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Super-resolution proximity labeling reveals anti-viral protein network and its structural changes against SARS-CoV-2 viral proteins

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Title
Super-resolution proximity labeling reveals anti-viral protein network and its structural changes against SARS-CoV-2 viral proteins
Author(s)
Lee, Yun-Bin; Jung, Minkyo; Kim, Jeesoo; Charles, Afandi; Christ, Wanda; Kang, Jiwoong; Kang, Myeong-Gyun; Kwak, Chulhwan; Klingström, Jonas; Smed-Sörensen, Anna; Jong-Seo Kim; Mun, Ji Young; Rhee, Hyun-Woo
Publication Date
2023-08
Journal
Cell Reports, v.42, no.8
Publisher
Elsevier B.V.
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) replicates in human cells by interacting with host factors following infection. To understand the virus and host interactome proximity, we introduce a super-resolution proximity labeling (SR-PL) method with a “plug-and-playable” PL enzyme, TurboID-GBP (GFP-binding nanobody protein), and we apply it for interactome mapping of SARS-CoV-2 ORF3a and membrane protein (M), which generates highly perturbed endoplasmic reticulum (ER) structures. Through SR-PL analysis of the biotinylated interactome, 224 and 272 peptides are robustly identified as ORF3a and M interactomes, respectively. Within the ORF3a interactome, RNF5 co-localizes with ORF3a and generates ubiquitin modifications of ORF3a that can be involved in protein degradation. We also observe that the SARS-CoV-2 infection rate is efficiently reduced by the overexpression of RNF5 in host cells. The interactome data obtained using the SR-PL method are presented at https://sarscov2.spatiomics.org. We hope that our method will contribute to revealing virus-host interactions of other viruses in an efficient manner. © 2023 The Authors
URI
https://pr.ibs.re.kr/handle/8788114/13872
DOI
10.1016/j.celrep.2023.112835
ISSN
2211-1247
Appears in Collections:
Center for RNA Research(RNA 연구단) > 1. Journal Papers (저널논문)
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