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• W2016001755 abstract "A recent gathering of researchers at the EMBO conference “At the joint edge of Cellular Microbiology and Cell Biology” was aimed at melding ideas from both scientific fields to advance our understanding of infectious diseases at the cellular level. Work presented at this meeting highlighted how pathogens exploit host cell membrane processes to their advantage and also revealed fundamental signaling and trafficking mechanisms of eukaryotic cells. A recent gathering of researchers at the EMBO conference “At the joint edge of Cellular Microbiology and Cell Biology” was aimed at melding ideas from both scientific fields to advance our understanding of infectious diseases at the cellular level. Work presented at this meeting highlighted how pathogens exploit host cell membrane processes to their advantage and also revealed fundamental signaling and trafficking mechanisms of eukaryotic cells. The EMBO conference “At the joint edge of Cellular Microbiology and Cell Biology: Spacial temporal control of signaling and virulence,” organized by Gisou van der Goot (EPFL, Switzerland) and Ivan Dikic (Goethe University School of Medicine, Germany), was held in the picturesque Swiss Alps village of Villars-sur Ollon on September 20–25, 2008. This meeting was the fifth edition in a series of conferences initiated by Pascale Cossart (Institut Pasteur, France) and Jean Gruenberg (University of Geneva, Switzerland) in 2000, that have successfully brought together the otherwise rarely interacting communities of cell biologists and microbiologists. The emergence of cellular microbiology (Cossart et al., 1996Cossart P. Boquet P. Normark S. Rappuoli R. Science. 1996; 271: 315-316Crossref PubMed Scopus (2) Google Scholar), a discipline studying the host-pathogen interface, has fostered such interactions and enhanced our understanding on both sides of this equation via the use of pathogens and their virulence proteins as biological tools. Some pathogenic microorganisms, or microbial products such as toxins, must enter mammalian cells during the disease process to either ensure their intracellular survival and proliferation, or their biological effects. Most use, or trigger, existing entry mechanisms, such as clathrin-mediated endocytosis, macropinocytosis, or phagocytosis, and then intersect the endocytic pathway to traffic within membrane-bound compartments to reach their replicative niche or site of action. However, by using these routes of entry pathogens and toxins face the risk of degradation via fusion with lysosomes, the terminal, degradative compartment of the endocytic pathway. Recent advances in endocytosis-associated signaling and membrane trafficking and how pathogenic microorganisms subvert endocytic signaling and function to ensure their intracellular lifestyle were the focus of this meeting. Here we will cover some of the presented work that illustrates the crossroads of the fields of cellular microbiology and cell biology. Normal membrane trafficking along the endocytic pathway determines identity, maintenance, and function of endocytic organelles. Various signaling and sorting complexes act sequentially along this pathway to transport and sort proteins and lipids for delivery to lysosomes or recycling to the plasma membrane (Gruenberg and van der Goot, 2006Gruenberg J. van der Goot F.G. Nat. Rev. Mol. Cell Biol. 2006; 7: 495-504Crossref PubMed Scopus (253) Google Scholar). One major function of endocytic trafficking is the degradation or recycling of signaling receptors after they have been activated at the plasma membrane. Simona Polo (Instituto FIRC di Oncologia Molecolare, Italy) presented evidence that the mode of epidermal growth factor (EGF) receptor (EGFR) internalization determines its downstream signaling effects. When low concentrations of EGF are used, EGFR is mainly internalized via clathrin-mediated endocytosis (CME) and is not ubiquitinated. The majority of EGFRs internalized via CME are not targeted to degradation, but rather recycled to the cell surface. This, in turn, allows signaling from endosomes before recycling of the receptor to the surface, thereby sustaining signaling, such as phosphorylation of the Akt/PKB kinase. At high EGF concentrations, the receptor becomes ubiquitinated and is internalized through both CME and nonclathrin endocytosis (NCE). NCE preferentially commits the receptor to degradation, thus leading to signal attenuation. In this way, this dual mechanism of EGFR internalization ensures proper and optimal balance of receptor signaling and attenuation. From her studies on the endosomal proteins APPL1/2, Marta Miaczynska (International Institute of Molecular and Cell Biology, Poland) presented the concept that endocytosed receptors keep signaling from endosomes. This