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Article ; Online: Transmembrane substrates of type three secretion system injectisomes.

Godlee, Camilla / Holden, David W

2023 Volume 169, Issue 1

Abstract: The type three secretion system injectisome of Gram-negative bacterial pathogens injects virulence proteins, called effectors, into host cells. Effectors of mammalian pathogens carry out a range of functions enabling bacterial invasion, replication, ... ...

Abstract	The type three secretion system injectisome of Gram-negative bacterial pathogens injects virulence proteins, called effectors, into host cells. Effectors of mammalian pathogens carry out a range of functions enabling bacterial invasion, replication, immune suppression and transmission. The injectisome secretes two translocon proteins that insert into host cell membranes to form a translocon pore, through which effectors are delivered. A subset of effectors also integrate into infected cell membranes, enabling a unique range of biochemical functions. Both translocon proteins and transmembrane effectors avoid cytoplasmic aggregation and integration into the bacterial inner membrane. Translocated transmembrane effectors locate and integrate into the appropriate host membrane. In this review, we focus on transmembrane translocon proteins and effectors of bacterial pathogens of mammals. We discuss what is known about the mechanisms underlying their membrane integration, as well as the functions conferred by the position of injectisome effectors within membranes.
MeSH term(s)	Animals ; Type III Secretion Systems/genetics ; Type III Secretion Systems/metabolism ; Cell Membrane/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Virulence ; Gram-Negative Bacteria/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Mammals/metabolism
Chemical Substances	Type III Secretion Systems ; Membrane Proteins ; Bacterial Proteins
Language	English
Publishing date	2023-01-28
Publishing country	England
Document type	Review ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.001292
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Article ; Online: Editorial: Single cell analysis of bacteria-host interaction.

Cerny, Ondrej / Godlee, Camilla / Lobato-Márquez, Damián

Frontiers in cellular and infection microbiology

2023 Volume 13, Page(s) 1196905

MeSH term(s)	Bacteria ; Host Microbial Interactions ; Single-Cell Analysis
Language	English
Publishing date	2023-04-21
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2023.1196905
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Article: A genome-wide CRISPR screen identifies host proteins required for depletion of surface MHCII by Salmonella

Alix, Eric / Tocci, Romina / Blundell, Lisa / Matthews, Sophie / Godlee, Camilla / Cerny, Ondrej / Holden, David

Molecular immunology. 2022 Oct., v. 150

2022

Abstract: Systemic infections caused by Salmonella enterica are largely controlled by activation of CD4 T cells. Dendritic cells phagocytose bacteria in the small intestine and present antigens to CD4 T cells via MHCII. Salmonella enterica serovar Typhimurium ... ...

Abstract	Systemic infections caused by Salmonella enterica are largely controlled by activation of CD4 T cells. Dendritic cells phagocytose bacteria in the small intestine and present antigens to CD4 T cells via MHCII. Salmonella enterica serovar Typhimurium impairs MHCII presentation by infected dendritic cells. We recently identified SteD, a bacterial virulence protein that is translocated into host cells by the SPI-2 type 3 secretion system, as required and sufficient for this activity (Bayer-Santos et al., 2016). Although SteD interacts with MHCII, its mechanism of action was unclear. Using a genome-wide CRISPR Knock-Out screen of Mel Juso cells expressing SteD, we identified two host proteins involved in SteD-dependent depletion of mature MHCII (mMHCII) from the cell surface. One is WWP2, an E3 ligase belonging to the Nedd4 family. The second is TMEM127, a transmembrane protein, which interacts with both WWP2 and SteD. We propose that SteD recruits WWP2 via TMEM127, resulting in ubiquitination of mMHCII. Ubiquitination of mMHCII by this mechanism involves mostly K63-linked chains and leads to its lysosomal degradation. Remarkably, we found that SteD is itself ubiquitinated by the same mechanism and this modification is important for SteD function. This study reveals how Salmonella enterica promotes immune escape by redirecting the activity of host proteins.
Keywords	Salmonella Typhimurium ; immunology ; mechanism of action ; small intestine ; transmembrane proteins ; type III secretion system ; ubiquitin-protein ligase ; ubiquitination ; virulence
Language	English
Dates of publication	2022-10
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2022.05.031
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: The Salmonella transmembrane effector SteD hijacks AP1-mediated vesicular trafficking for delivery to antigen-loading MHCII compartments.

Godlee, Camilla / Cerny, Ondrej / Liu, Mei / Blundell, Samkeliso / Gallagher, Alanna E / Shahin, Meriam / Holden, David W

PLoS pathogens

2022 Volume 18, Issue 5, Page(s) e1010252

Abstract: SteD is a transmembrane effector of the Salmonella SPI-2 type III secretion system that inhibits T cell activation by reducing the amounts of at least three proteins -major histocompatibility complex II (MHCII), CD86 and CD97 -from the surface of antigen- ...

