Cryo-EM structure of Nipah virus RNA polymerase complex.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 39661676.
- Also identified by DOI 10.1126/sciadv.adr7116 and PMC identifier 11633731.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Nipah virus, a member of the <i>Paramyxoviridae</i> family, is a highly pathogenic nonsegmented, negative-sense RNA virus (nsNSV) which causes severe neurological and respiratory illnesses in humans. There are no available drugs or vaccines to combat this virus. A complex of large polymerase protein (L) and phosphoprotein (P) of Nipah virus supports replication and transcription and affords a target for antiviral drug development. Structural information required for drug development is lacking. Here we report the 2.9-angstrom cryo-electron microscopy structure of the Nipah virus polymerase-phosphoprotein complex. The structure identifies conserved amino acids likely important for recognition of template RNA by nsNSVs and reveals the locations of mutation-prone sites among Nipah virus strains, which may facilitate the development of therapeutic agents against Nipah virus by targeting regions unaffected by these mutation sites.
Medical subject headings
- Nipah Virus
- Cryoelectron Microscopy
- DNA-Directed RNA Polymerases