is in keeping with observations that a number of specific signaling complexes are on endosomes and some endocytic proteins can also act in the cell nucleus (Miaczynska et al., 2004Miaczynska M. Pelkmans L. Zerial M. Curr. Opin. Cell Biol. 2004; 16: 400-406Crossref PubMed Scopus (441) Google Scholar). APPL proteins are effectors of the early endosomal GTPase Rab5 and regulate cell survival through the Akt/PKB pathway (Schenck et al., 2008Schenck A. Goto-Silva L. Collinet C. Rhinn M. Giner A. Habermann B. Brand M. Zerial M. Cell. 2008; 133: 486-497Abstract Full Text Full Text PDF PubMed Scopus (241) Google Scholar). In response to EGF stimulation, APPL1/2 translocate from endosomal membranes to the nucleus and bind the NuRD/MeCP1 nuclear chromatin remodeling complex. Although they do receive cargo destined for recycling and degradation, APPL-containing endosomes do not colocalize with the markers of known endocytic compartments, but do constitute a rather stable endosomal population that serves as a signaling platform for cell survival. An important function of the endocytic pathway is to sort cargo within intraluminal vesicles of multivesicular bodies/endosomes (MVB) to lysosomes for degradation. This process involves the various endosomal sorting complexes required for transport (ESCRT-0 to -III) and sorting nexins, a family of proteins involved in endosomal sorting. Mechanisms of MVB morphogenesis were discussed by Jean Gruenberg (University of Geneva, Switzerland) and Harald Stenmark (Norwegian Radium Hospital, Norway). Harald Stenmark reviewed the known functions of ESCRT complexes (Hurley, 2008Hurley J.H. Curr. Opin. Cell Biol. 2008; 20: 4-11Crossref PubMed Scopus (293) Google Scholar), and using small interfering RNA (siRNA) approaches showed all are involved in EGFR downregulation. When all four ESCRT complexes were simultaneously depleted, EGFR was no longer sorted into MVBs. Depletion of all four ESCRT complexes also affected MVB morphology, although some intraluminal vesicles (ILV) were still detected, raising the possibility of ESCRT-independent mechanisms of ILV formation. Hrs, a component of ESCRT-0, is not uniformly distributed on endosomal membranes. It localizes to clathrin-rich microdomains on early endosomes, distinct from EEA-1 microdomains on the same vesicle, through direct binding to clathrin. Deletion of the clathrin-binding domain of Hrs relocalized it to EEA-1-positive domains on early endosomes, implying an important role for clathrin in segregating sorting complexes on early endosomes. MVB formation invokes the mechanistic dilemma of limiting membrane deformation in opposite directions by membrane invagination and tubulation. Jean Gruenberg presented evidence from siRNA knockdown experiments that the sorting nexin SNX3 is directly involved in membrane invagination during MVB morphogenesis, while the ESCRT-0 complex protein Hrs is required for lysosomal targeting but is dispensable for MVB biogenesis. Both Hrs and SNX3 bind phosphatidyl inositol-3-phosphate, demonstrating that this signaling lipid is central to regulating MVB biogenesis (Pons et al., 2008Pons V. Luyet P.P. Morel E. Abrami L. van der Goot F.G. Parton R.G. Gruenberg J. PLoS Biol. 2008; 6: e214Crossref PubMed Scopus (75) Google Scholar). Jean Gruenberg also reported the presence of small actin patches on early endosomes that remain associated with these vesicles during movement, including during endosome fission. This phenomenon is required for early-to-late endosomal transport and is sensitive to annexin A2 siRNA. This actin-binding protein is enriched on early endosomes and necessary for MVB biogenesis but not invagination. Altogether, these presentations highlighted the important role of phosphoinositides and the cytoskeleton in the control of endosomal membrane dynamics. More examples of the complexities of endosomal transport were also presented during the meeting. Several years ago, it was shown that latex bead-containing phagosomes interact with the endoplasmic reticulum (ER) during their maturation (Gagnon et al., 2002Gagnon E. Duclos S. Rondeau C. Chevet E. Cameron P.H. Steele-Mortimer O. Paiement J. Bergeron J.J. Desjardins M. Cell. 2002; 110: 119-131Abstract Full Text Full Text PDF PubMed Scopus (549) Google Scholar), revealing unsuspected interactions between the ER and the endocytic pathway. Several independent pieces of evidence presented at this conference argue for such interactions and reinforce the concept of functional crosstalk between these two compartments. Coen Kuijl (The Netherlands Cancer Institute, The Netherlands) presented evidence for cholesterol (CHO)-dependent positioning of late endosomes via the Rab7 effector oxysterol-binding protein-related 1L (ORP1L) (Johansson et al., 2007Johansson M. Rocha N. Zwart W. Jordens I. Janssen L. Kuijl C. Olkkonen