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Literature summary extracted from

  • Wengler, G.
    The regulation of disassembly of alphavirus cores (2009), Arch. Virol., 154, 381-390.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.90 additional information cores, which are resistant to trypsin at physiological salt concentrations, whereas become trypsin sensitive at elevated salt concentrations and under these conditions, the carboxy-terminal domain, beginning with position M(106) is released as a soluble protein. Use of endoproteinase LysC instead of trypsin allows a somewhat larger soluble carboxy-terminal domain beginning with Q(94). The disassembly of cores is stimulated by increasing the concentration of NaCl in the reaction, by the presence of octylglycoside, and by lowering the pH of the reaction to 6.0 and is not stimulated by the presence of NP 40 Sindbis virus
3.4.21.90 additional information the disassembly of cores is stimulated by increasing the concentration of NaCl, but neither octylglucoside nor low pH stimulates the reaction Semliki forest virus

Application

EC Number Application Comment Organism
3.4.21.90 drug development alphavirus core protein is a target for antiviral chemotherapy Sindbis virus
3.4.21.90 drug development alphavirus core protein is a target for antiviral chemotherapy Semliki forest virus
3.4.21.90 drug development alphavirus core protein is a target for antiviral chemotherapy Chikungunya virus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.90 at 25 A resolution Ross River virus
3.4.21.90 at 9 A resolution, the C-terminal domain folds into a trypsin-like protease structure Semliki forest virus
3.4.21.90 at 9 A resolution, the carboxyterminal domain folds into a trypsin-like protease structure Sindbis virus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.90 drug development alphavirus core protein is a target for antiviral chemotherapy Ross River virus
3.4.21.90 additional information mutant containing a deletion of residues K(97) to M(106), wild-type-like cores are assembled in the cytoplasm, and particle formation is largely unaffected, but 26S subgenomic viral RNA, which is not incorporated into wild-type particles, is efficiently packaged into cores and virus particles. Mutations in the linker region and in neighbouring regions of the core protein have no effect on disassembly of viral cores during virus entry Sindbis virus
3.4.21.90 additional information mutants containing deletions of residues P(105) to D(118) and M(111) to D(118) in the core protein are viable, but the specific infectivity of these viruses is about 10fold less than the infectivity of wild-type virus. After lysis of infected cells or virus particles, mutant core protein with deletion of residues Q(40) to R(118) behaves as a monomer, whereby the core is generated during virus particle formation by the collection of core protein molecules by the viral membrane proteins prior to and/or during assembly of the viral surface proteins into an icosahedral shell Semliki forest virus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.90 additional information the carboxy-terminal amino acid residues of the core protein remain associated to the active site after cleavage and thereby inactivate the enzyme Semliki forest virus
3.4.21.90 additional information the carboxy-terminal amino acid residues of the core protein remain associated to the active site after cleavage and thereby inactivate the enzyme Sindbis virus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.90 additional information in the host, the core protein is transferred to ribosomes, the ribosome bound core protein is distributed throughout the cytoplasm, whereas the genome RNA remains associated with vacuolar membranes Semliki forest virus
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Organism

EC Number Organism UniProt Comment Textmining
3.4.21.90 Chikungunya virus
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3.4.21.90 Ross River virus
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3.4.21.90 Semliki forest virus
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3.4.21.90 Sindbis virus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.90 additional information the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. A short linker sequence connects the basic domain to the protease domain. In the Sindbis virus core protein, the basic domain, the linker sequence and the protease domain comprise amino acid residues M(1) to Q(94), P(95) to D(113), and R(114) to W(264), respectively. Core protein domain beginning at M(106) does not bind to the 60S ribosomal subunit, whereas core protein domain beginning at Q(94) binds to the 60S ribosomal subunit and inhibits the disassembly of cores in vitro Sindbis virus ?
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3.4.21.90 additional information the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. Core protein is associated to the large 60S ribosomal subunit during in vitro protein synthesis and in the infected cell Semliki forest virus ?
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Synonyms

EC Number Synonyms Comment Organism
3.4.21.90 core protein
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 Sindbis virus
3.4.21.90 core protein
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 Semliki forest virus
3.4.21.90 core protein
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 Ross River virus
3.4.21.90 core protein
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 Chikungunya virus