Cellular Microbiology最新文献

{"title":"Porphyromonas gingivalis induces penetration of lipopolysaccharide and peptidoglycan through the gingival epithelium via degradation of coxsackievirus and adenovirus receptor","authors":"Hiroki Takeuchi,&nbsp;Shunsuke Yamaga,&nbsp;Naoko Sasaki,&nbsp;Masae Kuboniwa,&nbsp;Michiya Matsusaki,&nbsp;Atsuo Amano","doi":"10.1111/cmi.13388","DOIUrl":"10.1111/cmi.13388","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p><i>Porphyromonas gingivalis</i> is a major pathogen of human periodontitis and dysregulates innate immunity at the gingival epithelial surface. We previously reported that the bacterium specifically degrades junctional adhesion molecule 1 (JAM1), causing gingival epithelial barrier breakdown. However, the functions of other JAM family protein(s) in epithelial barrier dysregulation caused by <i>P. gingivalis</i> are not fully understood. The present results show that gingipains, Arg-specific or Lys-specific cysteine proteases produced by <i>P. gingivalis</i>, specifically degrade coxsackievirus and adenovirus receptor (CXADR), a JAM family protein, at R145 and K235 in gingival epithelial cells. In contrast, a gingipain-deficient <i>P. gingivalis</i> strain was found to be impaired in regard to degradation of CXADR. Furthermore, knockdown of CXADR in artificial gingival epithelium increased permeability to dextran 40 kDa, lipopolysaccharide and peptidoglycan, whereas overexpression of CXADR in a gingival epithelial tissue model prevented penetration by those agents following <i>P. gingivalis</i> infection. Together, these results suggest that <i>P. gingivalis</i> gingipains breach the stratified squamous epithelium barrier by degrading CXADR as well as JAM1, which allows for efficient transfer of bacterial virulence factors into subepithelial tissues.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Takeaways</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li><i>P. gingivalis</i>, a periodontal pathogen, degraded coxsackievirus and adenovirus receptor (CXADR), a JAM family protein, in gingival epithelial tissues.</li>\u0000 \u0000 <li><i>P. gingivalis</i> gingipains, cysteine proteases, degraded CXADR at R145 and K235.</li>\u0000 \u0000 <li>CXADR degradation by <i>P. gingivalis</i> caused increased permeability to lipopolysaccharide and peptidoglycan through gingival epithelial tissues.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 11","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13388","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39359460","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Zinc finger proteins of Plasmodium falciparum","authors":"Che Julius Ngwa,&nbsp;Afia Farrukh,&nbsp;Gabriele Pradel","doi":"10.1111/cmi.13387","DOIUrl":"10.1111/cmi.13387","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Zinc finger proteins (ZFPs) are a large diverse family of proteins with one or more zinc finger domains in which zinc is important in stabilising the domain. ZFPs can interact with DNA, RNA, lipids or even other proteins and therefore contribute to diverse cellular processes including transcriptional regulation, ubiquitin-mediated protein degradation, mRNA decay and stability. In this review, we provide the first comprehensive classification of ZFPs of the malaria parasite <i>Plasmodium falciparum</i> and provide a state of knowledge on the main ZFPs in the parasite, which include the C2H2, CCCH, RING finger and the PHD finger proteins.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take aways</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>The <i>Plasmodium falciparum</i> genome encodes 170 putative Zinc finger proteins (ZFPs).</li>\u0000 \u0000 <li>The C2H2, CCCH, RING finger and PHD finger subfamilies of ZFPs are most represented.</li>\u0000 \u0000 <li>Known ZFP functions include the regulation of mRNA metabolism and proteostasis.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 12","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13387","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39331456","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular Microbiology: A New Vision and Expanded Scope.","authors":"M. Ostankovitch, T. Soldati, J. Helmann","doi":"10.1111/cmi.13386","DOIUrl":"https://doi.org/10.1111/cmi.13386","url":null,"abstract":"","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"1 1","pages":"e13386"},"PeriodicalIF":3.4,"publicationDate":"2021-08-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13386","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45285275","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cover Image: Disassembly of the apical junctional complex during the transmigration of Leptospira interrogans across polarized renal proximal tubule epithelial cells (Cellular Microbiology 09/2021)","authors":"Isabel Sebastián,&nbsp;Nobuhiko Okura,&nbsp;Bruno M. Humbel,&nbsp;Jun Xu,&nbsp;Idam Hermawan,&nbsp;Chiaki Matsuura,&nbsp;Malgorzata Hall,&nbsp;Chitoshi Takayama,&nbsp;Tetsu Yamashiro,&nbsp;Shuichi Nakamura,&nbsp;Claudia Toma","doi":"10.1111/cmi.13382","DOIUrl":"10.1111/cmi.13382","url":null,"abstract":"<p>Focused ion beam-scanning electron microscopy image of renal proximal tubule epithelial cells infected for 24 hrs with <i>Leptospira interrogans</i>. Leptospires localized in the gap between two adjacent cells (red and blue). For further details, readers are referred to the article by Sebastián et al. on p. e13343 of this issue.