V.M. Neefjes J. J. Cell Biol. 2007; 176: 459-471Crossref PubMed Scopus (324) Google Scholar) and interactions with the ER. CHO depletion or ORP1L knockdown induces lysosomal scattering, while increasing intracellular CHO levels result in lysosome clustering in an ORP1L-dependent manner. ORP1L directly binds CHO via its oxysterol-binding protein (OSBP)-related domain (ORD). In turn, this interaction prevents binding of its FFAT (two phenylalanines in an acidic tract) motif to the ER transmembrane protein VAMP (vesicle-associated membrane protein)-associated protein-A (VAP-A). As shown by fluorescence resonance energy transfer (FRET), late endosomes and ER undergo nonfusogenic contact, a phenomenon amplified by CHO depletion or deletion of the ORP1L ORD domain and diminished by increased intracellular CHO. Hence, CHO regulates interactions between lysosomes and the ER. These ER-endosomal interactions might prove relevant to pathogen-host cell interactions. The intracellular bacterial pathogen Brucella abortus resides within a membrane-bound vacuole, the Brucella-containing vacuole (BCV), which initially interacts with endocytic compartments, before fusing with the ER to generate an ER-derived replicative organelle. Although it was commonly accepted that Brucella intracellular survival relies on the avoidance of lysosome fusion, Jean Celli (Rocky Mountain Laboratories, NIH, USA) used live-cell imaging techniques to show that BCVs interact with late endocytic compartments (Figure 1A), including lysosomes, before reaching the ER, and that such trafficking is required for bacterial replication, raising the possibility that this pathogen uses late endosome-ER interactions to gain access to the ER. Another example of pathogenic subversion of endocytic compartments is provided by Toxoplasma gondii. This protozoan parasite resides within a parasitophorous vacuole (PV) composed of parasite proteins, including dense granule proteins (GRA) secreted by T. gondii. To address how this apicomplexan parasite acquires nutrients across the PV membrane when it remains isolated from host cell pathways, Isabelle Coppens (Johns Hopkins Bloomberg School of Public Health, USA) showed that the PV traffics along host microtubules to a juxtanuclear area, anchors to the nuclear envelope, and displaces the microtubule-organizing center to recruit microtubules and organelles such as late endosomes/lysosomes and the Golgi apparatus to the vicinity of the PV. Surprisingly, despite dramatic reorganization of the microtubule network, host actin filaments appear unperturbed in infected cells. Such host organelle recruitment allows the parasite to retrieve and internalize endocytic vesicles through PV membrane invaginations mediated by host microtubules (Figure 1D). The T. gondii protein, GRA7, forms constriction rings to stabilize these invaginations. GRA7, which is required for survival in nutrient-depleted conditions, is secreted within the PV, has high affinity for phosphoinositides, and can induce liposome deformation, consistent with its activity on PV membrane deformations (Coppens et al., 2006Coppens I. Dunn J.D. Romano J.D. Pypaert M. Zhang H. Boothroyd J.C. Joiner K.A. Cell. 2006; 125: 261-274Abstract Full Text Full Text PDF PubMed Scopus (227) Google Scholar). These PV membrane invaginations are used as conduits by endocytic vesicles, leading to their sequestration in the PV. Since the endosomal compartment constitutes a default pathway for many intracellular pathogens, most have evolved strategies to subvert normal endosomal sorting and signaling to avoid its degradative function. Recent advances in the basic cell biology of these processes, such as those described above, will be helpful in understanding pathogenic mechanisms. Intracellular trafficking is characterized by extensive and dynamic membrane remodeling, such as membrane tubulation and vesicle fusion and fission. These events are orchestrated by numerous membrane-associated proteins, including Rabs, SNAREs, and tethering factors (Cai et al., 2007Cai H. Reinisch K. Ferro-Novick S. Dev. Cell. 2007; 12: 671-682Abstract Full Text Full Text PDF PubMed Scopus (441) Google Scholar). Several presenters at the meeting highlighted unusual membrane deformation events, often due to pathogen interference with membranes of varied host cell compartments. The intracellular bacterium, Salmonella enterica, is well known to reorganize the late endocytic compartment into long, stabilized membrane tubules called Salmonella-induced filaments (Sifs) (Garcia-del Portillo et al., 1993Garcia-del Portillo F. Zwick M.B. Leung K.Y. Finlay B.B. Proc. Natl. Acad. Sci. USA. 1993; 90: 10544-10548Crossref PubMed Scopus (233) Google Scholar), and its vacuole (SCV) requires a functional secretory pathway for proper positioning in epithelial cells (Salcedo and Holden, 2003Salcedo