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PreprintCited by 53Plant Pathogens and ResistancePlant-Microbe Interactions and ImmunityPlant Pathogenic Bacteria Studies

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Pathogen protein modularity enables elaborate mimicry of a host phosphatase

Open access
Li, Hui, Wang, Jinlong, Kuan, Tung Ariel, Tang, Bozeng, Feng, Li, Wang, Jiuyu, Cheng, Zhi, Skłenar, Jan, Derbyshire, Paul, Hulin, Michelle, Li, Yufei, Zhai, Yi, Hou, Yingnan, Menke, Frank L.H., Wang, Yanli, Ma, Wenbo·2023·Cell
DOI 10.1101/2023.05.05.539533

Preprint — published as 10.1016/j.cell.2023.05.049 · Paper page

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Abstract

SUMMARY: Pathogens produce diverse effector proteins to manipulate host cellular processes. However, how functional diversity is generated in an effector repertoire is poorly understood. Many effectors in the devastating plant pathogen Phytophthora contain tandem repeats of the “(L)WY” motif, which are structurally conserved but variable in sequences. Here, we discovered a functional module formed by a specific (L)WY-LWY combination in multiple Phytophthora effectors, which efficiently recruit the Serine/Threonine protein phosphatase 2A (PP2A) core enzyme in plant hosts. Crystal structure of an effector-PP2A complex shows that the (L)WY-LWY module enables hijacking of the host PP2A core enzyme to form functional holoenzymes. While sharing the PP2A-interacting module at the amino terminus, these effectors possess divergent C-terminal LWY units and regulate distinct sets of phosphoproteins in the host. Our results highlight the appropriation of an essential host phosphatase through molecular mimicry by pathogens and diversification promoted by protein modularity in an effector repertoire.

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Metadata

Authors
Li, H., Wang, J., Kuan, T. A., Tang, B., Feng, L., Wang, J., Cheng, Z., Skłenar, J., Derbyshire, P., Hulin, M., Li, Y., Zhai, Y., Hou, Y., Menke, F. L. H., Wang, Y., & Ma, W.
Affiliations
  • University of East Anglia (GB)
  • Chinese Academy of Sciences (CN)
  • University of California, Riverside (US)
Corresponding author
Ma, Wenbo
ORCID
Venue
Cell
Publisher
openRxiv
Published
2023-05-05
Volume
186
Issue
15
Pages
3196-3207.e17
ISSN
0092-8674 (ISSN-L)
DOI
10.1101/2023.05.05.539533
OpenAlex
W4382139037
Cited by
53
References
1
Citations by year
2026: 12 · 2025: 21 · 2024: 12 · 2023: 8
FWCI
8.33
Type
journal article
Language
en
Open access
Licence
cc-by-nc-nd
Locations
  • Cell (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • SSRN Electronic Journal (acceptedVersion)
  • PubMed (publishedVersion)
  • UEA Digital Repository (University of East Anglia) (acceptedVersion)
Funders
  • National Science Foundation (1758889)
  • U.S. Department of Agriculture
  • UK Research and Innovation (BBS/E/J/000PR9797)
  • Gatsby Charitable Foundation
  • National Natural Science Foundation of China (31930065, 32071444, 22121003, 31630015, 32071198, 31725008, 91940302)
  • Chinese Academy of Sciences (XDB37010202)
  • Ministry of Science and Technology of the People's Republic of China (2017YFA0504203)
  • National Institute of Food and Agriculture (2018-67014-28488)
  • Biotechnology and Biological Sciences Research Council (BBS/E/JI/230001B, BB/W016788/1, BBS/E/J/000PR9797)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Pathogens and Resistance
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant-Microbe Interactions and Immunity
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Pathogenic Bacteria Studies
Keywords
protein phosphatase 2A
MeSH terms
Phosphoric Monoester Hydrolases, Phytophthora, Plant Diseases, Plants, Protein Processing, Post-Translational, Proteins, Protein Phosphatase 2

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