\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure></p>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 9","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-08-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13382","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45395980","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Host cell membrane microdomains and fungal infection","authors":"Taiane N. Souza,&nbsp;Alessandro F. Valdez,&nbsp;Juliana Rizzo,&nbsp;Daniel Zamith-Miranda,&nbsp;Allan Jefferson Guimarães,&nbsp;Joshua D. Nosanchuk,&nbsp;Leonardo Nimrichter","doi":"10.1111/cmi.13385","DOIUrl":"10.1111/cmi.13385","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Lipid microdomains or lipid rafts are dynamic and tightly ordered regions of the plasma membrane. In mammalian cells, they are enriched in cholesterol, glycosphingolipids, Glycosylphosphatidylinositol-anchored and signalling-related proteins. Several studies have suggested that mammalian pattern recognition receptors are concentrated or recruited to lipid domains during host-pathogen association to enhance the effectiveness of host effector processes. However, pathogens have also evolved strategies to exploit these domains to invade cells and survive. In fungal organisms, a complex cell wall network usually mediates the first contact with the host cells. This cell wall may contain virulence factors that interfere with the host membrane microdomains dynamics, potentially impacting the infection outcome. Indeed, the microdomain disruption can dampen fungus-host cell adhesion, phagocytosis and cellular immune responses. Here, we provide an overview of regulatory strategies employed by pathogenic fungi to engage with and potentially subvert the lipid microdomains of host cells.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Away</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>Lipid microdomains are ordered regions of the plasma membrane enriched in cholesterol, glycosphingolipids (GSL), GPI-anchored and signalling-related proteins.</li>\u0000 \u0000 <li>Pathogen recognition by host immune cells can involve lipid microdomain participation. During this process, these domains can coalesce in larger complexes recruiting receptors and signalling proteins, significantly increasing their signalling abilities.</li>\u0000 \u0000 <li>The antifungal innate immune response is mediated by the engagement of pathogen-associated molecular patterns to pattern recognition receptors (PRRs) at the plasma membrane of innate immune cells. Lipid microdomains can concentrate or recruit PRRs during host cell-fungi association through a multi-interactive mechanism. This association can enhance the effectiveness of host effector processes. However, virulence factors at the fungal cell surface and extracellular vesicles can re-assembly these domains, compromising the downstream signalling and favouring the disease development.</li>\u0000 \u0000 <li>Lipid microdomains are therefore very attractive targets for novel drugs to combat fungal infections.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 12","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13385","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39311100","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Host manipulation by bacterial type III and type IV secretion system effector proteases","authors":"Flávia Viana,&nbsp;Shruthi Sachidanandan Peringathara,&nbsp;Arshad Rizvi,&nbsp;Gunnar N. Schroeder","doi":"10.1111/cmi.13384","DOIUrl":"10.1111/cmi.13384","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Proteases are powerful enzymes, which cleave peptide bonds, leading most of the time to irreversible fragmentation or degradation of their substrates. Therefore they control many critical cell fate decisions in eukaryotes. Bacterial pathogens exploit this power and deliver protease effectors through specialised secretion systems into host cells. Research over the past years revealed that the functions of protease effectors during infection are diverse, reflecting the lifestyles and adaptations to specific hosts; however, only a small number of peptidase families seem to have given rise to most of these protease virulence factors by the evolution of different substrate-binding specificities, intracellular activation and subcellular targeting mechanisms. Here, we review our current knowledge about the enzymology and function of protease effectors, which Gram-negative bacterial pathogens translocate via type III and IV secretion systems to irreversibly manipulate host processes. We highlight emerging concepts such as signalling by protease cleavage products and effector-triggered immunity, which host cells employ to detect and defend themselves against a protease attack.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Away</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>Proteases irreversibly cleave proteins to control critical cell fate decisions.</li>\u0000 \u0000 <li>Gram-negative bacteria use type III and IV secretion systems to inject effectors.</li>\u0000 \u0000 <li>Protease effectors are integral weapons for the manipulation of host processes.</li>\u0000 \u0000 <li>Effectors evolved from few peptidase families to target diverse substrates.