About: Evolution and Structural Organization of the C Proteins of Paramyxovirinae

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Evolution and Structural Organization of the C Proteins of Paramyxovirinae
Creator	Karlin, David Lo, Michael Søgaard, Max
Source	PMC
abstract	The phosphoprotein (P) gene of most Paramyxovirinae encodes several proteins in overlapping frames: P and V, which share a common N-terminus (PNT), and C, which overlaps PNT. Overlapping genes are of particular interest because they encode proteins originated de novo, some of which have unknown structural folds, challenging the notion that nature utilizes only a limited, well-mapped area of fold space. The C proteins cluster in three groups, comprising measles, Nipah, and Sendai virus. We predicted that all C proteins have a similar organization: a variable, disordered N-terminus and a conserved, α-helical C-terminus. We confirmed this predicted organization by biophysically characterizing recombinant C proteins from Tupaia paramyxovirus (measles group) and human parainfluenza virus 1 (Sendai group). We also found that the C of the measles and Nipah groups have statistically significant sequence similarity, indicating a common origin. Although the C of the Sendai group lack sequence similarity with them, we speculate that they also have a common origin, given their similar genomic location and structural organization. Since C is dispensable for viral replication, unlike PNT, we hypothesize that C may have originated de novo by overprinting PNT in the ancestor of Paramyxovirinae. Intriguingly, in measles virus and Nipah virus, PNT encodes STAT1-binding sites that overlap different regions of the C-terminus of C, indicating they have probably originated independently. This arrangement, in which the same genetic region encodes simultaneously a crucial functional motif (a STAT1-binding site) and a highly constrained region (the C-terminus of C), seems paradoxical, since it should severely reduce the ability of the virus to adapt. The fact that it originated twice suggests that it must be balanced by an evolutionary advantage, perhaps from reducing the size of the genetic region vulnerable to mutations.
has issue date	2014-02-25(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0090003
bibo:pmid	24587180
has license	cc0
sha1sum (hex)	540ccda8bb32d2b9192782b878cc2759da109212
schema:url	https://doi.org/10.1371/journal.pone.0090003
resource representing a document's title	Evolution and Structural Organization of the C Proteins of Paramyxovirinae
has PubMed Central identifier	PMC3934983
has PubMed identifier	24587180
schema:publication	PLoS One
resource representing a document's body	covid:540ccda8bb32d2b9192782b878cc2759da109212#body_text
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