Cellular Microbiology最新文献

{"title":"Entry of the Varicellovirus Canid herpesvirus 1 into Madin–Darby canine kidney epithelial cells is pH-independent and occurs via a macropinocytosis-like mechanism but without increase in fluid uptake","authors":"Mohamed Eisa,&nbsp;Hamza Loucif,&nbsp;Julien van Grevenynghe,&nbsp;Angela Pearson","doi":"10.1111/cmi.13398","DOIUrl":"10.1111/cmi.13398","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p><i>Canid herpesvirus</i> 1 (CHV-1) is a <i>Varicellovirus</i> that causes self-limiting infections in adult dogs but morbidity and mortality in puppies. Using a multipronged approach, we discovered the CHV-1 entry pathway into Madin–Darby canine kidney (MDCK) epithelial cells. We found that CHV-1 triggered extensive host cell membrane lamellipodial ruffling and rapid internalisation of virions in large, uncoated vacuoles, suggestive of macropinocytosis. Treatment with inhibitors targeting key macropinocytosis factors, including inhibitors of Na⁺/H⁺ exchangers, F-actin, myosin light-chain kinase, protein kinase C, p21-activated kinase, phosphatidylinositol-3-kinase and focal adhesion kinase, significantly reduced viral replication. Moreover, the effect was restricted to exposure to the inhibitors early in infection, confirming a role for the macropinocytic machinery during entry. The profile of inhibitors also suggested a role for signalling via integrins and receptor tyrosine kinases in viral entry. In contrast, inhibitors of clathrin, caveolin, microtubules and endosomal acidification did not affect CHV-1 entry into MDCK cells. We found that the virus colocalised with the fluid-phase uptake marker dextran; however, surprisingly, CHV-1 infection did not enhance the uptake of dextran. Thus, our results indicate that CHV-1 uses a macropinocytosis-like, pH-independent entry pathway into MDCK cells, which nevertheless is not based on stimulation of fluid uptake.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Aways</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>CHV-1 enters epithelial cells via a macropinocytosis-like mechanism.</li>\u0000 \u0000 <li>CHV-1 induces extensive lamellipodial ruffling.</li>\u0000 \u0000 <li>CHV-1 entry into MDCK cells is pH-independent.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 12","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-10-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39557986","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: The fungivorous amoeba Protostelium aurantium targets redox homeostasis and cell wall integrity during intracellular killing of Candida parapsilosis (Cellular Microbiology 11/2021)","authors":"Silvia Radosa,&nbsp;Jakob L. Sprague,&nbsp;Siu-Hin Lau,&nbsp;Renáta Tóth,&nbsp;Jörg Linde,&nbsp;Thomas Krüger,&nbsp;Marcel Sprenger,&nbsp;Lydia Kasper,&nbsp;Martin Westermann,&nbsp;Olaf Kniemeyer,&nbsp;Bernhard Hube,&nbsp;Axel A. Brakhage,&nbsp;Attila Gácser,&nbsp;Falk Hillmann","doi":"10.1111/cmi.13396","DOIUrl":"10.1111/cmi.13396","url":null,"abstract":"<p>The fungivorous amoeba <i>Protostelium aurantium</i> feeds on a wide range of fungal species. The image shows amoebae digesting GFP-expressing cells of the human pathogenic yeast <i>Candida parapsilosis</i>. For further details, readers are referred to the article by Radosa et al. on p. e13389 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 11","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-10-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/cmi.13396","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41610318","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":"Dengue virus replication enhances labile zinc pools by modulation of ZIP8","authors":"Aleksha Panwar,&nbsp;Jigme Wangchuk,&nbsp;Meenakshi Kar,&nbsp;Rakesh Lodha,&nbsp;Guruprasad R. Medigeshi","doi":"10.1111/cmi.13395","DOIUrl":"10.1111/cmi.13395","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Zinc-dependent viral proteins rely on intracellular zinc homeostasis for successful completion of infectious life-cycle. Here, we report that the intracellular labile zinc levels were elevated at early stages of dengue virus (DENV) infection in hepatic cells and this increase in free zinc was abolished in cells infected with UV-inactivated virus or with a DENV replication inhibitor implicating a role for zinc homeostasis in viral RNA replication. This change in free zinc was mediated by zinc transporter, ZIP8, as siRNA-mediated knockdown of ZIP8 resulted in abrogation of increase in free zinc levels leading to significant reduction in DENV titers suggesting a crucial role for ZIP8 in early stages of DENV replication. Furthermore, elevated free zinc levels correlated with high copy numbers of dengue genome in peripheral blood leukocytes obtained from dengue patients compared to healthy controls suggesting a critical role for zinc homeostasis in dengue infection.