Yopj family effectors promote bacterial infection through a unique acetyltransferase activity

Ma, Ka Wai and Ma, Wenbo (2016) Yopj family effectors promote bacterial infection through a unique acetyltransferase activity. Microbiology and Molecular Biology Reviews, 80 (4). pp. 1011-1027. ISSN 1092-2172

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Abstract

Gram-negative bacterial pathogens rely on the type III secretion system to inject virulence proteins into host cells. These type III secreted "effector" proteins directly manipulate cellular processes to cause disease. Although the effector repertoires in different bacterial species are highly variable, the Yersinia outer protein J (YopJ) effector family is unique in that its members are produced by diverse animal and plant pathogens as well as a nonpathogenic microsymbiont. All YopJ family effectors share a conserved catalytic triad that is identical to that of the C55 family of cysteine proteases. However, an accumulating body of evidence demonstrates that many YopJ effectors modify their target proteins in hosts by acetylating specific serine, threonine, and/or lysine residues. This unique acetyltransferase activity allows the YopJ family effectors to affect the function and/or stability of their targets, thereby dampening innate immunity. Here, we summarize the current understanding of this prevalent and evolutionarily conserved type III effector family by describing their enzymatic activities and virulence functions in animals and plants. In particular, the molecular mechanisms by which representative YopJ family effectors subvert host immunity through posttranslational modification of their target proteins are discussed.

Item Type: Article
Additional Information: Publisher Copyright: © 2016, American Society for Microbiology. All Rights Reserved.
Uncontrolled Keywords: microbiology,molecular biology,infectious diseases,sdg 3 - good health and well-being ,/dk/atira/pure/subjectarea/asjc/2400/2404
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Depositing User: LivePure Connector
Date Deposited: 12 Sep 2022 12:30
Last Modified: 23 Sep 2022 02:53
URI: https://ueaeprints.uea.ac.uk/id/eprint/88151
DOI: 10.1128/MMBR.00032-16

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