RAB11-mediated trafficking in host–pathogen interactions

Guichard, Annabel; Nizet, Victor; Bier, Ethan

doi:10.1038/nrmicro3325

Cited by 78 publications

(74 citation statements)

References 79 publications

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“…Recently, the ERC has been shown to play a major role not only in pathogen entry and infection but also in the innate (beta interferon) immune response to viruses (54). Although a number of viruses traffic through the ERC during entry (55)(56)(57), their infection was not inhibited by Rab11-S25N, which is indicative of the Twenty-four hours later, the respective virus (at 100 TCID 50 /cell) was allowed to internalize for 60 min; unbound virus was washed away with cold PBSϩ containing 25 mM NH 4 Cl for 15 min, and replication was allowed to proceed for 6.5 h at 37°C in infection medium containing NH 4 Cl.…”

Section: Pre-incubation Virus Internalization Cold Washmentioning

confidence: 99%

ICAM-1 Binding Rhinoviruses A89 and B14 Uncoat in Different Endosomal Compartments

Conzemius

Ganjian

Blaas

et al. 2016

J Virol

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Human rhinovirus A89 (HRV-A89) and HRV-B14 bind to and are internalized by intercellular adhesion molecule 1 (ICAM-1); as demonstrated earlier, the RNA genome of HRV-B14 penetrates into the cytoplasm from endosomal compartments of the lysosomal pathway. Here, we show by immunofluorescence microscopy that HRV-A89 but not HRV-B14 colocalizes with transferrin in the endocytic recycling compartment (ERC). Applying drugs differentially interfering with endosomal recycling and with the pathway to lysosomes, we demonstrate that these two major-group HRVs productively uncoat in distinct endosomal compartments. Overexpression of constitutively active (Rab11-GTP) and dominant negative (Rab11-GDP) mutants revealed that uncoating of HRV-A89 depends on functional Rab11. Thus, two ICAM-1 binding HRVs are routed into distinct endosomal compartments for productive uncoating. IMPORTANCEBased on similarity of their RNA genomic sequences, the more than 150 currently known common cold virus serotypes were classified as species A, B, and C. The majority of HRV-A viruses and all HRV-B viruses use ICAM-1 for cell attachment and entry. Our results highlight important differences of two ICAM-1 binding HRVs with respect to their intracellular trafficking and productive uncoating; they demonstrate that serotypes belonging to species A and B, but entering the cell via the same receptors, direct the endocytosis machinery to ferry them along distinct pathways toward different endocytic compartments for uncoating.

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Section: Pre-incubation Virus Internalization Cold Washmentioning

confidence: 99%

ICAM-1 Binding Rhinoviruses A89 and B14 Uncoat in Different Endosomal Compartments

Conzemius

Ganjian

Blaas

et al. 2016

J Virol

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“…It is also interesting that the cholera toxin ADP-ribosylates the stimulatory G protein (G s␣ ), which causes a pathological intracellular increase of cAMP, and RAB11 disruption through PKA and EPAC-RAP-1 (42). How cAMP increase affects RAB11 regulation is still unknown, but this may explain some effects observed on the cytoskeleton organization (43).…”

Section: Discussionmentioning

confidence: 99%

Micropatterned Macrophage Analysis Reveals Global Cytoskeleton Constraints Induced by Bacillus anthracis Edema Toxin

et al. 2015

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c Bacillus anthracis secretes the edema toxin (ET) that disrupts the cellular physiology of endothelial and immune cells, ultimately affecting the adherens junction integrity of blood vessels that in turn leads to edema. The effects of ET on the cytoskeleton, which is critical in cell physiology, have not been described thus far on macrophages. In this study, we have developed different adhesive micropatterned surfaces (L and crossbow) to control the shape of bone marrow-derived macrophages (BMDMs) and primary peritoneal macrophages. We found that macrophage F-actin cytoskeleton adopts a specific polar organization slightly different from classical human HeLa cells on the micropatterns. Moreover, ET induced a major quantitative reorganization of F-actin within 16 h with a collapse at the nonadhesive side of BMDMs along the nucleus. There was an increase in size and deformation into a kidney-like shape, followed by a decrease in size that correlates with a global cellular collapse. The collapse of F-actin was correlated with a release of focal adhesion on the patterns and decreased cell size. Finally, the cell nucleus was affected by actin reorganization. By using this technology, we could describe many previously unknown macrophage cellular dysfunctions induced by ET. This novel tool could be used to analyze more broadly the effects of toxins and other virulence factors that target the cytoskeleton.A nthrax is a disease caused by Bacillus anthracis, a Gram-positive, rod-shaped, spore-forming bacterium whose spores are considered a serious bioterrorism agent (1). The major known virulence factors of B. anthracis include edema toxin (ET), formed by the association of the protective antigen (PA) component with edema factor (EF). Once in the cytosol, EF acts as a calmodulin (CaM)-dependent adenylate cyclase that increases intracellular cyclic AMP (cAMP) concentrations (2, 3).At the cellular level, ET effects have been more precisely described over the last decade. PA binds to at least two independent receptors (ANTXR1 or TEM-8 [tumor endothelial marker 8] and ANTXR2 or CMG-2 [capillary morphogenesis protein 2]) on target cells (4). ANTXR2 plays the major role in vivo for toxin entry. A third coreceptor, named low-density lipoprotein (LDL) receptor protein 6 (LRP-6), has also been proposed (5-7). PA subunits associate into heptamers to form a prepore throughout the cell surface via lipid rafts. This PA heptamer enables the binding of EF components to the cell surface in a stoichiometric ratio of 7/3. The toxin-receptor complex is then internalized by clathrin-dependent endocytosis (8, 9). The pH decrease of early endosomes results in the translocation of these factors in multivesicular bodies (MVB), finally merging with the intracellular membrane of late endosomes. This last step is responsible for translocating EF into the cytoplasm, where it stays associated with the membrane of the late endosome (10). Its perinuclear localization generates intracellular cAMP gradients from the cell nucleus to the periphery. In tur...

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“…Specific virulence factors disable or subvert vesicular trafficking pathways to and from the host cell surface, which promotes pathogen entry, replication or escape (Guichard et al 2014).…”

Section: An Intracellular Lifestylementioning

confidence: 99%

A Glance at Prokaryotes and Eukaryotes Interplay and Campylobacter jejuni–Host Interaction

Santos

Martins

Tavares

et al. 2016

Campylobacter Spp. And Related Organisms in Poultry

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This chapter begins with the historical background to the evolutionary development of the cells. The endosymbiosis theory by which prokaryotes gave rise to the first eukaryotic cells describe the relationship between cell types that may have evolved through predation to mutualism or parasitism. There is also discussion of some interactions between parasitic unicellular organisms and their cell hosts taking into account the dynamic actin cytoskeleton and the immune response resulting from the invasion. Finally, C. jejuni, its types of invasion routes, intracellular traffic, virulence factors, and colonization of poultry cells by C. jejuni are discussed.

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RAB11-mediated trafficking in host–pathogen interactions

Cited by 78 publications

References 79 publications

ICAM-1 Binding Rhinoviruses A89 and B14 Uncoat in Different Endosomal Compartments

ICAM-1 Binding Rhinoviruses A89 and B14 Uncoat in Different Endosomal Compartments

Micropatterned Macrophage Analysis Reveals Global Cytoskeleton Constraints Induced by Bacillus anthracis Edema Toxin

A Glance at Prokaryotes and Eukaryotes Interplay and Campylobacter jejuni–Host Interaction

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