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Aways</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>Dengue virus utilises cellular zinc homeostasis during replication of its RNA.</li>\u0000 \u0000 <li>ZIP8 upregulates free zinc levels during dengue virus replication.</li>\u0000 \u0000 <li>Enhanced viremia associates with elevated intracellular free zinc in dengue.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 12","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7612096/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39518423","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":"Cover Image: Candidalysin delivery to the invasion pocket is critical for host epithelial damage induced by Candida albicans (Cellular Microbiology 10/2021)","authors":"Selene Mogavero,&nbsp;Frank M. Sauer,&nbsp;Sascha Brunke,&nbsp;Stefanie Allert,&nbsp;Daniela Schulz,&nbsp;Stephanie Wisgott,&nbsp;Nadja Jablonowski,&nbsp;Osama Elshafee,&nbsp;Thomas Krüger,&nbsp;Olaf Kniemeyer,&nbsp;Axel A. Brakhage,&nbsp;Julian R. Naglik,&nbsp;Edward Dolk,&nbsp;Bernhard Hube","doi":"10.1111/cmi.13393","DOIUrl":"10.1111/cmi.13393","url":null,"abstract":"<p><i>Candida albicans</i> hyphae secreting the peptide toxin candidalysin (green) during invasion of epithelial cells. The toxin accumulates in the “invasion pocket” and damages the host cell. For further details, readers are referred to the article by Mogavero et al. on p. e13378 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 10","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/cmi.13393","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46979064","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":"Bacterial Atlas of Mouse Gut Microbiota","authors":"Mengqi Chu, Xiaobo Zhang","doi":"10.21203/rs.3.rs-829178/v1","DOIUrl":"https://doi.org/10.21203/rs.3.rs-829178/v1","url":null,"abstract":"Background: Mouse model is one of of the most widely used animal models for exploring the roles of human gut microbiota, a complex system involving in human immunity and metabolism. However, the structure of mouse gut bacterial community has not been explored at a large scale. To address this concern, the diversity and composition of the gut bacteria of 600 mice was characterized in this study. Results: The results showed that the bacteria belonging to 8 genera were found in the gut microbiota of all mouse individuals, indicating that the 8 bacteria were the core bacteria of mouse gut microbiota. The dominant genera of the mouse gut bacteria contained 15 bacterial genera. It was found that the bacteria in the gut microbiota were mainly involved in host’s metabolisms via the collaborations between the gut bacteria. The further analysis demonstrated that the composition of mouse gut microbiota was similar to that of human gut microbiota. Conclusion: Our study presented a bacterial atlas of mouse gut microbiota, providing a solid basis for investing the bacterial communities of mouse gut microbiota.","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":" ","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49217555","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":"Egress of archaeal viruses","authors":"Diana P. Baquero,&nbsp;Junfeng Liu,&nbsp;David Prangishvili","doi":"10.1111/cmi.13394","DOIUrl":"10.1111/cmi.13394","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Viruses of Archaea, arguably the most mysterious part of the virosphere due to their unique morphotypes and genome contents, exploit diverse mechanisms for releasing virus progeny from the host cell. These include virus release as a result of the enzymatic degradation of the cell wall or budding through it, common for viruses of Bacteria and Eukarya, as well as a unique mechanism of virus egress through small polygonal perforations on the cell surface. The process of the formation of these perforations includes the development of pyramidal structures on the membrane of the infected cell, which gradually grow by the expansion of their faces and eventually open like flower petals. This mechanism of virion release is operating exclusively in cells of hyperthermophilic hosts from the phylum Crenarchaeota, which are encased solely by a layer of surface proteins, S-layer. The review focuses on recent developments in understanding structural and biochemical details of all three types of egress mechanisms of archaeal viruses.