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@ARTICLE{SchamoniKast:637344,
author = {Schamoni-Kast, Kira and Uetrecht, Charlotte},
title = {{F}rom {S}cience to {F}iction – {C}onnecting {I}n {V}ivo
and {I}n {V}itro {R}esults in {P}olyprotein {P}rocessing of
{C}oronaviruses},
journal = {Journal of molecular biology},
volume = {437},
number = {22},
issn = {0022-2836},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {PUBDB-2025-03836},
pages = {169370},
year = {2025},
abstract = {Polyprotein processing is a common strategy in many
positive sense single-stranded RNA ((+)ssRNA) viruses. This
highly regulated process is crucial for viral progeny and
ensures the release of functional replicase proteins in the
correct location and at the right time. Coronaviruses (CoVs)
have one of the largest genomes on average among (+)ssRNA
viruses requiring a unique replication-transcription complex
(RTC) with proofreading function that prevents error
catastrophe. Two thirds of the CoV genome encode for the
non-structural proteins (nsps) that drive replication. These
are directly synthesized by RNA genome translation after
infection as two large polyproteins pp1a and pp1ab. A
regulated polyprotein proteolytic auto-processing is
essential for viral growth and always has been an
interesting target for therapeutics.Here, we present an
overview of polyprotein processing and RTC research in CoVs
in vitro and in vivo over the last 30 years. We highlight
cutting-edge methodologies such as super resolution
microscopy or structural mass spectrometry approaches and
demonstrate how these have contributed to polyprotein
research, e.g. by providing comprehensive structural models.
We illustrate exciting examples of polyprotein processing in
other viruses that could be transferred to CoVs, too.
Additionally, we identify critical knowledge gaps in
polyprotein processing and RTC assembly, proposing future
perspectives to address these limitations.},
cin = {CSSB-LIV/DESY-CU},
ddc = {610},
cid = {$I:(DE-H253)CSSB-LIV_DESY-CU-20220525$},
pnm = {633 - Life Sciences – Building Blocks of Life: Structure
and Function (POF4-633) / ARIADNE - Redefining mass
spectrometry – a breakthrough platform for real-time
noninvasive breath analysis with single ion detection of
intact viruses and bacteria and post-analysis molecular
characterization (964553) / SPOCkS MS - Sampling Protein
cOmplex Conformational Space with native top down Mass
Spectrometry (759661)},
pid = {G:(DE-HGF)POF4-633 / G:(EU-Grant)964553 /
G:(EU-Grant)759661},
experiment = {EXP:(DE-MLZ)NOSPEC-20140101},
typ = {PUB:(DE-HGF)16},
doi = {10.1016/j.jmb.2025.169370},
url = {https://bib-pubdb1.desy.de/record/637344},
}