Open AccessObservation of arenavirus nucleoprotein heptamer assembly
Author(s) -
Papageorgiou Nicolas,
Vaitsopoulou Afroditi,
Diop Awa,
Nguyen Thi Hong Van,
Canard Bruno,
Alvarez Karine,
Ferron François
Publication year - 2021
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.13106
Subject(s) - nucleoprotein , arenavirus , ribonucleoprotein , virology , negative stain , rna , biology , transcription (linguistics) , circular rna , microbiology and biotechnology , virus , genetics , electron microscope , gene , physics , lymphocytic choriomeningitis , antigen , linguistics , optics , philosophy , cd8
Arenaviruses are enveloped viruses containing a segmented, negative, and ambisense single‐stranded RNA genome wrapped with a nucleoprotein (NP). The NP is the most abundant viral protein in infected cells and plays a critical role in both replication/transcription and virion assembly. The NP associates with RNA to form a ribonucleoprotein (RNP) complex, and this implies self‐assembly while the exact structure of this polymer is not yet known. Here, we report a measurement of the full‐length Mopeia virus NP by negative stain transmission electron microscopy. We observed RNP complex particles with diameter 15 ± 1 nm as well as symmetric circular heptamers of the same diameter, consistent with previous observations.