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Aways</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>Many archaeal viruses exit the host via polygonal perforations on the cell membrane.</li>\u0000 \u0000 <li>The molecular mechanism of exit via specific apertures is unique for archaeal viruses.</li>\u0000 \u0000 <li>Some enveloped archaeal viruses exploit the budding mechanism for egress.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 12","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13394","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39411184","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":"Blockade of endoplasmic reticulum stress-induced cell death by Ureaplasma parvum vacuolating factor","authors":"Fumiko Nishiumi,&nbsp;Yasuhiro Kawai,&nbsp;Yukiko Nakura,&nbsp;Michinobu Yoshimura,&nbsp;Heng Ning Wu,&nbsp;Mitsuhide Hamaguchi,&nbsp;Shigeyuki Kakizawa,&nbsp;Yo Suzuki,&nbsp;John I. Glass,&nbsp;Itaru Yanagihara","doi":"10.1111/cmi.13392","DOIUrl":"10.1111/cmi.13392","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Previously, we found that <i>Ureaplasma parvum</i> internalised into HeLa cells and cytosolic accumulation of galectin-3. <i>U. parvum</i> induced the host cellular membrane damage and survived there. Here, we conducted vesicular trafficking inhibitory screening in yeast to identify <i>U. parvum</i> vacuolating factor (UpVF). <i>U. parvum</i> triggered endoplasmic reticulum (ER) stress and upregulated the unfolded protein response-related factors, including BiP, P-eIF2 and IRE1 in the host cells, but it blocked the induction of the downstream apoptotic factors. MicroRNA library screening of <i>U. parvum</i>-infected cells and UpVF-transfected cells identified miR-211 and miR-214 as the negative regulators of the apoptotic cascade under ER stress. Transient expression of UpVF induced HeLa cell death with intracellular vacuolization; however, some stable UpVF transformant survived. <i>U. parvum</i>-infected cervical cell lines showed resistance to actinomycin D, and UpVF stable transformant cell lines exhibited resistance to X-ray irradiation, as well as cisplatin and paclitaxel. UpVF expressing cervical cancer xenografts in nude mice also acquired resistance to cisplatin and paclitaxel. A mycoplasma expression vector based on <i>Mycoplasma mycoides,</i> Syn-MBA (multiple banded antigen)-UpVF, reduced HeLa cell survival compared with that of Syn-MBA after 72 hr of infection. These findings together suggest novel mechanisms for <i>Ureaplasma</i> infection and the possible implications for cervical cancer malignancy.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Aways</h3>\u0000 \u0000 <p>• Ureaplasmal novel virulence factor, UpVF, was identified.</p>\u0000 \u0000 <p>• UpVF triggered ER stress but suppressed apoptotic cascade via miR-211 and -214.</p>\u0000 \u0000 <p>• UpVF conferred resistance to anticancer treatments both in vivo and in vitro.</p>\u0000 \u0000 <p>• Dual expression of MBA and UpVF in JCVI-syn3B showed host cell damage.</p>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 12","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13392","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39391235","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":"BSC2 induces multidrug resistance via contributing to the formation of biofilm in Saccharomyces cerevisiae","authors":"Zhiwei Huang,&nbsp;Hongsheng Dai,&nbsp;Xiaoyu Zhang,&nbsp;Qiao Wang,&nbsp;Jing Sun,&nbsp;Yunxia Deng,&nbsp;Ping Shi","doi":"10.1111/cmi.13391","DOIUrl":"10.1111/cmi.13391","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Biofilm plays an important role in fungal multidrug resistance (MDR). Our previous studies showed that <i>BSC2</i> is involved in