Lüder, Carsten Günter Kurt

[["dc.bibliographiccitation.artnumber","235"],["dc.bibliographiccitation.journal","Frontiers in Cellular and Infection Microbiology"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Ehmen, Hauke G."],["dc.contributor.author","Lüder, Carsten G. K."],["dc.date.accessioned","2019-07-09T11:51:58Z"],["dc.date.available","2019-07-09T11:51:58Z"],["dc.date.issued","2019"],["dc.description.abstract","Toxoplasma gondii is a prevalent parasite of mammals and birds including up to 30% of humans world-wide. Primary infection of immunocompetent hosts leads to a robust cell-mediated immune response, which controls but does not clear the infection, thus enabling long-term parasite persistence in brain and muscle tissues. Chronic toxoplasmosis in mice is associated with resistance to heterologous pathogens and this has been related to increased numbers of inflammatory monocytes. Here we have analyzed whether chronic T. gondii infection impacts the subset distribution and the phenotype of peripheral human monocytes in vivo and their responses to parasite infection in vitro. CD14+ monocytes from T. gondii-seropositive blood donors expressed significantly less FcγRIII (CD16) than those from seronegative controls, but they did not show a shift in the distribution of classical, intermediate and non-classical monocyte subpopulations. Percentages of CD62L+ and CD64+ monocytes were however decreased and increased, respectively, in chronically infected individuals as compared to naïve controls. Infection of monocyte-enriched PBMCs from both seropositive and seronegative individuals with T. gondii led to an increase of CD14+CD16− classical monocytes and a decrease of CD14+CD16+ double positive monocytes. Remarkably, after in vitro parasite infection, expression of the chemokine receptor CCR2 was severely impaired in monocytes from both, individuals with chronic toxoplasmosis and seronegative controls. In contrast, only monocytes from chronically infected humans but not those from controls dose-dependently up-regulated HLA-DR, DP, DQ expression following in vitro infection. Furthermore, monocyte-enriched PBMCs from seropositive individuals up-regulated IL-12 mRNA more vigorously after in vitro infection than cells from naïve controls. Collectively, our results establish that infection of humans with T. gondii exerts long-term effects on the phenotype and responsiveness of blood monocytes. This may have important implications for innate immune responses to T. gondii and unrelated pathogens."],["dc.identifier.doi","10.3389/fcimb.2019.00235"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16249"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60052"],["dc.language.iso","en"],["dc.subject.ddc","610"],["dc.title","Long-Term Impact of Toxoplasma gondii Infection on Human Monocytes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0004205"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","PLoS Neglected Tropical Diseases"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Damerow, Sebastian"],["dc.contributor.author","Hoppe, Carolin"],["dc.contributor.author","Bandini, Giulia"],["dc.contributor.author","Zarnovican, Patricia"],["dc.contributor.author","Buettner, Falk R."],["dc.contributor.author","Lueder, Carsten Guenter Kurt"],["dc.contributor.author","Ferguson, Michael A. J."],["dc.contributor.author","Routier, Francoise H."],["dc.date.accessioned","2018-11-07T09:49:10Z"],["dc.date.available","2018-11-07T09:49:10Z"],["dc.date.issued","2015"],["dc.description.abstract","Interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal) by the UDP-Glc 4'-epimerase intimately connects the biosynthesis of these two nucleotide sugars. Their de novo biosynthesis involves transformation of glucose-6-phosphate into glucose-1-phosphate by the phosphoglucomutase and subsequent activation into UDP-Glc by the specific UDP-Glc pyrophosphorylase (UGP). Besides UGP, Leishmania parasites express an uncommon UDP-sugar pyrophosphorylase (USP) able to activate both galactose-1-phosphate and glucose-1-phosphate in vitro. Targeted gene deletion of UGP alone was previously shown to principally affect expression of lipophosphoglycan, resulting in a reduced virulence. Since our attempts to delete both UGP and USP failed, deletion of UGP was combined with conditional destabilisation of USP to control the biosynthesis of UDP-Glc and UDP-Gal. Stabilisation of the enzyme produced by a single USP allele was sufficient to maintain the steady-state pools of these two nucleotide sugars and preserve almost normal glycoinositolphospholipids galactosylation, but at the apparent expense of lipophosphoglycan biosynthesis. However, under destabilising conditions, the absence of both UGP and USP resulted in depletion of UDP-Glc and UDP-Gal and led to growth cessation and cell death, suggesting that either or both of these metabolites is/are essential."