Improvements in large-scale production of tobacco etch virus protease [PDF]
Protein Expression and PurificationTobacco-etch-virus (TEV) protease is the workhorse of many laboratories in which protein expression is the linchpin of downstream experiments. TEV protease is remarkable in its sequence specificity as the cleavage sequence rarely appears in higher organisms and its ability to cleave fusion tag proteins from proteins of interest.
Simon Messing, Carissa Grose
exaly +4 more sources
Stability and Fitness Impact of the Visually Discernible Rosea1 Marker in the Tobacco etch virus Genome [PDF]
Viruses, 2013 Antirrhinum majus Rosea1 (Ros1) is an MYB-related transcription factor that induces anthocyanin biosynthesis in plant tissues, and has been shown to be suitable for visual tracking of virus infection in plants.
Mark P. Zwart +2 more
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Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self‐cleavage exhibits enhanced enzymatic activity [PDF]
FEBS Open Bio, 2020 Tobacco etch virus (TEV) protease is a 27‐kDa catalytic domain of the polyprotein nuclear inclusion a (NIa) in TEV, which recognizes the specific amino acid sequence ENLYFQG/S and cleaves between Q and G/S.
Heejin Nam +4 more
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A tobacco etch virus protease with increased substrate tolerance at the P1' position. [PDF]
PLoS ONE, 2013 Site-specific proteases are important tools for in vitro and in vivo cleavage of proteins. They are widely used for diverse applications, like protein purification, assessment of protein-protein interactions or regulation of protein localization ...
Christian Renicke +2 more
doaj +5 more sources
Differential temperature dependence of tobacco etch virus and rhinovirus 3C proteases [PDF]
Analytical Biochemistry, 2013 Because of their stringent sequence specificity, the 3C-like proteases from tobacco etch virus (TEV) and human rhinovirus are often used for the removal of affinity tags. The latter enzyme is rumored to have greater catalytic activity at 4 °C, the temperature at which fusion protein substrates are usually digested.
József Tőzsér +2 more
exaly +4 more sources
Development of a Platform for Noncovalent Coupling of Full Antigens to Tobacco Etch Virus-Like Particles by Means of Coiled-Coil Oligomerization Motifs [PDF]
Molecules, 2021 Virus-like particles are excellent inducers of the adaptive immune response of humans and are presently being used as scaffolds for the presentation of foreign peptides and antigens derived from infectious microorganisms for subunit vaccine development ...
Lorena Zapata-Cuellar +7 more
doaj +2 more sources
Expression and Purification of Recombinant Skd3 (Human ClpB) Protein and Tobacco Etch Virus (TEV) Protease from Escherichia coli [PDF]
Bio-Protocol, 2020 Skd3 (encoded by human CLPB) is a mitochondrial AAA+ protein comprised of an N-terminal ankyrin-repeat domain and a C-terminal HCLR-clade nucleotide-binding domain. The function of Skd3 has long remained unknown due to challenges in purifying the protein
Ryan Cupo, James Shorter
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Resistance to Tobacco Etch Virus in Capsicum annuum: Inhibition of Virus RNA Accumulation [PDF]
Molecular Plant-Microbe Interactions, 1997 Resistance to tobacco etch potyvirus (TEV) in Capsicum annuum cv. Dempsey gene eta . When Dempsey pepper plants were inoculated with either of two TEV isolates, virus did not accumulate in inoculated or noninoculated leaves. In contrast, each TEV isolate
C. Michael Deom +2 more
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Differences in accumulation and virulence determine the outcome of competition during Tobacco etch virus coinfection. [PDF]
PLoS ONE, 2011 Understanding the evolution of virulence for RNA viruses is essential for developing appropriate control strategies. Although it has been usually assumed that virulence is a consequence of within-host replication of the parasite, viral strains may be ...
Guillaume Lafforgue +2 more
doaj +2 more sources
Maturation-deficient chikungunya virus elicits protective immune responses in a murine challenge model [PDF]
npj VaccinesMaturation of chikungunya virus (CHIKV) particles is dependent on cleavage of the precursor glycoprotein p62 into the proteins E3 and E2 by the cellular protease furin.
Danillo Lucas Alves Esposito +3 more
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