YopJ Family Effectors Promote Bacterial Infection through a Unique Acetyltransferase Activity

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.

Advances on Vibrio parahaemolyticus research in the postgenomic era

“…YopJ of Yersinia spp. inhibits the mitogen‐activated protein kinase (MAPK) and nuclear factor kappa B (NF‐κB) signaling pathways by acetylating MAPK kinases (MKKs) . Interestingly, VopA/P inhibits MAPK but does not affect NF‐κB signaling .…”

“…inhibits the mitogenactivated protein kinase (MAPK) and nuclear factor kappa B (NF-κB) signaling pathways by acetylating MAPK kinases (MKKs). 96,97 Interestingly, VopA/P inhibits MAPK but does not affect NF-κB signaling. 90 Both YopJ and VopA/P acetylate three residues in the activation loop of MKK6 to block phosphorylation.…”

Analysis of the ZAR1 Immune Complex Reveals Determinants for Immunity and Molecular Interactions

“…AtZAR1 was first identified as being required for the recognition of the T3SE HopZ1a from the pathogenic bacteria P. syringae (Lewis et al, 2010). HopZ1a is part of the YopJ superfamily of T3SEs that are found in animal and plant pathogenic bacteria and is an acetyltransferase (Lewis et al, 2008(Lewis et al, , 2011Lee et al, 2012;Ma and Ma, 2016). Detection of HopZ1a by AtZAR1 requires AtZED1 (HOPZ-ETI-DEFICIENT1), a receptorlike cytoplasmic kinase (RLCK) belonging to the RLCK XII-2 family (Lewis et al, 2013).…”

Perturbations of a Kinase-Pseudokinase Module Activate Plant Immunity

“…HopZ1a is a member of a large and diverse family of bacterial effector proteins with similarity to the YopJ effector from Y. pestis . YopJ-like effectors are produced by a variety of pathogens of both plants and animals, and even among P. syringae strains there are five recognized distinct lineages of HopZ effectors (HopZ1 through HopZ5) [58,59]. This inter-allelic sequence variation confers significant functional differences, since only HopZ1a is capable of inducing ETI in Arabidopsis .…”