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [RO 3591/2-1]; Wellcome Trust [101842]"],["dc.identifier.doi","10.1371/journal.pntd.0004205"],["dc.identifier.isi","000368344400025"],["dc.identifier.pmid","26529232"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12900"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35451"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.haserratum","/handle/2/62126"],["dc.relation.issn","1935-2735"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Depletion of UDP-Glucose and UDP-Galactose Using a Degron System Leads to Growth Cessation of Leishmania major"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Cellular and Infection Microbiology"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Rahman, Md. Taibur"],["dc.contributor.author","Swierzy, Izabela J."],["dc.contributor.author","Downie, Bryan"],["dc.contributor.author","Salinas, Gabriela"],["dc.contributor.author","Blume, Martin"],["dc.contributor.author","McConville, Malcolm J."],["dc.contributor.author","Lüder, Carsten G. K."],["dc.date.accessioned","2022-01-11T14:06:06Z"],["dc.date.available","2022-01-11T14:06:06Z"],["dc.date.issued","2021"],["dc.description.abstract","Toxoplasma gondii is an obligatory intracellular parasite that causes persistent infections in birds and mammals including ~30% of the world’s human population. Differentiation from proliferative and metabolically active tachyzoites to largely dormant bradyzoites initiates the chronic phase of infection and occurs predominantly in brain and muscle tissues. Here we used murine skeletal muscle cells (SkMCs) to decipher host cellular factors that favor T. gondii bradyzoite formation in terminally differentiated and syncytial myotubes, but not in proliferating myoblast precursors. Genome-wide transcriptome analyses of T. gondii -infected SkMCs and non-infected controls identified ~6,500 genes which were differentially expressed (DEGs) in myotubes compared to myoblasts, largely irrespective of infection. On the other hand, genes related to central carbohydrate metabolism, to redox homeostasis, and to the Nrf2-dependent stress response pathway were enriched in both infected myoblast precursors and myotubes. Stable isotope-resolved metabolite profiling indicated increased fluxes into the oxidative branch of the pentose phosphate pathway (OxPPP) in infected myoblasts and into the TCA cycle in infected myotubes. High OxPPP activity in infected myoblasts was associated with increased NADPH/NADP + ratio while myotubes exhibited higher ROS levels and lower expression of anti-oxidants and detoxification enzymes. Pharmacological reduction of ROS levels in SkMCs inhibited bradyzoite differentiation, while increased ROS induced bradyzoite formation. Thus, we identified a novel host cell-dependent mechanism that triggers stage conversion of T. gondii into persistent tissue cysts in its natural host cell type."],["dc.description.abstract","Toxoplasma gondii is an obligatory intracellular parasite that causes persistent infections in birds and mammals including ~30% of the world’s human population. Differentiation from proliferative and metabolically active tachyzoites to largely dormant bradyzoites initiates the chronic phase of infection and occurs predominantly in brain and muscle tissues. Here we used murine skeletal muscle cells (SkMCs) to decipher host cellular factors that favor T. gondii bradyzoite formation in terminally differentiated and syncytial myotubes, but not in proliferating myoblast precursors. Genome-wide transcriptome analyses of T. gondii -infected SkMCs and non-infected controls identified ~6,500 genes which were differentially expressed (DEGs) in myotubes compared to myoblasts, largely irrespective of infection. On the other hand, genes related to central carbohydrate metabolism, to redox homeostasis, and to the Nrf2-dependent stress response pathway were enriched in both infected myoblast precursors and myotubes. Stable isotope-resolved metabolite profiling indicated increased fluxes into the oxidative branch of the pentose phosphate pathway (OxPPP) in infected myoblasts and into the TCA cycle in infected myotubes. High OxPPP activity in infected myoblasts was associated with increased NADPH/NADP + ratio while myotubes exhibited higher ROS levels and lower expression of anti-oxidants and detoxification enzymes. Pharmacological reduction of ROS levels in SkMCs inhibited bradyzoite differentiation, while increased ROS induced bradyzoite formation. Thus, we identified a novel host cell-dependent mechanism that triggers stage conversion of T. gondii into persistent tissue cysts in its natural host cell type."],["dc.identifier.doi","10.3389/fcimb.2021.798549"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/97828"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-507"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","2235-2988"],["dc.rights","http://creativecommons.org/licenses/by/4.0/"],["dc.title","The Redox Homeostasis of Skeletal Muscle Cells Regulates Stage Differentiation of Toxoplasma gondii"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3511"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","3521"],["dc.bibliographiccitation.volume","122"],["dc.contributor.author","Hippe, Diana"],["dc.contributor.author","Weber, Arnim"],["dc.contributor.author","Zhou, L."],["dc.contributor.author","Chang, Donald