</li>\u0000 \u0000 <li>Effector-triggered immunity upon proteolytic attack emerges as host defence.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 11","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13384","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39311101","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mucosal immune responses in the trachea after chronic infection with Mycoplasma gallisepticum in unvaccinated and vaccinated mature chickens","authors":"Sathya N. Kulappu Arachchige,&nbsp;Nadeeka K. Wawegama,&nbsp;Mauricio J. C. Coppo,&nbsp;Habtamu B. Derseh,&nbsp;Paola K. Vaz,&nbsp;Anna Kanci Condello,&nbsp;Oluwadamilola S. Omotainse,&nbsp;Amir H. Noormohammadi,&nbsp;Glenn F. Browning","doi":"10.1111/cmi.13383","DOIUrl":"10.1111/cmi.13383","url":null,"abstract":"&lt;div&gt;\u0000 \u0000 \u0000 &lt;section&gt;\u0000 \u0000 &lt;p&gt;Tracheitis associated with the chronic respiratory disease in chickens caused by &lt;i&gt;Mycoplasma gallisepticum&lt;/i&gt; is marked by infiltration of leukocytes into the mucosa. Although cytokines/chemokines are known to play a key role in the recruitment, differentiation, and proliferation of leukocytes, those that are produced and secreted into the trachea during the chronic stages of infection with &lt;i&gt;M. gallisepticum&lt;/i&gt; have not been described previously. In this study, the levels of transcription in the trachea of genes encoding a panel of 13 cytokines/chemokines were quantified after experimental infection with the &lt;i&gt;M. gallisepticum&lt;/i&gt; wild-type strain Ap3AS in unvaccinated chickens and chickens vaccinated 40-, 48- or 57-weeks previously with the novel attenuated strain ts-304. These transcriptional levels in unvaccinated/infected and vaccinated/infected chickens were compared with those of unvaccinated/uninfected and vaccinated/uninfected chickens. Pathological changes and subsets of leukocytes infiltrating the tracheal mucosa were concurrently assessed by histopathological examination and indirect immunofluorescent staining. After infection, unvaccinated birds had a significant increase in tracheal mucosal thickness and in transcription of genes for cytokines/chemokines, including those for IFN-γ, IL-17, RANTES (CCLi4), and CXCL-14, and significant downregulation of IL-2 gene transcription. B cells, CD3&lt;sup&gt;+&lt;/sup&gt; or CD4&lt;sup&gt;+&lt;/sup&gt; cells and macrophages (KUL01&lt;sup&gt;+&lt;/sup&gt;) accumulated in the mucosa but CD8&lt;sup&gt;+&lt;/sup&gt; cells were not detected. In vaccinated birds, the levels of transcription of the genes for IL-6, IL-2, RANTES and CXCL-14 were significantly lower after infection than in the unvaccinated/infected and/or unvaccinated/uninfected birds, while the transcription of the IFN-γ gene was significantly upregulated, and there were aggregations of B cells in the tracheal mucosa. These observations indicated that &lt;i&gt;M. gallisepticum&lt;/i&gt; may have suppressed Th2 responses by upregulating secretion of IFN-γ and IL-17 by CD4&lt;sup&gt;+&lt;/sup&gt; cells and induced immune dysregulation characterized by depletion of CD8&lt;sup&gt;+&lt;/sup&gt; cells and downregulation of IL-2 in the tracheas of unvaccinated birds. The ts-304 vaccine appeared to induce long-term protection against this immune dysregulation.&lt;/p&gt;\u0000 &lt;/section&gt;\u0000 \u0000 &lt;section&gt;\u0000 \u0000 &lt;h3&gt; Take Away&lt;/h3&gt;\u0000 \u0000 &lt;div&gt;\u0000 &lt;ul&gt;\u0000 \u0000 &lt;li&gt;The ts-304 vaccine-induced long-term protection against immune dysregulation caused by &lt;i&gt;M. gallisepticum&lt;/i&gt;&lt;/li&gt;\u0000 \u0000 &lt;li&gt;Detection of B cells and plasma cells in the tracheal mucosa suggested that long-term protection is mediated by mucosal B cell memory&lt;/li&gt;\u0000 \u0000 &lt;li&gt;Infection of","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 11","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-08-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13383","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39271613","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Feminising Wolbachia disrupt Armadillidium vulgare insulin-like signalling pathway","authors":"Benjamin Herran,&nbsp;Camille Houdelet,&nbsp;Maryline Raimond,&nbsp;Carine Delaunay,&nbsp;Nicolas Cerveau,&nbsp;Catherine Debenest,&nbsp;Pierre Grève,&nbsp;Joanne Bertaux","doi":"10.1111/cmi.13381","DOIUrl":"10.1111/cmi.13381","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>The endosymbiont <i>Wolbachia</i> feminises male isopods by making them refractory to the insulin-like masculinising hormone, which shunts the autocrine development of the androgenic glands. It was, therefore, proposed that <i>Wolbachia</i> silences the IR receptors, either by preventing their expression or by inactivating them. We describe here the two IR paralogs of <i>Armadillidium vulgare</i>. They displayed a conventional structure and belonged to a family widespread among isopods. Av-IR1 displayed an ubiquist expression, whereas the expression of Av-IR2 was restricted to the gonads. Both were constitutively expressed in males and females and throughout development. However, upon silencing, altered gland physiology and gene expression therein suggested antagonistic roles for Av-IR1 (androinhibiting) and Av-IR2 (androstimulating). They may function in tandem with regulating neurohormones, as a conditional platform that conveys insulin signalling. <i>Wolbachia</i> infection did not alter their expression patterns: leaving the IRs unscathed, the bacteria would suppress the secretion of the neurohormones, thus inducing body-wide IR deactivation and feminisation. Adult males injected with <i>Wolbachia</i> acquired an intersexed physiology. Their phenotypes and gene expressions mirrored the silencing of Av-IR1 only, suggesting that imperfect feminisation stems from a flawed invasion of the androstimulating centre, whereas in fully feminised males invasion would be complete in early juveniles.