S.P. Holden D.W. EMBO J. 2003; 22: 5003-5014Crossref PubMed Scopus (147) Google Scholar). Jaime Mota (Imperial College London, UK) screened a siRNA library designed against 190 Golgi- and endosome-related proteins for host factors that control SCV positioning in epithelial cells. Two integral membrane proteins were identified that concentrate on perinuclear membranes—specifically the trans-Golgi network and endocytic recycling compartment. Their identification suggests a direct connection between SCVs and post-Golgi trafficking. Interestingly, Salmonella infection caused the redistribution of one of these proteins into long tubules that were found to emanate from the SCV. Live-cell imaging showed that these tubules (named SCATs) are distinct from Sifs. The formation of Sifs and SCATs both require microtubules and the same subset of type III effectors, indicating that Salmonella effectors induce membrane tubulation from both the endocytic and secretory pathways. A number of speakers at the conference covered the exit from, or movement through, cells. Upon entry in either macrophages or the amoeba Dictyostelium discoideum, Mycobacterium marinum resides and proliferates in a phagosome whose maturation is arrested; then M. marinum lyses this vacuole to escape to the cytosol where it can undergo actin-based motility. The subsequent fate of cytosolic bacteria has, until now, remained uncharacterized. Thierry Soldati (University of Geneva, Switzerland) presented data on the cell-to-cell transmission of M. marinum in D. discoideum. He showed that the host Rho GTPase protein, RacH, is essential for bacterial exit and dissemination, and this process is associated with a “spike” in F-actin polymerization at the site of bacterium-plasma membrane contact (Figure 1C). This expands and generates a structure he called an “ejectosome,” which allows bacterial extrusion through the plasma membrane without any detectable host cell leakage. Ejectosome formation depends upon an intact bacterial RD1 locus, encoding a type VII secretion system, and is a conserved virulence mechanism also shared by cytosolic M. tuberculosis. Another means of host cell egress was presented for the protozoan parasite, Plasmodium berghei, by Volker Heussler (Bernard Nocht Institute of Tropical Medicine, Germany). During the liver stage of infection, the malaria parasite inhabits and replicates to large numbers in hepatocytes, but does not induce host cell death. In order to enter blood vessels and eventually infect red blood cells, rather than simply rupturing the hepatocyte plasma membrane, parasites induce the formation of merozoite-filled vesicles called merosomes, which act as a transmission organelle. These plasma membrane-derived structures protect the parasite from host phagocytic cell attack and translocate merozoites directly into blood vessels to allow hemocyte infection (Sturm et al., 2006Sturm A. Amino R. van de Sand C. Regen T. Retzlaff S. Rennenberg A. Krueger A. Pollok J.M. Menard R. Heussler V.T. Science. 2006; 313: 1287-1290Crossref PubMed Scopus (348) Google Scholar). Merosomes likely account for the transition from the silent hepatic stage to the pathologic blood stage of malaria, and constitute an original example of host plasma membrane subversion. Plasma membrane openings were also described by Anne Ridley (King's College London, UK). Leukocytes normally undergo transendothelial migration during inflammation by either a paracellular (between cells) or transcellular (through cells) route. Anne Ridley reported that T cells bound to the apical surface of endothelial cells could extend protrusions down to the basal endothelial membrane to form a transcellular channel. The adhesion receptor ICAM-1, caveolin, and F-actin were enriched around these channels. Transcellular, but not paracellular, migration was sensitive to caveolin siRNA knockdown, suggesting that caveola-rich membrane domains are required for T cell-induced channel formation. Intercellular transmission of viruses also involves plasma membrane protrusions. Vincent Piguet (University of Geneva, Switzerland) described transmission of human immunodeficiency virus (HIV) from infected dendritic cells to T cells via a virological synapse. A role for filopodial extensions originating at the plasma membrane during the transfer across the infectious synapse was proposed. Bacterial toxins have proven to be an invaluable tool for deciphering many cell biological processes. One major site of action for these toxins is host cell membranes. Emmanuel Lemichez (University of Nice, France) reported that the Staphylococcus aureus EDIN toxin impacts endothelium barrier function, by producing large transcellular tunnels called macroapertures (Figure 1B). This toxin has a higher prevalence in pathogenic strains of S. aureus. It belongs to the