E3 ubiquitin ligases and plant innate immunity

Craig, A.; Ewan, Richard; Mesmar, Joelle; Gudipati, Venugopal; Sadanandom, Ari

doi:10.1093/jxb/erp059

Cited by 143 publications

(113 citation statements)

References 63 publications

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“…Recent reports reveal that the UPP is closely related to several immunologic processes, such as regulation of immune response and induction of inflammatory response (6,8,19). Yeast cells lacking the E2 enzymes (Ubc4 and Ubc5) have an increased sensitivity to stress conditions, which is consistent with the demand of E2 for stress tolerance (2).…”

mentioning

confidence: 58%

Enzyme E2 from Chinese White Shrimp Inhibits Replication of White Spot Syndrome Virus and Ubiquitinates Its RING Domain Proteins

Chen

Wang

Zhao

et al. 2011

J Virol

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Recent studies have shown that the ubiquitin (Ub) proteasome pathway (UPP) is closely related to immune defense. We have identified a ubiquitin-conjugating enzyme, E2, from the Chinese white shrimp, Fenneropenaeus chinensis (FcUbc). Injection of recombinant FcUbc protein (rFcUbc) reduced the mortality of shrimp infected with white spot syndrome virus (WSSV) and inhibited replication of WSSV. rFcUbc, but not a mutant FcUbc (mFcUbc), bound to WSSV RING domains (WRDs) from four potential E3 ligase proteins of WSSV in vitro. Importantly, rFcUbc could ubiquitinate the RING domains (named WRD2 and WRD3) of WSSV277 and WSSV304 proteins in vitro and the two proteins in WSSV-infected Drosophila melanogaster Schneider 2 (S2) cells. Furthermore, overexpression of FcUbc increased ubiquitination of WSSV277 and WSSV304 during WSSV infection. In summary, our study demonstrates that FcUbc from Chinese white shrimp inhibited WSSV replication and could ubiquitinate WSSV RING domain-containing proteins. This is the first report about antiviral function of Ubc E2 in shrimp.

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mentioning

confidence: 58%

Enzyme E2 from Chinese White Shrimp Inhibits Replication of White Spot Syndrome Virus and Ubiquitinates Its RING Domain Proteins

Chen

Wang

Zhao

et al. 2011

J Virol

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“…27 This is consistent with suggestions on the involvement of ubiquitination in disease resistance. 32,33 Proteasome-dependent degradation of some factor might trigger membrane fusion, followed by the discharge of vacuolar contents for the purpose of attacking bacteria (Figure 2a).…”

Section: Non-destructive Versus Destructive Vacuole-mediated Cell Deathmentioning

confidence: 99%

The role of vacuole in plant cell death

2011

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Almost all plant cells have large vacuoles that contain both hydrolytic enzymes and a variety of defense proteins. Plants use vacuoles and vacuolar contents for programmed cell death (PCD) in two different ways: for a destructive way and for a nondestructive way. Destruction is caused by vacuolar membrane collapse, followed by the release of vacuolar hydrolytic enzymes into the cytosol, resulting in rapid and direct cell death. The destructive way is effective in the digestion of viruses proliferating in the cytosol, in susceptible cell death induced by fungal toxins, and in developmental cell death to generate integuments (seed coats) and tracheary elements. On the other hand, the non-destructive way involves fusion of the vacuolar and the plasma membrane, which allows vacuolar defense proteins to be discharged into the extracellular space where the bacteria proliferate. Membrane fusion, which is normally suppressed, was triggered in a proteasome-dependent manner. Intriguingly, both ways use enzymes with caspase-like activity; the membrane-fusion system uses proteasome subunit PBA1 with caspase-3-like activity, and the vacuolar-collapse system uses vacuolar processing enzyme (VPE) with caspase-1-like activity. This review summarizes two different ways of vacuole-mediated PCD and discusses how plants use them to attack pathogens that invade unexpectedly.

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“…The ubiquitin-proteasome-dependent pathway is involved in the response of plants to most environmental modifications and stresses, including plant-pathogen interactions (Craig et al 2009;Dielen et al 2010). Recent advances in hormone signaling research have uncovered a common strategy in which proteasome-mediated degradation complexes are central for the transmission of hormonal signals in plant defense responses (Chini et al 2009).…”

Section: Compared With Single Infections Co-infection Of Nicotiana Bmentioning

confidence: 99%

Comparative Analysis of Transcriptomic and Hormonal Responses to Compatible and Incompatible Plant-Virus Interactions that Lead to Cell Death

Pacheco¹,

García-Marcos²,

Manzano³

et al. 2012

MPMI

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Hypersensitive response-related programmed cell death (PCD) has been extensively analyzed in various plantvirus interactions. However, little is known about the changes in gene expression and phytohormone levels associated with cell death caused by compatible viruses. The synergistic interaction of Potato virus X (PVX) with a number of Potyvirus spp. results in increased symptoms that lead to systemic necrosis (SN) in Nicotiana benthamiana. Here, we show that SN induced by a PVX recombinant virus expressing a potyviral helper componentproteinase (HC-Pro) gene is associated with PCD. We have also compared transcriptomic and hormonal changes that occur in response to a compatible synergistic virus interaction that leads to SN, a systemic incompatible interaction conferred by the Tobacco mosaic virus-resistance gene N, and a PCD response conditioned by depletion of proteasome function. Our analysis indicates that the SN response clusters with the incompatible response by the similarity of their overall gene expression profiles. However, the expression profiles of both defense-related genes and hormone-responsive genes, and also the relative accumulation of several hormones in response to SN, relate more closely to the response to depletion of proteasome function than to that elicited by the incompatible interaction. This suggests a potential contribution of proteasome dysfunction to the increased pathogenicity observed in PVX-Potyvirus mixed infections. Furthermore, silencing of coronatine insensitive 1, a gene involved in jasmonate perception, in N. benthamiana accelerated cell death induced by PVX expressing HC-Pro.

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E3 ubiquitin ligases and plant innate immunity

Cited by 143 publications

References 63 publications

Enzyme E2 from Chinese White Shrimp Inhibits Replication of White Spot Syndrome Virus and Ubiquitinates Its RING Domain Proteins

Enzyme E2 from Chinese White Shrimp Inhibits Replication of White Spot Syndrome Virus and Ubiquitinates Its RING Domain Proteins

The role of vacuole in plant cell death

Comparative Analysis of Transcriptomic and Hormonal Responses to Compatible and Incompatible Plant-Virus Interactions that Lead to Cell Death

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