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Away</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>Two antagonistic Insulin Receptors were characterised in <i>Armadillidium vulgare</i>.</li>\u0000 \u0000 <li>The IRs were involved in androstimulating and androinhibiting functions.</li>\u0000 \u0000 <li><i>Wolbachia</i>-induced feminisation did not prevent the expression of the IRs.</li>\u0000 \u0000 <li>Imperfectly feminised intersexes phenocopied the silencing of Av-IR1 only.</li>\u0000 \u0000 <li><i>Wolbachia</i> would deactivate the IRs by suppressing neurosecretory co-factors.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 11","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-07-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13381","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39225678","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Endocytosis of the CdtA subunit from the Haemophilus ducreyi cytolethal distending toxin","authors":"G. Robb Huhn III,&nbsp;Naly Torres-Mangual,&nbsp;John Clore,&nbsp;Lucia Cilenti,&nbsp;Teresa Frisan,&nbsp;Ken Teter","doi":"10.1111/cmi.13380","DOIUrl":"10.1111/cmi.13380","url":null,"abstract":"Many Gram‐negative pathogens produce a cytolethal distending toxin (CDT) with two cell‐binding subunits (CdtA + CdtC) and a catalytic CdtB subunit. After adhesion to the plasma membrane of a target cell, CDT moves by retrograde transport to endoplasmic reticulum. CdtB then enters the nucleus where it generates DNA breaks that lead to cell cycle arrest and apoptosis or senescence. CdtA anchors the CDT holotoxin to the plasma membrane and is thought to remain on the cell surface after endocytosis of the CdtB/CdtC heterodimer. Here, we re‐examined the potential endocytosis and intracellular transport of CdtA from the Haemophilus ducreyi CDT. We recorded the endocytosis of holotoxin‐associated CdtA with a cell‐based enzyme‐linked immunoabsorbent assay (CELISA) and visualised its presence in the early endosomes by confocal microscopy 10 min after CDT binding to the cell surface. Western blot analysis documented the rapid degradation of internalised CdtA. Most of internalised CdtB and CdtC were degraded as well. The rapid rate of CDT internalisation and turnover, which could explain why CdtA endocytosis was not detected in previous studies, suggests only a minor pool of cell‐associated CdtB reaches the nucleus. Our work demonstrates that CDT is internalised as an intact holotoxin and identifies the endosomes as the site of CdtA dissociation from CdtB/CdtC.","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 11","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13380","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39208259","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Hepatitis E virus egress and beyond – the manifold roles of the viral ORF3 protein","authors":"Mirco Glitscher,&nbsp;Eberhard Hildt","doi":"10.1111/cmi.13379","DOIUrl":"10.1111/cmi.13379","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Although the hepatitis E virus represents an uprising threat to the global community by representing the commonest cause of an acute viral hepatitis worldwide, its life cycle is grossly understudied. Albeit HEV is a non-enveloped virus, its progeny is released as quasi-enveloped virions. Thus, the responsible accessory protein pORF3 gained rising attention in the past years. It mediates viral release via the exosomal route by targeting the viral capsid to the endosomal system, more precisely to multivesicular bodies. As this is followed by quasi-envelopment, pORF3 may in terms represent a substitute to a conventional envelope protein. This feature proofs to be rather unique with respect to other enteric viruses, although the protein's role in the viral life cycle seems to reach far beyond simply maintaining release of progeny viruses. How pORF3 affects viral morphogenesis, how it mediates efficient viral release and how it supports viral spread is summarised in this microreview. With this, we aim to shed light on functions of pORF3 to gain further insights in still enigmatic aspects of the HEV life cycle.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Aways</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>HEV is released as exosome via multivesicular bodies</li>\u0000 \u0000 <li>Viral pORF3 mediates release via endosomal complexes required for transport</li>\u0000 \u0000 <li>pORF3 modulates various cellular processes in infected cells</li>\u0000 \u0000 <li>Elucidation of pORF3-related processes imply novel clinical strategies</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 12","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13379","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39192540","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}