The NEL Family of Bacterial E3 Ubiquitin Ligases

Bullones-Bolaños, Andrea; Bernal-Bayard, Joaquín; Ramos‐Morales, Francisco

doi:10.3390/ijms23147725

Cited by 19 publications

(24 citation statements)

References 238 publications

(358 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The genes encoding the NEL E3 ligases found in S. enterica have a complex phylogenetic distribution [ 55 ]. While slrP and sspH2 are common to most salmonellae, sspH1 has a more restricted dissemination [ 10 ] and is absent in some laboratory Typhimurium strains as well as in the better characterized strains of typhoidal Salmonella .…”

Section: Discussionmentioning

confidence: 99%

SNRPD2 Is a Novel Substrate for the Ubiquitin Ligase Activity of the Salmonella Type III Secretion Effector SlrP

Bullones-Bolaños

Araujo-Garrido

Fernández-García

et al. 2022

Biology

View full text Add to dashboard Cite

SlrP is a protein with E3 ubiquitin ligase activity that is translocated by Salmonella enterica serovar Typhimurium into eukaryotic host cells through a type III secretion system. A yeast two-hybrid screen was performed to find new human partners for this protein. Among the interacting proteins identified by this screen was SNRPD2, a core component of the spliceosome. In vitro ubiquitination assays demonstrated that SNRPD2 is a substrate for the catalytic activity of SlrP, but not for other members of the NEL family of E3 ubiquitin ligases, SspH1 and SspH2. The lysine residues modified by this activity were identified by mass spectrometry. The identification of a new ubiquitination target for SlrP is a relevant contribution to the understanding of the role of this Salmonella effector.

show abstract

Section: Discussionmentioning

confidence: 99%

SNRPD2 Is a Novel Substrate for the Ubiquitin Ligase Activity of the Salmonella Type III Secretion Effector SlrP

Bullones-Bolaños

Araujo-Garrido

Fernández-García

et al. 2022

Biology

View full text Add to dashboard Cite

show abstract

“…While SspH1 and SspH2 share 69 % amino acid sequence similarity, their localization and interaction partners suggest they induce divergent cellular effects in host cells [11,90]. SspH1 is translocated by both the SPI-1 and SPI-2 T3SSs and is localized to the nucleus while SspH2, delivered by the SPI-2 T3SS, migrates to the apical surface of epithelial cells [11,91,92]. SspH1 interacts with the serine/threonine protein kinase N1 (PKN1) through its N terminal LRR domain, with SspH1-mediated ubiquitylation targeting PKN1 for proteasomal degradation [93,94] (Fig.…”

Section: Ssph1 and Ssph2 And Their Divergent Targetsmentioning

confidence: 99%

“…In addition to Salmonella , LRR–NEL-containing proteins, referred to as the IpaH family, occur in the gastrointestinal pathogens Shigella and enteroinvasive E. coli (EIEC) [91, 98, 105, 106]. Some of these have distinct functions, with IpaH9.8 targeting members of the interferon-induced GTPase family of guanylate-binding proteins (GBPs), subverting their function to promote Shigella motility and cell-to-cell spread [107].…”

Section: Biochemical Modification Of Host Proteins By Salmonella ...mentioning

confidence: 99%

Speaking the host language: how Salmonella effector proteins manipulate the host

Pillay,

Hettiarachchi,

Gan

et al. 2023

Microbiology

View full text Add to dashboard Cite

Salmonella injects over 40 virulence factors, termed effectors, into host cells to subvert diverse host cellular processes. Of these 40 Salmonella effectors, at least 25 have been described as mediating eukaryotic-like, biochemical post-translational modifications (PTMs) of host proteins, altering the outcome of infection. The downstream changes mediated by an effector’s enzymatic activity range from highly specific to multifunctional, and altogether their combined action impacts the function of an impressive array of host cellular processes, including signal transduction, membrane trafficking, and both innate and adaptive immune responses. Salmonella and related Gram-negative pathogens have been a rich resource for the discovery of unique enzymatic activities, expanding our understanding of host signalling networks, bacterial pathogenesis as well as basic biochemistry. In this review, we provide an up-to-date assessment of host manipulation mediated by the Salmonella type III secretion system injectosome, exploring the cellular effects of diverse effector activities with a particular focus on PTMs and the implications for infection outcomes. We also highlight activities and functions of numerous effectors that remain poorly characterized.

show abstract

“…Similarly, the potato cyst nematode effector RHA1B suppresses ETI via E3‐dependent degradation of NLRs (Kud et al., 2019). Interestingly, the invasive plasmid antigen H (IpaH) family of effectors found in animal‐pathogenic, commensal and plant‐pathogenic bacteria encode a novel E3 ligase (NEL), primarily in the Salmonella , Shigella , Sinorhizobium and Ralstonia genera (Bullones‐Bolaños et al., 2022). NEL effectors typically comprise an N‐terminal leucine‐rich repeat (LRR) and a C‐terminal α‐helical catalytic domain, but no LRR motif has been reported in Ralstonia NEL‐type T3Es (Bullones‐Bolaños et al., 2022; Cheng et al., 2021; Nakano et al., 2017).…”

Section: Introductionmentioning

confidence: 99%

The Ralstonia solanacearum effector RipV1 acts as a novel E3 ubiquitin ligase to suppress plant PAMP‐triggered immunity responses and promote susceptibility in potato

Cheng,

Zhou,

Wang

et al. 2024

Plant Pathology

View full text Add to dashboard Cite

Bacterial wilt caused by Ralstonia solanacearum is a destructive plant disease, particularly in potato (Solanum tuberosum). R. solanacearum deploys a diverse and potent arsenal of type III effectors to inhibit the plant immune system. However, the understanding of individual effectors promoting susceptibility in host plants and interfering with plant immunity responses is still limited. Here, we demonstrated that the type III effector RipV1 functioned as a novel E3 ubiquitin ligase (NEL) effector and exhibited E3 ubiquitin ligase activity in vitro. Transient expression of RipV1 suppressed plant pathogen‐associated molecular pattern (PAMP)‐triggered immunity (PTI) responses in Nicotiana benthamiana, such as the expression of PTI‐related genes and the reactive oxygen species (ROS) burst. Prolonged expression of RipV1 induced cell death in N. benthamiana leaves. Notably, mutating the conserved cysteine residue of RipV1 abolished its E3 ligase activity and its ability to suppress plant PTI responses. This study also revealed the indispensability of RipV1 for R. solanacearum's full virulence in potato. Transgenic potato plants overexpressing ripV1 but not the catalytic mutant ripV1‐C444A displayed enhanced susceptibility to R. solanacearum. RipV1 was observed to localize specifically to the plant plasma membrane, with its N‐terminus being pivotal in determining this localization. These findings showcase that RipV1 acts as a NEL effector and contributes to R. solanacearum virulence by suppressing plant PTI responses through its E3 activity.

show abstract

The NEL Family of Bacterial E3 Ubiquitin Ligases

Cited by 19 publications

References 238 publications

SNRPD2 Is a Novel Substrate for the Ubiquitin Ligase Activity of the Salmonella Type III Secretion Effector SlrP

SNRPD2 Is a Novel Substrate for the Ubiquitin Ligase Activity of the Salmonella Type III Secretion Effector SlrP

Speaking the host language: how Salmonella effector proteins manipulate the host

The Ralstonia solanacearum effector RipV1 acts as a novel E3 ubiquitin ligase to suppress plant PAMP‐triggered immunity responses and promote susceptibility in potato

Contact Info

Product

Resources

About