Abstract	SteD is a transmembrane effector of the Salmonella SPI-2 type III secretion system that inhibits T cell activation by reducing the amounts of at least three proteins -major histocompatibility complex II (MHCII), CD86 and CD97 -from the surface of antigen-presenting cells. SteD specifically localises at the trans-Golgi network (TGN) and MHCII compartments; however, the targeting, membrane integration and trafficking of SteD are not understood. Using systematic mutagenesis, we identify distinct regions of SteD that are required for these processes. We show that SteD integrates into membranes of the ER/Golgi through a two-step mechanism of membrane recruitment from the cytoplasm followed by integration. SteD then migrates to and accumulates within the TGN. From here it hijacks the host adaptor protein (AP)1-mediated trafficking pathway from the TGN to MHCII compartments. AP1 binding and post-TGN trafficking require a short sequence in the N-terminal cytoplasmic tail of SteD that resembles the AP1-interacting dileucine sorting signal, but in inverted orientation, suggesting convergent evolution.
MeSH term(s)	Major Histocompatibility Complex ; Protein Transport ; Salmonella/metabolism ; Type III Secretion Systems/metabolism ; trans-Golgi Network/metabolism
Chemical Substances	Type III Secretion Systems
Language	English
Publishing date	2022-05-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010252
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Article ; Online: SrcA is a chaperone for the Salmonella SPI-2 type three secretion system effector SteD.

Godlee, Camilla / Cerny, Ondrej / Durkin, Charlotte H / Holden, David W

Microbiology (Reading, England)

2018 Volume 165, Issue 1, Page(s) 15–25

Abstract: Effector proteins of type three secretion systems (T3SS) often require cytosolic chaperones for their stabilization, to interact with the secretion machinery and to enable effector delivery into host cells. We found that deletion of srcA, previously ... ...

Abstract	Effector proteins of type three secretion systems (T3SS) often require cytosolic chaperones for their stabilization, to interact with the secretion machinery and to enable effector delivery into host cells. We found that deletion of srcA, previously shown to encode a chaperone for the Salmonella pathogenicity island 2 (SPI-2) T3SS effectors SseL and PipB2, prevented the reduction of mature Major Histocompatibility Complex class II (mMHCII) from the surface of antigen-presenting cells during Salmonella infection. This activity was shown previously to be caused by the SPI-2 T3SS effector SteD. Since srcA and steD are located in the same operon on the Salmonella chromosome, this suggested that the srcA phenotype might be due to an indirect effect on SteD. We found that SrcA is not translocated by the SPI-2 T3SS but interacts directly and forms a stable complex with SteD in bacteria with a 2 : 1 stoichiometry. We found that SrcA was not required for SPI-2 T3SS-dependent, neutral pH-induced secretion of either SseL or PipB2 but was essential for secretion of SteD. SrcA therefore functions as a chaperone for SteD, explaining its requirement for the reduction in surface levels of mMHCII.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Genomic Islands ; Humans ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Operon ; Protein Transport ; Salmonella Infections/microbiology ; Salmonella typhimurium/genetics ; Salmonella typhimurium/metabolism ; Type III Secretion Systems/genetics ; Type III Secretion Systems/metabolism
Chemical Substances	Bacterial Proteins ; Molecular Chaperones ; SteD protein, Salmonella typhimurium ; Type III Secretion Systems
Language	English
Publishing date	2018-11-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.000732
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Article ; Online: CD97 stabilises the immunological synapse between dendritic cells and T cells and is targeted for degradation by the Salmonella effector SteD.

Cerny, Ondrej / Godlee, Camilla / Tocci, Romina / Cross, Nancy E / Shi, Haoran / Williamson, James C / Alix, Eric / Lehner, Paul J / Holden, David W

PLoS pathogens

2021 Volume 17, Issue 7, Page(s) e1009771

Abstract: The Salmonella enterica effector SteD depletes mature MHC class II (mMHCII) molecules from the surface of infected antigen-presenting cells through ubiquitination of the cytoplasmic tail of the mMHCII β chain. This requires the Nedd4 family HECT E3 ... ...