ADP-ribosyltransferases of the Clostridium botulinum C3 exoenzyme family, and modifies the small GTPase RhoA on Asn41 to prevent its activation. No apoptosis or lysosomal exocytosis is associated with the opening of macroapertures. Microaperture formation can be recapitulated by RNA interference (RNAi)-mediated RhoA knockdown, or to a lesser extent by inhibition of the Rho-associated kinase ROCK and disruption of actin stress fibers. Microaperture closure involves the formation of membrane waves containing F-actin, through recruitment of the Rac1 GTPase, cortactin, and the Actin-related protein (Arp) 2/3 complex. Large tunnels are also formed by S. aureus producing EDIN, leading to the idea that this may favor bacterial attachment to the endothelium basement membrane. Work on how the B subunits of bacterial A/B toxins can deform membranes to initiate their internalization by clathrin-independent endocytosis was presented by Ludger Johannes and Patricia Bassereau (Institut Curie, France). Shiga toxin induces tubular structures at the plasma membrane as an initial step of its uptake into cells. Processing of these tubular invaginations is perturbed upon modification of cholesterol homeostasis and dynamin and F-actin dynamics. Using model membranes, namely giant unilamellar vesicles (GUVs), to study the mechanism by which Shiga toxin induces membrane invaginations, Ludger Johannes presented evidence that toxin binding of up to 15 Gb3 receptor molecules leads to lipid compaction in the exoplasmic membrane leaflet, generating the curvature changes needed for tubule formation. Remarkably, the same observations were made for other toxins and certain animal viruses, all of which enter cells in a clathrin-independent manner and share a structural element that serves as an interaction platform with glycosphingolipid receptors. Patricia Bassereau further investigated the biophysics of toxin-induced spontaneous membrane curvature. She first showed that cholera toxin depletion from a membrane tubule, and consequently its GM1 receptor, increases with curvature, independently of membrane composition. In turn, membrane curvature can induce lipid sorting if the lipid mixture is close to phase separation, a process further amplified by protein binding. Altogether, these presentations emphasized how pathogens and their effector molecules exacerbate normal host membrane remodeling events. Originally identified as a homeostatic mechanism to remove damaged organelles and address anabolic needs under conditions of starvation, autophagy has more recently been recognized as a central component in both inflammation and innate and adaptive immunity. By sequestering cytosolic content for delivery to lysosomes, this process contributes to removal of intracellular bacteria and viruses and major histocompatibility complex (MHC) II presentation of cytosolic antigens. Additionally, regulatory and functional links to apoptosis and proinflammatory responses have associated autophagy with cell death and resolution of inflammation (Maiuri et al., 2007Maiuri M.C. Zalckvar E. Kimchi A. Kroemer G. Nat. Rev. Mol. Cell Biol. 2007; 8: 741-752Crossref PubMed Scopus (2510) Google Scholar, Saitoh et al., 2008Saitoh T. Fujita N. Jang M.H. Uematsu S. Yang B.G. Satoh T. Omori H. Noda T. Yamamoto N. Komatsu M. et al.Nature. 2008; 456: 264-268Crossref PubMed Scopus (1455) Google Scholar). Vojo Deretic (University of New Mexico School of Medicine, USA) introduced the significance of this pathway with regard to infection and human genetic diseases, emphasizing its induction by the proinflammatory cytokines IFN-γ and TNF-α and its regulation by two host-specific GTPases, interferon-inducible p47 (IRG47) in mice, and IRGM in humans (Singh et al., 2006Singh S.B. Davis A.S. Taylor G.A. Deretic V. Science. 2006; 313: 1438-1441Crossref PubMed Scopus (707) Google Scholar). Further characterization of IRGM showed that one splice variant of IRGM affected cell survival. Describing how autophagy is involved in the intracellular degradation of protein aggregates, Ivan Dikic (Goethe University School of Medicine, Germany) compared the early autophagy conjugation machinery to ubiquitination and showed that the autophagic protein Atg8/LC3 is conjugated to phosphatidylethanolamine on autophagic membranes by a ubiquitination-like process and serves as a binding partner for a family of receptors able to bind directly to Atg8/LC3. Among them was p62, also known as sequestosome-1 (SQSTM), which binds Atg8/LC3 through its LC3-interacting region (LIR). Ivan Dikic described a high-throughput method utilizing the yeast two-hybrid system to identify novel proteins binding to Atg8/LC3, named autophagy receptors. These receptors are targeted to lysosomes and are degraded in a LIR-dependent manner, unless autophagy is interrupted (V. Kirkin, T. Johansen, and I. Dikic, unpublished data). Interestingly, the p62-type autophagy receptors also bind ubiquitin via their UBA domains and therefore constitute a molecular link between ubiquitination- and autophagy-mediated degradation. Given that autophagy is an important host defense pathway against many different kinds of infections, it is not surprising that pathogens have evolved strategies to counter, and in some cases exploit, this host cell autophagic response (Orvedahl and Levine, 2008Orvedahl A. Levine B. Cell Death Differ. 