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Structure and stability of the Human respiratory syncytial virus M RNA-binding core domain reveals a compact and cooperative folding unit. | LitMetric

Structure and stability of the Human respiratory syncytial virus M RNA-binding core domain reveals a compact and cooperative folding unit.

Acta Crystallogr F Struct Biol Commun

The Hamburg Centre for Ultrafast Imaging and Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.

Published: January 2018

AI Article Synopsis

  • Human syncytial respiratory virus (HRSV) is a negative-strand RNA virus that primarily affects infants and has been reclassified into the Pneumoviridae family due to its unique features.
  • The virus has a transcriptional antiterminator named M, which plays a crucial role in RNA synthesis and is unusual among viruses, making its mechanism of action intriguing to researchers.
  • Recent studies provide a detailed crystal structure of the M protein, revealing important insights into its RNA-binding domain and stability, which could have implications for understanding transcription regulation and developing antiviral therapies.

Article Abstract

Human syncytial respiratory virus is a nonsegmented negative-strand RNA virus with serious implications for respiratory disease in infants, and has recently been reclassified into a new family, Pneumoviridae. One of the main reasons for this classification is the unique presence of a transcriptional antiterminator, called M. The puzzling mechanism of action of M, which is a rarity among antiterminators in viruses and is part of the RNA polymerase complex, relies on dissecting the structure and function of this multidomain tetramer. The RNA-binding activity is located in a monomeric globular `core' domain, a high-resolution crystal structure of which is now presented. The structure reveals a compact domain which is superimposable on the full-length M tetramer, with additional electron density for the C-terminal tail that was not observed in the previous models. Moreover, its folding stability was determined through chemical denaturation, which shows that the secondary and tertiary structure unfold concomitantly, which is indicative of a two-state equilibrium. These results constitute a further step in the understanding of this unique RNA-binding domain, for which there is no sequence or structural counterpart outside this virus family, in addition to its implications in transcription regulation and its likeliness as an antiviral target.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5947689PMC
http://dx.doi.org/10.1107/S2053230X17017381DOI Listing

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