Abstract	The Salmonella enterica effector SteD depletes mature MHC class II (mMHCII) molecules from the surface of infected antigen-presenting cells through ubiquitination of the cytoplasmic tail of the mMHCII β chain. This requires the Nedd4 family HECT E3 ubiquitin ligase Wwp2 and a tumor-suppressing transmembrane protein adaptor Tmem127. Here, through a proteomic screen of dendritic cells, we found that SteD targets the plasma membrane protein CD97 for degradation by a similar mechanism. SteD enhanced ubiquitination of CD97 on K555 and mutation of this residue eliminated the effect of SteD on CD97 surface levels. We showed that CD97 localises to and stabilises the immunological synapse between dendritic cells and T cells. Removal of CD97 by SteD inhibited dendritic cell-T cell interactions and reduced T cell activation, independently of its effect on MHCII. Therefore, SteD suppresses T cell immunity by two distinct processes.
MeSH term(s)	Animals ; Antigen Presentation/immunology ; Bacterial Proteins/metabolism ; Dendritic Cells/immunology ; Immunological Synapses/immunology ; Lymphocyte Activation/immunology ; Mice ; Mice, Inbred C57BL ; Receptors, G-Protein-Coupled/immunology ; Salmonella Infections/metabolism ; Salmonella enterica ; T-Lymphocytes/immunology
Chemical Substances	Adgre5 protein, mouse ; Bacterial Proteins ; Receptors, G-Protein-Coupled ; SteD protein, Salmonella typhimurium
Language	English
Publishing date	2021-07-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1009771
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Article ; Online: Review series: From uncertain beginnings: initiation mechanisms of clathrin-mediated endocytosis.

Godlee, Camilla / Kaksonen, Marko

The Journal of cell biology

2013 Volume 203, Issue 5, Page(s) 717–725

Abstract: Clathrin-mediated endocytosis is a central and well-studied trafficking process in eukaryotic cells. How this process is initiated is likely to be a critical point in regulating endocytic activity spatially and temporally, but the underlying mechanisms ... ...

Abstract	Clathrin-mediated endocytosis is a central and well-studied trafficking process in eukaryotic cells. How this process is initiated is likely to be a critical point in regulating endocytic activity spatially and temporally, but the underlying mechanisms are poorly understood. During the early stages of endocytosis three components-adaptor and accessory proteins, cargo, and lipids-come together at the plasma membrane to begin the formation of clathrin-coated vesicles. Although different models have been proposed, there is still no clear picture of how these three components cooperate to initiate endocytosis, which may indicate that there is some flexibility underlying this important event.
MeSH term(s)	Biological Transport/physiology ; Clathrin-Coated Vesicles/physiology ; Endocytosis/physiology ; Models, Biological ; Phosphatidylinositol 4,5-Diphosphate/physiology
Chemical Substances	Phosphatidylinositol 4,5-Diphosphate
Language	English
Publishing date	2013-12-10
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201307100
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Article ; Online: The Tumour Suppressor TMEM127 Is a Nedd4-Family E3 Ligase Adaptor Required by Salmonella SteD to Ubiquitinate and Degrade MHC Class II Molecules.

Alix, Eric / Godlee, Camilla / Cerny, Ondrej / Blundell, Samkeliso / Tocci, Romina / Matthews, Sophie / Liu, Mei / Pruneda, Jonathan N / Swatek, Kirby N / Komander, David / Sleap, Tabitha / Holden, David W

Cell host & microbe

2020 Volume 28, Issue 1, Page(s) 54–68.e7

Abstract	The Salmonella enterica effector SteD depletes mature MHC class II (mMHCII) molecules from the surface of infected antigen-presenting cells through ubiquitination of the cytoplasmic tail of the mMHCII β chain. Here, through a genome-wide mutant screen of human antigen-presenting cells, we show that the NEDD4 family HECT E3 ubiquitin ligase WWP2 and a tumor-suppressing transmembrane protein of unknown biochemical function, TMEM127, are required for SteD-dependent ubiquitination of mMHCII. Although evidently not involved in normal regulation of mMHCII, TMEM127 was essential for SteD to suppress both mMHCII antigen presentation in mouse dendritic cells and MHCII-dependent CD4
MeSH term(s)	Animals ; Antigen Presentation ; Bacterial Proteins/physiology ; CRISPR-Cas Systems ; Cell Line ; Dendritic Cells/immunology ; Dendritic Cells/microbiology ; Female ; Histocompatibility Antigens Class II/metabolism ; Host-Pathogen Interactions ; Humans ; Lymphocyte Activation ; Membrane Proteins/physiology ; Mice ; Mice, Inbred C57BL ; Mutation ; Protein Binding ; Salmonella Infections/immunology ; Salmonella Infections/microbiology ; Salmonella typhimurium/physiology ; T-Lymphocytopenia, Idiopathic CD4-Positive/immunology ; T-Lymphocytopenia, Idiopathic CD4-Positive/microbiology ; Ubiquitin-Protein Ligases/physiology ; Ubiquitination ; Virulence
Chemical Substances	Bacterial Proteins ; Histocompatibility Antigens Class II ; Membrane Proteins ; SteD protein, Salmonella typhimurium ; TMEM127 protein, human ; WWP2 protein, human (EC 2.3.2.26) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2020-06-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2020.04.024
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Article ; Online: Quantification of cytosolic interactions identifies Ede1 oligomers as key organizers of endocytosis.