2008; https://doi.org/10.1038/cdd.2008.130Crossref PubMed Scopus (163) Google Scholar). Using in vitro coculture systems with primary CD4 T cells and effector cells expressing the HIV envelope glycoproteins, Env (gp120 and gp41), Lucile Espert (CPBS-University of Montpellier, France) reported that gp41-mediated intercellular membrane fusion induces cell death that requires autophagy genes. This Env-mediated autophagic response is needed to trigger apoptosis and is independent of CXCR4 and CD4 signaling. These results suggest that HIV-infected cells can induce autophagy in bystander CD4 T lymphocytes through the fusogenic function of gp41, leading to apoptotic cell death, a mechanism most likely contributing to immunodeficiency. Similarly, Kim Orth (University of Texas Southwestern Medical Center, USA) showed that the rapid host cell cytotoxicity associated with the type III secretion system encoded on chromosome 1 (T3SS1) of Vibrio parahaemolyticus results, in part, from an unregulated induction of autophagy by the T3SS1 effector protein VopQ, which is followed by the action of another T3SS1 effector, VopS, on Rho GTPases (Burdette et al., 2008Burdette D.L. Yarbrough M.L. Orvedahl A. Gilpin C.J. Orth K. Proc. Natl. Acad. Sci. USA. 2008; 105: 12497-12502Crossref PubMed Scopus (88) Google Scholar). Illustrating a pathogenic response to an autophagic challenge, Vincent Piguet (University of Geneva, Switzerland) reported that HIV capture by dendritic cells leads to a block of autophagy associated with a decrease in levels of autophagy-associated proteins and the lipidated form of LC3. Furthermore, siRNA depletion of LC3 increased dendritic cell-associated viral particles and enhanced viral transfer from dendritic cells to T cells, suggesting that autophagy may represent a mechanism of defense against HIV during the early events of HIV infection. Given its regulatory links to cell death and involvement in pathogen clearance, autophagy constitutes a primary pathway for pathogenic interference, either by counteraction or abuse. While research at the interface of cell biology and cellular microbiology has been remarkably productive at advancing our knowledge of pathogenesis at the cellular level, this meeting also illustrated the future direction of this area of study, namely more global approaches to pathogen-host cell interactions. This was exemplified by the work of Lucas Pelkmans (ETH Zürich, Switzerland), who applied a systems biology approach to the infectious entry of viruses. By using genome-wide siRNA screens and top-down data-driven modeling, one may uncover global differences between the subversion of cellular systems by different viruses. An additional level of understanding of virus-host cell interactions can be achieved by predicting cell-to-cell variation of infection in a whole population of cells. This can be revealed by integrating several population-based properties in the analysis of infection, and might allow the prediction of heterogeneity patterns of infection in a population of cells. The development of such population behavior prediction tools will undoubtedly improve our understanding of pathogen-host cell interactions, with potential applications to in vivo infections. This EMBO conference successfully brought together cell biologists and cellular microbiologists to foster discussion about the cellular and molecular mechanisms of infectious diseases. The emphasis was on how parasites and toxins manipulate host membrane-associated processes, reinforcing the concept of pathogens as critical tools for dissecting fundamental cell biology mechanisms. Common themes in discussions included pathogenic reorganization of intracellular membrane compartments and subversion of the endocytic and autophagic pathways for the purpose of entry, survival, proliferation, cytotoxicity, and egress. This meeting exemplified how advances in fundamental cell biology nurture discoveries in cellular microbiology. Future research efforts at the interface of both fields will undoubtedly lead to important discoveries on how hosts and microbes interact." @default.
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• W2016001755 title "Of Microbes and Membranes: Pathogenic Subversion of Host Cell Processes" @default.
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