Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein
| العنوان: | Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein |
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| المؤلفون: | Robert J. Fletterick, J F Bazan, David W. McCourt, T J Chambers, R C Weir, Charles M. Rice, Arash Grakoui |
| المصدر: | Proceedings of the National Academy of Sciences. 87:8898-8902 |
| بيانات النشر: | Proceedings of the National Academy of Sciences, 1990. |
| سنة النشر: | 1990 |
| مصطلحات موضوعية: | Genes, Viral, viruses, medicine.medical_treatment, DNA Mutational Analysis, Viral Nonstructural Proteins, Virus, Viral Proteins, Flaviviridae, Capsid, medicine, Cloning, Molecular, Protein Precursors, Viral Structural Proteins, Serine protease, NS3, Multidisciplinary, Protease, biology, Viral Core Proteins, Serine Endopeptidases, biology.organism_classification, Virology, Molecular biology, NS2-3 protease, Flavivirus, Protein Biosynthesis, biology.protein, Yellow fever virus, MASP1, Research Article |
| الوصف: | Sequence homology and molecular modeling studies have suggested that the N-terminal one-third of the flavirvirus nonstructural protein NS3 functions as a trypsin-like serine protease. To examine the putative proteolytic activity of NS3, segments of the yellow fever virus genome were subcloned into plasmid transcription/translation vectors and cell-free translation products were characterized. The results suggest that a protease activity encoded within NS2B and the N-terminal one-third of yellow fever virus NS3 is capable of cis-acting site-specific proteolysis at the NS2B-NS3 cleavage site and dilution-insensitive cleavage of the NS2A-NS2B site. Site-directed mutagenesis of the His-53, Asp-77, and Ser-138 residues of NS3 that compose the proposed catalytic triad implicates this domain as a serine protease. Infectious virus was not recovered from mammalian cells transfected with RNAs transcribed from full-length yellow fever virus cDNA templates containing mutations at Ser-138 (which abolish or dramatically reduce protease activity in vitro), suggesting that the protease is required for viral replication. |
| تدمد: | 1091-6490 0027-8424 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9327c9e3d2300755b43e273a12ccf2b7 https://doi.org/10.1073/pnas.87.22.8898 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....9327c9e3d2300755b43e273a12ccf2b7 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10916490 00278424 |
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