期刊
JOURNAL OF VIROLOGY
卷 85, 期 1, 页码 638-643出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01806-10
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资金
- Public Health Service [AI72493, AI26765]
- National Institutes of Health
- American Asthma Foundation
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI072493, R01AI026765, R56AI026765] Funding Source: NIH RePORTER
The nsp1 protein of transmissible gastroenteritis virus (TGEV), an alphacoronavirus, efficiently suppressed protein synthesis in mammalian cells. Unlike the nsp1 protein of severe acute respiratory syndrome coronavirus, a betacoronavirus, the TGEV nsp1 protein was unable to bind 40S ribosomal subunits or promote host mRNA degradation. TGEV nsp1 also suppressed protein translation in cell-free HeLa cell extract; however, it did not affect translation in rabbit reticulocyte lysate (RRL). Our data suggested that HeLa cell extracts and cultured host cells, but not RRL, contain a host factor(s) that is essential for TGEV nsp1-induced translational suppression.
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