Order and disorder bound together in SARS-CoV-2 Nsp1 suppress host translation

David S Libich; Antoine Baudin

doi:10.1016/j.str.2023.01.004

Order and disorder bound together in SARS-CoV-2 Nsp1 suppress host translation

Structure. 2023 Feb 2;31(2):121-122. doi: 10.1016/j.str.2023.01.004.

Authors

David S Libich¹, Antoine Baudin²

Affiliations

¹ Greehey Children's Cancer Research Institute, The University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA; The Department of Biochemistry and Structural Biology, The University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA. Electronic address: libich@uthscsa.edu.
² Greehey Children's Cancer Research Institute, The University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA; The Department of Biochemistry and Structural Biology, The University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.

Abstract

In this issue of Structure, Wang et al. investigate the interplay between folded and disordered regions of the SARS-CoV-2 non-structural protein 1 (Nsp1) that promotes the suppression of host protein translation. Their investigation will lead to novel avenues to therapeutically target critical viral functions necessary for host immune-response suppression.

Publication types

Comment

MeSH terms

COVID-19*
Humans
SARS-CoV-2* / metabolism
Viral Nonstructural Proteins / chemistry

Substances

Viral Nonstructural Proteins