Boeke, Dominik / Trautmann, Susanne / Meurer, Matthias / Wachsmuth, Malte / Godlee, Camilla / Knop, Michael / Kaksonen, Marko

Molecular systems biology

2014 Volume 10, Page(s) 756

Abstract: Clathrin-mediated endocytosis is a highly conserved intracellular trafficking pathway that depends on dynamic protein-protein interactions between up to 60 different proteins. However, little is known about the spatio-temporal regulation of these ... ...

Abstract	Clathrin-mediated endocytosis is a highly conserved intracellular trafficking pathway that depends on dynamic protein-protein interactions between up to 60 different proteins. However, little is known about the spatio-temporal regulation of these interactions. Using fluorescence (cross)-correlation spectroscopy in yeast, we tested 41 previously reported interactions in vivo and found 16 to exist in the cytoplasm. These detected cytoplasmic interactions included the self-interaction of Ede1, homolog of mammalian Eps15. Ede1 is the crucial scaffold for the organization of the early stages of endocytosis. We show that oligomerization of Ede1 through its central coiled coil domain is necessary for its localization to the endocytic site and we link the oligomerization of Ede1 to its function in locally concentrating endocytic adaptors and organizing the endocytic machinery. Our study sheds light on the importance of the regulation of protein-protein interactions in the cytoplasm for the assembly of the endocytic machinery in vivo.
MeSH term(s)	Cytosol/physiology ; Endocytosis ; Gene Expression Regulation, Fungal ; Genome, Fungal ; Protein Interaction Domains and Motifs ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Spectrometry, Fluorescence
Chemical Substances	Ede1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2014-11-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2193510-5
ISSN	1744-4292 ; 1744-4292
ISSN (online)	1744-4292
ISSN	1744-4292
DOI	10.15252/msb.20145422
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Article ; Online: The initiation of clathrin-mediated endocytosis is mechanistically highly flexible.

Brach, Thorsten / Godlee, Camilla / Moeller-Hansen, Iben / Boeke, Dominik / Kaksonen, Marko

Current biology : CB

2014 Volume 24, Issue 5, Page(s) 548–554

Abstract: Clathrin-mediated endocytosis is driven by a complex machinery of proteins, which assemble in a regular order at the plasma membrane. The assembly of the endocytic machinery is conventionally thought to be a continuous process of mechanistically ... ...

Abstract	Clathrin-mediated endocytosis is driven by a complex machinery of proteins, which assemble in a regular order at the plasma membrane. The assembly of the endocytic machinery is conventionally thought to be a continuous process of mechanistically dependent steps, starting from a defined initiation step. Indeed, several initiation mechanisms involving single proteins have been proposed in mammalian cells. Here, we demonstrate that the initiation mechanism of endocytosis is highly flexible. We disrupted the long early phase of endocytosis in yeast by deleting seven genes encoding early endocytic proteins. Surprisingly, membrane uptake and vesicle budding dynamics were largely normal in these mutant cells. Regulated cargo recruitment was, however, defective. In addition, different early endocytic proteins were able to initiate vesicle budding when anchored to a plasma membrane domain where endocytosis does not normally take place. Our results suggest that the cargo-recruiting early phase is not mechanistically required for vesicle budding, but early-arriving proteins can recruit the budding machinery into position at the plasma membrane. Separable early and late phases allow for a robust process of vesicle budding to follow from variable initiation mechanisms. Such a modular design could easily adapt and evolve to respond to different cellular requirements.
MeSH term(s)	Adaptor Proteins, Vesicular Transport/genetics ; Adaptor Proteins, Vesicular Transport/metabolism ; Clathrin/metabolism ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Endocytosis ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Molecular Imaging/methods ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism
Chemical Substances	ABP1 protein, S cerevisiae ; Adaptor Proteins, Vesicular Transport ; Clathrin ; Cytoskeletal Proteins ; ENT1 protein, S cerevisiae ; ENT2 protein, S cerevisiae ; Ede1 protein, S cerevisiae ; Microfilament Proteins ; SLA1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Vesicular Transport Proteins ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2014-03-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2014.01.048
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