Evidence map›Paper›PMID 37398474›Full record

ArticlebioRxiv : the preprint server for biology2023

Phage anti-CBASS protein simultaneously sequesters cyclic trinucleotides and dinucleotides.

Xueli Cao, Yu Xiao, Erin Huiting, Xujun Cao, Dong Li, Jie Ren, Linlin Guan, Yu Wang, Lingyin Li, Joseph Bondy-Denomy and 1 more

Open access · greenAbstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 7 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 2 countries.

Xueli CaoBeijing Advanced Innovation Center for Soft Matter Science and Engineering, State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China.
Yu XiaoMinistry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Tsinghua-Peking Center for Life Sciences, Beijing 100084, China.
Erin HuitingDepartment of Microbiology and Immunology, University of California, San Francisco, San Francisco, CA, 94158, USA.
Xujun CaoDepartment of Chemistry, Stanford University, Stanford, CA, 94305, USA.
Dong LiBeijing Advanced Innovation Center for Soft Matter Science and Engineering, State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China.
Jie RenState Key Laboratory for Biology of Plant Diseases and Insect Pests, Ministry of Agriculture, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Linlin GuanBeijing Advanced Innovation Center for Soft Matter Science and Engineering, State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China.
Yu WangBeijing Advanced Innovation Center for Soft Matter Science and Engineering, State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China.
Lingyin LiDepartment of Biochemistry, Stanford University, Stanford, CA, 94305, USA.
Joseph Bondy-DenomyDepartment of Microbiology and Immunology, University of California, San Francisco, San Francisco, CA, 94158, USA.
Yue FengBeijing Advanced Innovation Center for Soft Matter Science and Engineering, State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China.
Beijing University of Chemical Technology · CNPalo Alto Institute · USUniversity of California, San Francisco · USCenter for Life Sciences · CNInstitute of Plant Protection · CN

Funding

Uncovering the mechanism and role of a widespread anti-CRISPR-Cas9 proteinR01GM127489 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BONDY-DENOMY, JOSEPH · 2018 to 2022
$1.7M
Identifying the mechanism of bacteriophage detection by cyclic-oligonucleotide signaling systemsR21AI168811 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BONDY-DENOMY, JOSEPH · 2022 to 2023
$444k
NIAID NIH HHS R21 AI168811NIGMS NIH HHS R01 GM127489
6 · The paper itself

Abstract

CBASS is a common anti-phage immune system that uses cyclic oligonucleotide signals to activate effectors and limit phage replication. In turn, phages encode anti-CBASS (Acb) proteins. We recently uncovered a widespread phage anti-CBASS protein Acb2 that acts as a "sponge" by forming a hexamer complex with three cGAMP molecules. Here, we identified that Acb2 binds and sequesters many CBASS and cGAS-produced cyclic dinucleotides

Identifiers

PMID37398474
PMCPMC10312549
OpenAlexW4379157420

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.