Journal Article

PUBDB-2021-04335

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Hallmarks of Alpha- and Betacoronavirus non-structural protein 7+8 complexes

Krichel, B. ; Bylapudi, G. ; Schmidt, C. ; Blanchet, C.Extern*EMBL* ; Schubert, R. ; Brings, L. ; Koehler, M. ; Zenobi, R. ; Svergun, D.EMBL* ; Lorenzen, K.XFEL.EU* ; Madhugiri, R. ; Ziebuhr, J. ; Uetrecht, C. (Corresponding author)CSSB*XFEL.EU*

2021
Assoc. Washington, DC [u.a.]

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Please use a persistent id in citations: doi:10.1126/sciadv.abf1004  doi:10.3204/PUBDB-2021-04335

Abstract: Coronaviruses infect many different species including humans. The last two decades have seen three zoonotic coronaviruses, with SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) causing a pandemic in 2020. Coronaviral non-structural proteins (nsps) form the replication-transcription complex (RTC). Nsp7 and nsp8 interact with and regulate the RNA-dependent RNA-polymerase and other enzymes in the RTC. However, the structural plasticity of nsp7+8 complexes has been under debate. Here, we present the framework of nsp7+8 complex stoichiometry and topology based on native mass spectrometry and complementary biophysical techniques of nsp7+8 complexes from seven coronaviruses in the genera Alpha- and Betacoronavirus including SARS-CoV-2. Their complexes cluster into three groups, which systematically form either heterotrimers or heterotetramers or both, exhibiting distinct topologies. Moreover, even at high protein concentrations, SARS-CoV-2 nsp7+8 consists primarily of heterotetramers. From these results, the different assembly paths can be pinpointed to specific residues and an assembly model proposed.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)
2. EMBL (EMBL)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2021

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