Title |
“Self-cleaving” 2A peptide from porcine teschovirus-1 mediates cleavage of dual fluorescent proteins in transgenic Eimeria tenella
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Published in |
Veterinary Research, June 2016
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DOI | 10.1186/s13567-016-0351-z |
Pubmed ID | |
Authors |
Xinming Tang, Xianyong Liu, Geru Tao, Mei Qin, Guangwen Yin, Jingxia Suo, Xun Suo |
Abstract |
The "self-cleaving" 2A sequence of picornavirus, which mediates ribosome-skipping events, enables the generation of two or more separate peptide products from one mRNA containing one or more "self-cleaving" 2A sequences. In this study, we introduced a single 2A sequence of porcine teschovirus-1 (P2A) linked to two fluorescent protein genes, the enhanced yellow fluorescent protein (EYFP) gene and the red fluorescent protein (RFP) gene, in a single cassette into transgenic Eimeria tenella (EtER). As expected, we obtained two separated protein molecules rather than a fused protein, although the two molecules were translated from the same mRNA carrying a single "self-cleaving" 2A sequence. Importantly, RFP led by a secretion signal was secreted into parasitophorous vacuoles, while EYFP localized mainly to the nucleus of EtER. Our results demonstrate that the "self-cleaving" 2A sequence actively mediated cleavage of polyproteins in the apicomplexan parasite E. tenella. |
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United States | 1 | 50% |
Unknown | 1 | 50% |
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Members of the public | 2 | 100% |
Mendeley readers
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Student > Ph. D. Student | 10 | 18% |
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Researcher | 6 | 11% |
Student > Doctoral Student | 4 | 7% |
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Immunology and Microbiology | 1 | 2% |
Other | 3 | 5% |
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