Molecular basis for inhibition of type III-B CRISPR-Cas by an archaeal viral anti-CRISPR protein

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Molecular basis for inhibition of type III-B CRISPR-Cas by an archaeal viral anti-CRISPR protein. / Lin, Jinzhong; Alfastsen, Lauge; Bhoobalan-Chitty, Yuvaraj; Peng, Xu.

I: Cell Host and Microbe, Bind 31, Nr. 11, 2023, s. 1837-1849.e5.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Lin, J, Alfastsen, L, Bhoobalan-Chitty, Y & Peng, X 2023, 'Molecular basis for inhibition of type III-B CRISPR-Cas by an archaeal viral anti-CRISPR protein', Cell Host and Microbe, bind 31, nr. 11, s. 1837-1849.e5. https://doi.org/10.1016/j.chom.2023.10.003

APA

Lin, J., Alfastsen, L., Bhoobalan-Chitty, Y., & Peng, X. (2023). Molecular basis for inhibition of type III-B CRISPR-Cas by an archaeal viral anti-CRISPR protein. Cell Host and Microbe, 31(11), 1837-1849.e5. https://doi.org/10.1016/j.chom.2023.10.003

Vancouver

Lin J, Alfastsen L, Bhoobalan-Chitty Y, Peng X. Molecular basis for inhibition of type III-B CRISPR-Cas by an archaeal viral anti-CRISPR protein. Cell Host and Microbe. 2023;31(11):1837-1849.e5. https://doi.org/10.1016/j.chom.2023.10.003

Author

Lin, Jinzhong ; Alfastsen, Lauge ; Bhoobalan-Chitty, Yuvaraj ; Peng, Xu. / Molecular basis for inhibition of type III-B CRISPR-Cas by an archaeal viral anti-CRISPR protein. I: Cell Host and Microbe. 2023 ; Bind 31, Nr. 11. s. 1837-1849.e5.

Bibtex

@article{d8ac7356bbc847fd802b23cde0053641,
title = "Molecular basis for inhibition of type III-B CRISPR-Cas by an archaeal viral anti-CRISPR protein",
abstract = "Despite a wide presence of type III clustered regularly interspaced short palindromic repeats, CRISPR-associated (CRISPR-Cas) in archaea and bacteria, very few anti-CRISPR (Acr) proteins inhibiting type III immunity have been identified, and even less is known about their inhibition mechanism. Here, we present the discovery of a type III CRISPR-Cas inhibitor, AcrIIIB2, encoded by Sulfolobus virus S. islandicus rod-shaped virus 3 (SIRV3). AcrIIIB2 inhibits type III-B CRISPR-Cas immune response to protospacers encoded in middle/late-expressed viral genes. Investigation of the interactions between S. islandicus type III-B CRISPR-Cas Cmr-α-related proteins and AcrIIIB2 reveals that the Acr does not bind to Csx1 but rather interacts with the Cmr-α effector complex. Furthermore, in vitro assays demonstrate that AcrIIIB2 can block the dissociation of cleaved target RNA from the Cmr-α complex, thereby inhibiting the Cmr-α turnover, thus preventing host cellular dormancy and further viral genome degradation by the type III-B CRISPR-Cas immunity.",
keywords = "Acr inhibition mechanism, anti-CRISPR, CRISPR-Cas turnover, type III CRISPR",
author = "Jinzhong Lin and Lauge Alfastsen and Yuvaraj Bhoobalan-Chitty and Xu Peng",
note = "Publisher Copyright: {\textcopyright} 2023 Elsevier Inc.",
year = "2023",
doi = "10.1016/j.chom.2023.10.003",
language = "English",
volume = "31",
pages = "1837--1849.e5",
journal = "Cell Host & Microbe",
issn = "1931-3128",
publisher = "Cell Press",
number = "11",

}

RIS

TY - JOUR

T1 - Molecular basis for inhibition of type III-B CRISPR-Cas by an archaeal viral anti-CRISPR protein

AU - Lin, Jinzhong

AU - Alfastsen, Lauge

AU - Bhoobalan-Chitty, Yuvaraj

AU - Peng, Xu

N1 - Publisher Copyright: © 2023 Elsevier Inc.

PY - 2023

Y1 - 2023

N2 - Despite a wide presence of type III clustered regularly interspaced short palindromic repeats, CRISPR-associated (CRISPR-Cas) in archaea and bacteria, very few anti-CRISPR (Acr) proteins inhibiting type III immunity have been identified, and even less is known about their inhibition mechanism. Here, we present the discovery of a type III CRISPR-Cas inhibitor, AcrIIIB2, encoded by Sulfolobus virus S. islandicus rod-shaped virus 3 (SIRV3). AcrIIIB2 inhibits type III-B CRISPR-Cas immune response to protospacers encoded in middle/late-expressed viral genes. Investigation of the interactions between S. islandicus type III-B CRISPR-Cas Cmr-α-related proteins and AcrIIIB2 reveals that the Acr does not bind to Csx1 but rather interacts with the Cmr-α effector complex. Furthermore, in vitro assays demonstrate that AcrIIIB2 can block the dissociation of cleaved target RNA from the Cmr-α complex, thereby inhibiting the Cmr-α turnover, thus preventing host cellular dormancy and further viral genome degradation by the type III-B CRISPR-Cas immunity.

AB - Despite a wide presence of type III clustered regularly interspaced short palindromic repeats, CRISPR-associated (CRISPR-Cas) in archaea and bacteria, very few anti-CRISPR (Acr) proteins inhibiting type III immunity have been identified, and even less is known about their inhibition mechanism. Here, we present the discovery of a type III CRISPR-Cas inhibitor, AcrIIIB2, encoded by Sulfolobus virus S. islandicus rod-shaped virus 3 (SIRV3). AcrIIIB2 inhibits type III-B CRISPR-Cas immune response to protospacers encoded in middle/late-expressed viral genes. Investigation of the interactions between S. islandicus type III-B CRISPR-Cas Cmr-α-related proteins and AcrIIIB2 reveals that the Acr does not bind to Csx1 but rather interacts with the Cmr-α effector complex. Furthermore, in vitro assays demonstrate that AcrIIIB2 can block the dissociation of cleaved target RNA from the Cmr-α complex, thereby inhibiting the Cmr-α turnover, thus preventing host cellular dormancy and further viral genome degradation by the type III-B CRISPR-Cas immunity.

KW - Acr inhibition mechanism

KW - anti-CRISPR

KW - CRISPR-Cas turnover

KW - type III CRISPR

U2 - 10.1016/j.chom.2023.10.003

DO - 10.1016/j.chom.2023.10.003

M3 - Journal article

C2 - 37909049

AN - SCOPUS:85175531148

VL - 31

SP - 1837-1849.e5

JO - Cell Host & Microbe

JF - Cell Host & Microbe

SN - 1931-3128

IS - 11

ER -

ID: 372810596