Autophagy Induction by the Pathogen Receptor CD46

Joubert, Pierre-Emmanuel; Meiffren, Grégory; Grégoire, Isabel Pombo; Pontini, Guillemette; Richetta, Clémence; Flacher, Monique; Azocar, Olga; Vidalain, Pierre‐Olivier; Vidal, Marc; Lotteau, Vincent; Codogno, Patrice; Rabourdin–Combe, Chantal; Faure, Mathias

doi:10.1016/j.chom.2009.09.006

Cited by 228 publications

(241 citation statements)

References 59 publications

(78 reference statements)

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“…Among the latter, CD46, a complement regulatory protein, has been reported to induce autophagy upon engagement, and seems to facilitate the entrance of opLM into HeLa cells. 44 These results indicate that the VSIG4 signal alone is potent enough to induce autophagosome formation.…”

Section: Discussionmentioning

confidence: 63%

Extracellular stimulation of VSIG4/complement receptor Ig suppresses intracellular bacterial infection by inducing autophagy

et al. 2016

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VSIG4/CRIg (V-set and immunoglobulin domain containing 4) is a transmembrane receptor of the immunoglobulin superfamily that is expressed specifically on macrophages and mature dendritic cells. VSIG4 signaling accelerates phagocytosis of C3-opsonized bacteria, thereby efficiently clearing pathogens within macrophages. We found that VSIG4 signaling triggered by C3-opsonized Listeria (opLM) or by agonistic anti-VSIG4 monoclonal antibody (mAb) induced macrophages to form autophagosomes. VSIG4-induced autophagosomes were selectively colocalized with the intracellular LM while starvation-induced autophagosomes were not. Consistent with these results, the frequency of autophagosomes induced by infection with opLM was lower in VSIG4-deficient bone marrow-derived macrophages (BMDMs) than in WT BMDMs. Furthermore, when VSIG4 molecules were overexpressed in HeLa cells, which are nonmacrophage cells, VSIG4 triggering led to efficient uptake of LM, autophagosome formation, and killing of the infected LM. These findings suggest that VSIG4 signaling not only promotes rapid phagocytosis and killing of C3-opsonized intracellular bacteria, as previously reported, but also induces autophagosome formation, eliminating the LM that have escaped from phagosomes. We conclude that VSIG4 signaling provides an anti-immune evasion mechanism that prevents the outgrowth of intracellular bacteria in macrophages.

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Section: Discussionmentioning

confidence: 63%

Extracellular stimulation of VSIG4/complement receptor Ig suppresses intracellular bacterial infection by inducing autophagy

et al. 2016

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“…40 Another example includes the pathogen receptor CD46 that binds Streptococci and triggers autophagy. 41 Thus, these two examples provide evidence that pathogen recognition in different animal systems is directly linked to higher levels of autophagic activity.…”

Section: Autophagy In Immunitymentioning

confidence: 99%

Role of autophagy in disease resistance and hypersensitive response-associated cell death

Hofius

Munch²,

Bressendorff³

et al. 2011

Cell Death Differ

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Ancient autophagy pathways are emerging as key defense modules in host eukaryotic cells against microbial pathogens. Apart from actively eliminating intracellular intruders, autophagy is also responsible for cell survival, for example by reducing the deleterious effects of endoplasmic reticulum stress. At the same time, autophagy can contribute to cellular suicide. The concurrent engagement of autophagy in these processes during infection may sometimes mask its contribution to differing pro-survival and pro-death decisions. The importance of autophagy in innate immunity in mammals is well documented, but how autophagy contributes to plant innate immunity and cell death is not that clear. A few research reports have appeared recently to shed light on the roles of autophagy in plant-pathogen interactions and in disease-associated host cell death. We present a first attempt to reconcile the results of this research. Cell Death and Differentiation (2011) 18, 1257-1262 doi:10.1038/cdd.2011 published online 29 April 2011 Autophagy mediates the degradation of bulk proteins and is also involved in the clearance of damaged organelles, insoluble protein aggregates and lipids. 1-3 Autophagic digestion and recycling can occur as a survival mechanism to maintain cellular homeostasis and to respond to environmental stresses, such as nutrient depletion or pathogen attack, but may also function as a mediator and/or mechanism of programmed cell death. [4][5][6][7][8] Several subtypes of autophagy are described, but macroautophagy (hereafter termed autophagy) is the most extensively studied 9 and will be the only form described here. The process is characterized by the formation of large, double-membrane vesicles called autophagosomes. These structures arise from expanding single membranes (termed phagophores), which enclose cytoplasmic material and organelles for degradation. Completed autophagosomes fuse with the vacuole/lysosome to release the inner singlemembrane vesicle, called the autophagic body, into the lumen for hydrolytic degradation and recycling. 2,10 The mechanism of autophagy is conserved in yeast, plants and metazoans, and involves the action of canonical autophagy related genes (ATG) that synthesize and coordinate membrane rearrangements to allow cellular catabolism. 1,2 The core sets of ATG genes seem to be present in all eukaryotes and to be essential for the autophagy pathway (Figure 1). For instance, induction of autophagy requires the negative regulator target of rapamycin (TOR) kinase and the ATG1 kinase complex, which control the activity of the phosphatidylinositol 3-kinase complex containing, for example, ATG6/Beclin1. 11 Initiation and completion of autophagosome formation involves two ubiquitin-like conjugation systems to produce ATG12-ATG5 and ATG8-phosphatidylethanolamine (ATG8-PE) conjugates. ATG8-PE conjugation involves the cysteine proteinase ATG4 and the E1-like protein ATG7, and lipidated ATG8 is linked to and translocated with autophagosomes to the vacuole. 12 Therefore, conversion from solu...

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“…with Vps34/Beclin-1 via its scaffold protein GOPC but not Cyt-2 (18). Therefore, we assessed whether the full-length and short forms of Slamf1 function differently.…”

Section: Slamf1 Recruits a Beclin-1/vps34/uvrag Complexmentioning

confidence: 99%

Receptor Signaling Lymphocyte-activation Molecule Family 1 (Slamf1) Regulates Membrane Fusion and NADPH Oxidase 2 (NOX2) Activity by Recruiting a Beclin-1/Vps34/Ultraviolet Radiation Resistance-associated Gene (UVRAG) Complex

Wang

Detre

et al. 2012

Journal of Biological Chemistry

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Background:The receptor Slamf1 functions as a microbial sensor regulating phagocytosis. Results: Slamf1 interacts with Vps34/Beclin-1/UVRAG complex in a wide range of cells. Conclusion: Slamf1 recruits a subset of ubiquitous autophagy-associated proteins, which is involved in membrane fusion and NOX2 regulation. Significance: These studies provide insight into the regulation of microbicidal function allowing for potential therapeutic discoveries.

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Autophagy Induction by the Pathogen Receptor CD46

Cited by 228 publications

References 59 publications

Extracellular stimulation of VSIG4/complement receptor Ig suppresses intracellular bacterial infection by inducing autophagy

Extracellular stimulation of VSIG4/complement receptor Ig suppresses intracellular bacterial infection by inducing autophagy

Role of autophagy in disease resistance and hypersensitive response-associated cell death

Receptor Signaling Lymphocyte-activation Molecule Family 1 (Slamf1) Regulates Membrane Fusion and NADPH Oxidase 2 (NOX2) Activity by Recruiting a Beclin-1/Vps34/Ultraviolet Radiation Resistance-associated Gene (UVRAG) Complex

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