Structure of the C-Terminal Domain of Lettuce Necrotic Yellows Virus Phosphoprotein

Abstract

e Lettuce necrotic yellows virus (LNYV) is a prototype of the plant-adapted cytorhabdoviruses. Through a meta-prediction of disorder, we localized a folded C-terminal domain in the amino acid sequence of its phosphoprotein. This domain consists of an autonomous folding unit that is monomeric in solution. Its structure, solved by X-ray crystallography, reveals a lollipop-shaped structure comprising five helices. The structure is different from that of the corresponding domains of other Rhabdoviridae, Filoviridae, and Paramyxovirinae; only the overall topology of the polypeptide chain seems to be conserved, suggesting that this domain evolved under weak selective pressure and varied in size by the acquisition or loss of functional modules.

Complete genome sequence and integrated protein localization and interaction map for alfalfa dwarf virus, which combines properties of both cytoplasmic and nuclear plant rhabdoviruses

“…Little is known about the functions of cytorhabdovirus P proteins, besides the recently determined structure of the Cterminal domain of LNYV P and its local RNA silencing suppressor activity in plants (Martinez et al, 2013;Mann et al, 2015). It would be of particular interest to determine if P protein nuclear localization and interaction with N protein may also be a feature of other cytorhabdoviruses that are closely related to ADV, like PeVA and SCV.…”

Unraveling virus relationships by structure-based phylogenetic classification

“…Calculated evolutionary distances derived from this analysis are indicated next to each branch. phosphoprotein CTD core (Martinez et al 2013) and Bcl-2/Bcl-2like proteins (Graham et al 2008;Bahar et al 2011b;Neidel et al 2015) provides a context for how a common protein fold may be elaborated to achieve distinct functionality.…”

“…A phosphoprotein (P) composed of a three-domain assembly (a disordered N-terminal domain, a central oligomerization domain, and a conserved C-terminal domain) plays essential roles in viral RNA synthesis across a number of negative-stranded RNA viruses from the order Mononegavirales, including members of the Filoviridae, Paramyxoviridae, and Rhabdoviridae families (Assenberg et al 2010;Ivanov et al 2010;Martinez et al 2013). Although sequence homology of this protein across these families is low and in some cases undetectable (Delmas et al 2010;Karlin and Belshaw 2012), structural analyses have revealed that the C-terminal domain (P CTD ) of the molecule contains a common a-helical core (Fig.…”

“…Indeed, the addition of five a-helices to the plant rhabdovirus P CTD , and ahelical and b-sheet subdomains to the filovirus P CTD have both been shown to regulate viral transcription (Das et al 1997) and facilitate additional RNA binding and immune evasion functionality (Leung et al 2009(Leung et al , 2010. The structural elaboration of the evolutionarily conserved P CTD core is reflected upon SBPA (Martinez et al 2013), where P CTD structures from each viral family classify to a single branch on the tree. In this case, SBPA provides an efficient means to visualize how a basic protein fold scaffold has been adapted to achieve different functionalities.…”

Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1

“…The threshold to distinguish between the ordered and disordered regions is set at 0. algorithms accessible through web servers and by calculating a consensus prediction as described previously (32,50). The calculated disorder score (D-score) varies between 0 and 1, and generally, regions with a D-score lower than 0.5 are intrinsically disordered, whereas regions with a score higher than 0.5 are either folded domains (50)(51)(52) or potential molecular recognition elements for partner proteins (53).…”