Journal of Molecular Biology
Regular ArticleThe Refined Three-Dimensional Structure of an Insect Virus at 2·8 Å Resolution
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Icosahedral virus structures and the protein data bank
2021, Journal of Biological ChemistryCitation Excerpt :Input from Sgro and others guided efforts at Purdue to develop straightforward lists of residues at subunit interfaces and residues solvent-exposed on the interior and exterior surfaces. These were extended to determine the character of subunit interfaces by developing contact tables where comparisons could be made between quasi-equivalent interfaces and comparable icosahedral interfaces and the character of the stabilizing forces determined (i.e., ionic, hydrophobic, etc.) (22). These were assembled by virus crystallographers at Purdue for coordinates in the pdb and supplied to virologists to develop structure-based investigations of virus biology.
Evolutionary history of ssDNA bacilladnaviruses features horizontal acquisition of the capsid gene from ssRNA nodaviruses
2017, VirologyCitation Excerpt :However, in bacilladnaviruses, the classical jelly-roll core (Rossmann and Johnson, 1989) is embellished with additional structural elements that are uniquely shared with the CPs of nodaviruses. Most notably, CPs in both virus groups contain one N-terminal and two C-terminal α-helices, which are oriented into the interior of the capsid and, in the case of nodaviruses, have been shown to form a helix bundle and interact with the viral genome (Wery et al., 1994). In addition, the CPs share two β-hairpins inserted into the jelly-roll core: the first of these hairpins extends one of the two β-sheets in the jelly-roll fold which becomes 6-stranded (instead of the 4-stranded β-sheet in the classical jelly-roll fold), whereas the second twisted hairpin makes hydrophobic contacts with the corresponding hairpins from the neighboring subunits at the quasi 3-fold axes of the icosahedral capsid, forming protrusions that face away from the virion surface (Wery et al., 1994).
C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization
2017, Virus ResearchCitation Excerpt :Along with the ability of chymotrypsin to hydrolyze the C-terminal domain tagged with hexahistidine residues, it thus suggested outward protrusion of the C-terminal domain from the capsid shell of the MrNV VLPs. The location of an external, protruding C-terminal domain of the viral capsids is applicable to the betanodaviruses rather than the alphanodaviruses, where in FHV and PaV the C-terminal domain is part of the internal domain of the capsid subunit (Fisher and Johnson, 1993; Tang et al., 2001; Wery et al., 1994). It is thus presumed that MrNV capsid would be more resembled to that of the known structure of the betanodavirus MGNNV.
Encapsulation and delivery of plasmid DNA by virus-like nanoparticles engineered from Macrobrachium rosenbergii nodavirus
2014, Virus ResearchCitation Excerpt :Although MrNv has been discovered for a considerable period of time (Arcier et al., 1999; Qian et al., 2003), detailed studies on its viral capsid protein were not reported until recently (Goh et al., 2011). In contrast, more extensive data has been available of other nodaviruses in fish and insects (Fisher and Johnson, 1993; Tang et al., 2001, 2002; Wery et al., 1994). The lack of MrNv information is partly due to the lack of continuous crustacean cell lines that can be used for the virus replication and propagation (Sudhakaran et al., 2007).
Introduction: Aspartic and Glutamic Peptidases and Their Clans
2013, Handbook of Proteolytic EnzymesCharacterization of member of DUF1888 protein family, self-cleaving and self-assembling endopeptidase
2012, Journal of Biological ChemistryCitation Excerpt :Several peptidases display self-cleaving activity that results in significant conformational change in the protein. This feature is observed in viral proteins, where autocatalytic cleavage is followed by assembly of mature proteins into infectious virions (34–36). Clan AB represents the aspartyl endopeptidases that are viral coat proteins from nodavirus and tetravirus.