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Both ADP-Ribosyl-Binding and Hydrolase Activities of the Alphavirus nsP3 Macrodomain Affect Neurovirulence in Mice.
Title: Both ADP-Ribosyl-Binding and Hydrolase Activities of the Alphavirus nsP3 Macrodomain Affect Neurovirulence in Mice.
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These data suggest that in spite of the differences in morphology and composition of the Sindbis- and Venezuelan equine encephalitis virus-specific nsP3 complexes, it is likely that they have similar functions in virus replication.[nsP3]
Title: Hypervariable domains of nsP3 proteins of New World and Old World alphaviruses mediate formation of distinct, virus-specific protein complexes.
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analysis of the early temporal and spatial interaction of the Sindbis virus capsid and E2 proteins with reverse genetics [capsid, E2]
Title: Probing the early temporal and spatial interaction of the Sindbis virus capsid and E2 proteins with reverse genetics.
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Data suggest that Sindbis virus infection leads to the formation of two types of nsP3-containing complexes, one of which is found in association with the plasma membrane and endosome-like vesicles, while the second is coisolated with cell nuclei [nsP3].
Title: Different types of nsP3-containing protein complexes in Sindbis virus-infected cells.
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The defective and lethal mutants give insight into regions of E2 important for protein stability, transport to the cell membrane, E1-E2 contacts, and receptor binding [E2]
Title: Functional characterization of the Sindbis virus E2 glycoprotein by transposon linker-insertion mutagenesis.
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investigated the role of the amino acid residues located at or around position E2 391 and constraints on the length of the endodomain on virus assembly [E2 protein]
Title: Single amino acid insertions at the junction of the sindbis virus E2 transmembrane domain and endodomain disrupt virus envelopment and alter infectivity.
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Requirements for the binding of Sindbis virus capsid protein to the cytoplasmic domain of the E2 glycoprotein, (capsid)
Title: Association of sindbis virus capsid protein with phospholipid membranes and the E2 glycoprotein: implications for alphavirus assembly.
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Deletions in the glycoprotein E2 endodomain (delta406-407, delta409-411, and delta414-417) resulted in the failure to assemble virions in mammalian cells [glycoprotein E2]
Title: Mutations in the endodomain of Sindbis virus glycoprotein E2 define sequences critical for virus assembly.
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analysis of free cysteinyl residues in the Sindbis virus E1 and E2 glycoproteins [E1, E2]
Title: Location and role of free cysteinyl residues in the Sindbis virus E1 and E2 glycoproteins.
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Seven sites of biotin modification were identified in the E2 glycoprotein, while one site of modification in the E1 glycoprotein (K16) was identified, confirming that the E1 protein is almost completely buried in the virus structure.[E2]
Title: Structural characterization of the E2 glycoprotein from Sindbis by lysine biotinylation and LC-MS/MS.