resistance to amphotericin B (AMB) through antioxidation in <i>Saccharomyces cerevisiae</i>. In this study, the overexpression of <i>BSC2</i> and <i>IRC23</i> induced strong MDR in <i>S. cerevisiae</i>. <i>BSC2</i>-overexpression affected cellular flocculation, cell surface hydrophobicity, biofilm formation and invasive growth. However, it failed to induce caspofungin (CAS) resistance and affect the invasive growth in <i>FLO</i> mutant strains (<i>FLO11</i>Δ, <i>FLO1</i>Δ, <i>FLO8</i>Δ and <i>TUP1</i>Δ). Furthermore, the overexpression of <i>BSC2</i> compensated for chitin synthesis defects to maintain the cell wall integrity and significantly reduced the cell morphology abnormality induced by CAS. However, it could not repair the cell wall damage caused by CAS in the <i>FLO</i> mutant strains. Although <i>BSC2</i> overexpression increased the level of mannose in the cell wall, <i>DPM1</i> overexpression in both BY4741 and <i>bsc2</i>∆ could confer resistance to CAS and AMB. In addition, <i>BSC2</i> overexpression significantly increased the mRNA expression of <i>FLO11</i>, <i>FLO1</i>, <i>FLO8</i> and <i>TUP1</i>. <i>BSC2</i> may function as a regulator of <i>FLO</i> genes and be involved in cell wall integrity in yeast. Taken together, our data demonstrate that <i>BSC2</i> induces MDR in a <i>FLO</i> pathway-dependent manner via contributing to the formation of biofilms in <i>S. cerevisiae</i>.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Aways</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>Overexpression of <i>BSC2</i> induced strong MDR in <i>S. cerevisiae</i>.</li>\u0000 \u0000 <li><i>BSC2</i> affected cellular flocculation, CSH, biofilm formation and invasive growth.</li>\u0000 \u0000 <li><i>BSC2</i> could not repair the cell wall damage caused by CAS in the <i>FLO</i> mutants.</li>\u0000 \u0000 <li><i>BSC2</i> may function as a regulator of <i>FLO</i> genes to maintain cell wall integrity.</li>\u0000 \u0000 <li><i>BSC2</i> promotes biofilm formation in a <i>FLO</i> pathway-dependent manner to induce MDR.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 12","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-09-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13391","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39384095","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":"Rickettsia conorii survival in THP-1 macrophages involves host lipid droplet alterations and active rickettsial protein production","authors":"Paige E. Allen,&nbsp;Robert C. Noland,&nbsp;Juan J. Martinez","doi":"10.1111/cmi.13390","DOIUrl":"10.1111/cmi.13390","url":null,"abstract":"&lt;div&gt;\u0000 \u0000 \u0000 &lt;section&gt;\u0000 \u0000 &lt;p&gt;&lt;i&gt;Rickettsia conorii&lt;/i&gt; is a Gram-negative, cytosolic intracellular bacterium that has classically been investigated in terms of endothelial cell infection. However, &lt;i&gt;R. conorii&lt;/i&gt; and other human pathogenic &lt;i&gt;Rickettsia&lt;/i&gt; species have evolved mechanisms to grow in various cell types, including macrophages, during mammalian infection. During infection of these phagocytes, &lt;i&gt;R. conorii&lt;/i&gt; shifts the host cell's overall metabolism towards an anti-inflammatory M2 response, metabolically defined by an increase in host lipid metabolism and oxidative phosphorylation. Lipid metabolism has more recently been identified as a key regulator of host homeostasis through modulation of immune signalling and metabolism. Intracellular pathogens have adapted mechanisms of hijacking host metabolic pathways including host lipid catabolic pathways for various functions required for growth and survival. In the present study, we hypothesised that alterations of host lipid droplets initiated by lipid catabolic pathways during &lt;i&gt;R. conorii&lt;/i&gt; infection is important for bacterial survival in macrophages. Herein, we determined that host lipid droplet modulation is initiated early during &lt;i&gt;R. conorii&lt;/i&gt; infection, and these alterations rely on active bacteria and lipid catabolic pathways. We also find that these lipid catabolic pathways are essential for efficient bacterial survival. Unlike the mechanisms used by other intracellular pathogens, the catabolism of lipid droplets induced by &lt;i&gt;R. conorii&lt;/i&gt; infection is independent of upstream host peroxisome proliferator-activated receptor-alpha (PPARα) signalling. Inhibition of PPARɣ signalling and lipid droplet accumulation in host cells cause a significant decrease in &lt;i&gt;R. conorii&lt;/i&gt; survival suggesting a negative correlation with lipid droplet production and &lt;i&gt;R. conorii&lt;/i&gt; survival. Together, these results strongly suggest that the modulation of lipid droplets in macrophage cells infected by &lt;i&gt;R. conorii&lt;/i&gt; is an important and underappreciated aspect of the infection process.