Identification of a guanine-specific pocket in the protein N of SARS-CoV-2

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Identification of a guanine-specific pocket in the protein N of SARS-CoV-2. / Rafael Ciges-Tomas, J.; Franco, María Luisa; Vilar, Marçal.

In: Communications Biology , Vol. 5, No. 1, 711, 2022.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rafael Ciges-Tomas, J, Franco, ML & Vilar, M 2022, 'Identification of a guanine-specific pocket in the protein N of SARS-CoV-2', Communications Biology , vol. 5, no. 1, 711. https://doi.org/10.1038/s42003-022-03647-8

APA

Rafael Ciges-Tomas, J., Franco, M. L., & Vilar, M. (2022). Identification of a guanine-specific pocket in the protein N of SARS-CoV-2. Communications Biology , 5(1), [711]. https://doi.org/10.1038/s42003-022-03647-8

Vancouver

Rafael Ciges-Tomas J, Franco ML, Vilar M. Identification of a guanine-specific pocket in the protein N of SARS-CoV-2. Communications Biology . 2022;5(1). 711. https://doi.org/10.1038/s42003-022-03647-8

Author

Rafael Ciges-Tomas, J. ; Franco, María Luisa ; Vilar, Marçal. / Identification of a guanine-specific pocket in the protein N of SARS-CoV-2. In: Communications Biology . 2022 ; Vol. 5, No. 1.

Bibtex

@article{ec9e94136f944db09bc138ed024ab87c,
title = "Identification of a guanine-specific pocket in the protein N of SARS-CoV-2",
abstract = "The SARS-CoV-2 nucleocapsid protein (N) is responsible for RNA binding. Here we report the crystal structure of the C-terminal domain (NCTD) in open and closed conformations and in complex with guanine triphosphate, GTP. The crystal structure and biochemical studies reveal a specific interaction between the guanine, a nucleotide enriched in the packaging signals regions of coronaviruses, and a highly conserved tryptophan residue (W330). In addition, EMSA assays with SARS-CoV-2 derived RNA hairpin loops from a putative viral packaging sequence showed the preference interaction of the N-CTD to RNA oligonucleotides containing G and the loss of the specificity in the mutant W330A. Here we propose that this interaction may facilitate the viral assembly process. In summary, we have identified a specific guanine-binding pocket in the N protein that may be used to design viral assembly inhibitors.",
keywords = "COVID-19, Guanine, Humans, Nucleocapsid Proteins/chemistry, RNA, Viral/metabolism, SARS-CoV-2/genetics",
author = "{Rafael Ciges-Tomas}, J. and Franco, {Mar{\'i}a Luisa} and Mar{\c c}al Vilar",
note = "{\textcopyright} 2022. The Author(s).",
year = "2022",
doi = "10.1038/s42003-022-03647-8",
language = "English",
volume = "5",
journal = "Communications Biology",
issn = "2399-3642",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Identification of a guanine-specific pocket in the protein N of SARS-CoV-2

AU - Rafael Ciges-Tomas, J.

AU - Franco, María Luisa

AU - Vilar, Marçal

N1 - © 2022. The Author(s).

PY - 2022

Y1 - 2022

N2 - The SARS-CoV-2 nucleocapsid protein (N) is responsible for RNA binding. Here we report the crystal structure of the C-terminal domain (NCTD) in open and closed conformations and in complex with guanine triphosphate, GTP. The crystal structure and biochemical studies reveal a specific interaction between the guanine, a nucleotide enriched in the packaging signals regions of coronaviruses, and a highly conserved tryptophan residue (W330). In addition, EMSA assays with SARS-CoV-2 derived RNA hairpin loops from a putative viral packaging sequence showed the preference interaction of the N-CTD to RNA oligonucleotides containing G and the loss of the specificity in the mutant W330A. Here we propose that this interaction may facilitate the viral assembly process. In summary, we have identified a specific guanine-binding pocket in the N protein that may be used to design viral assembly inhibitors.

AB - The SARS-CoV-2 nucleocapsid protein (N) is responsible for RNA binding. Here we report the crystal structure of the C-terminal domain (NCTD) in open and closed conformations and in complex with guanine triphosphate, GTP. The crystal structure and biochemical studies reveal a specific interaction between the guanine, a nucleotide enriched in the packaging signals regions of coronaviruses, and a highly conserved tryptophan residue (W330). In addition, EMSA assays with SARS-CoV-2 derived RNA hairpin loops from a putative viral packaging sequence showed the preference interaction of the N-CTD to RNA oligonucleotides containing G and the loss of the specificity in the mutant W330A. Here we propose that this interaction may facilitate the viral assembly process. In summary, we have identified a specific guanine-binding pocket in the N protein that may be used to design viral assembly inhibitors.

KW - COVID-19

KW - Guanine

KW - Humans

KW - Nucleocapsid Proteins/chemistry

KW - RNA, Viral/metabolism

KW - SARS-CoV-2/genetics

U2 - 10.1038/s42003-022-03647-8

DO - 10.1038/s42003-022-03647-8

M3 - Journal article

C2 - 35842466

VL - 5

JO - Communications Biology

JF - Communications Biology

SN - 2399-3642

IS - 1

M1 - 711

ER -

ID: 314626731