X
Publisher:
American Society for MicrobiologyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 19 works
Citation information provided by
Web of Science

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Cited By (2)


Figures / Tables (8)