&lt;/p&gt;\u0000 &lt;/section&gt;\u0000 \u0000 &lt;section&gt;\u0000 \u0000 &lt;h3&gt; Take Aways&lt;/h3&gt;\u0000 \u0000 &lt;div&gt;\u0000 &lt;ul&gt;\u0000 \u0000 &lt;li&gt;Host lipid droplets are differentially altered in early and replicative stages of THP-1 macrophage infection with &lt;i&gt;R. conorii&lt;/i&gt;.&lt;/li&gt;\u0000 \u0000 &lt;li&gt;Lipid droplet alterations are initiated in a bacterial-dependent manner and do not require host peroxisome proliferator-activated receptors α or ɣ activation.&lt;/li&gt;\u0000 \u0000 &lt;li&gt;Pharmacological inhibition of host lipid catabolic processes during &lt;i&gt;R. conorii&lt;/i&gt; infection indicates a requirement of lipid catabolism for bacterial survival and initiation of lipid droplet modulation.&lt;/li&gt;\u0000 \u0000 ","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 11","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-08-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13390","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39369562","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":"The fungivorous amoeba Protostelium aurantium targets redox homeostasis and cell wall integrity during intracellular killing of Candida parapsilosis","authors":"Silvia Radosa,&nbsp;Jakob L. Sprague,&nbsp;Siu-Hin Lau,&nbsp;Renáta Tóth,&nbsp;Jörg Linde,&nbsp;Thomas Krüger,&nbsp;Marcel Sprenger,&nbsp;Lydia Kasper,&nbsp;Martin Westermann,&nbsp;Olaf Kniemeyer,&nbsp;Bernhard Hube,&nbsp;Axel A. Brakhage,&nbsp;Attila Gácser,&nbsp;Falk Hillmann","doi":"10.1111/cmi.13389","DOIUrl":"10.1111/cmi.13389","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Predatory interactions among microbes are major evolutionary driving forces for biodiversity. The fungivorous amoeba <i>Protostelium aurantium</i> has a wide fungal food spectrum including foremost pathogenic members of the genus <i>Candida</i>. Here we show that upon phagocytic ingestion by the amoeba, <i>Candida parapsilosis</i> is confronted with an oxidative burst and undergoes lysis within minutes of processing in acidified phagolysosomes. On the fungal side, a functional genomic approach identified copper and redox homeostasis as primary targets of amoeba predation, with the highly expressed copper exporter gene <i>CRP1</i> and the peroxiredoxin gene <i>PRX1</i> contributing to survival when encountered with <i>P. aurantium</i>. The fungicidal activity was largely retained in intracellular vesicles of the amoebae. Following their isolation, the content of these vesicles induced immediate killing and lysis of <i>C. parapsilosis</i> in vitro. Proteomic analysis identified 56 vesicular proteins from <i>P. aurantium</i>. Although completely unknown proteins were dominant, many of them could be categorised as hydrolytic enzymes targeting the fungal cell wall, indicating that fungal cell wall structures are under selection pressure by predatory phagocytes in natural environments.</p>\u0000 </section>\u0000 \u0000 <section>\u0000 \u0000 <h3> Take Away</h3>\u0000 \u0000 <div>\u0000 <ul>\u0000 \u0000 <li>The amoeba <i>Protostelium aurantium</i> feeds on fungi, such as <i>Candida parapsilosis</i>.</li>\u0000 \u0000 <li>Ingested yeast cells are exposed to reactive oxygen species.</li>\u0000 \u0000 <li>A copper exporter and a peroxiredoxin contribute to fungal defence.</li>\u0000 \u0000 <li>Yeast cells undergo intracellular lysis.</li>\u0000 \u0000 <li>Lysis occurs via a cocktail of hydrolytic enzymes from intracellular vesicles.</li>\u0000 </ul>\u0000 </div>\u0000 </section>\u0000 </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 11","pages":""},"PeriodicalIF":3.4,"publicationDate":"2021-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13389","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39382953","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}