C."],["dc.contributor.author","Haecker, Georg"],["dc.contributor.author","Lueder, Carsten Guenter Kurt"],["dc.date.accessioned","2018-11-07T11:23:48Z"],["dc.date.available","2018-11-07T11:23:48Z"],["dc.date.issued","2009"],["dc.description.abstract","In order to accomplish their life style, intracellular pathogens, including the apicomplexan Toxoplasma gondii, subvert the innate apoptotic response of infected host cells. However, the precise mechanisms of parasite interference with the mitochondrial apoptotic pathway remain unknown. Here, we used the conditional expression of the BH3-only protein Bim(S) to pinpoint the interaction of T. gondii with the intrinsic pathway of apoptosis. Infection of epithelial cells with T. gondii dose-dependently abrogated Bim(S)-triggered release of cytochrome c from host-cell mitochondria into the cytosol, induction of activity of caspases 3, 7 and 9, and chromatin condensation. Furthermore, inhibition of apoptosis in parasite-infected lymphocytes counteracted death of Toxoplasma-infected host cells. Although total cellular levels and mitochondrial targeting of BimS was not altered by the infection, the activation of pro-apoptotic effector proteins Bax and Bak was strongly impaired. Inhibition of Bax and Bak activation by T. gondii was seen with regard to their conformational changes, the cytosol-to-mitochondria targeting and the oligomerization of Bax but not their cellular protein levels. Blockade of Bax and Bak activation was not mediated by the upregulation of antiapoptotic Bcl-2-like proteins following infection. Further, the BH3-mimetic ABT-737 failed to overcome the Toxoplasma-imposed inhibition of Bim(S)-triggered apoptosis. These results indicate that T. gondii targets activation of pro-apoptotic Bax and Bak to inhibit the apoptogenic function of mitochondria and to increase host-cell viability."],["dc.identifier.doi","10.1242/jcs.050963"],["dc.identifier.isi","000269839900010"],["dc.identifier.pmid","19737817"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6225"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56267"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","0021-9533"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Toxoplasma gondii infection confers resistance against Bim(S)-induced apoptosis by preventing the activation and mitochondrial targeting of pro-apoptotic Bax"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","203"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Microbial cell (Graz, Austria)"],["dc.bibliographiccitation.lastpage","211"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Lüder, Carsten G K"],["dc.contributor.author","Rahman, Taibur"],["dc.date.accessioned","2019-07-09T11:43:27Z"],["dc.date.available","2019-07-09T11:43:27Z"],["dc.date.issued","2017-06-22"],["dc.description.abstract","The unicellular parasite Toxoplasma gondii infects warm-blooded animals and humans, and it is highly prevalent throughout the world. Infection of immunocompetent hosts is usually asymptomatic or benign but leads to long-term parasite persistence mainly within neural and muscular tissues. The transition from acute primary infection towards chronic toxoplasmosis is accompanied by a developmental switch from fast replicating and metabolically highly active tachyzoites to slow replicating and largely dormant bradyzoites within tissue cysts. Such developmental differentiation is critical for T. gondii in order to complete its life cycle and for pathogenesis. Herein, we summarize accumulating evidence indicating a major impact of the host cell physiology on stage conversion between the tachyzoite and the bradyzoite stage of the parasite. Withdrawal from cell cycle progression, proinflammatory responses, reduced availability of nutrients and extracellular adenosine can indeed induce tachyzoite-to-bradyzoite differentiation and tissue cyst formation. In contrast, high glycolytic activity as indicated by increased lactate secretion can inhibit bradyzoite formation. These examples argue for the intriguing possibility that after dissemination within its host, T. gondii can sense its cellular microenvironment to initiate the developmental program towards the bradyzoite stage in distinct cells. This may also explain the predominant localization of T. gondii in neural and muscular tissues during chronic toxoplasmosis."],["dc.description.abstract","The unicellular parasite Toxoplasma gondii infects warm-blooded animals and humans, and it is highly prevalent throughout the world. Infection of immunocompetent hosts is usually asymptomatic or benign but leads to long-term parasite persistence mainly within neural and muscular tissues. The transition from acute primary infection towards chronic toxoplasmosis is accompanied by a developmental switch from fast replicating and metabolically highly active tachyzoites to slow replicating and largely dormant bradyzoites within tissue cysts. Such developmental differentiation is critical for T. gondii in order to complete its life cycle and for pathogenesis. Herein, we summarize accumulating evidence indicating a major impact of the host cell physiology on stage conversion between the tachyzoite and the bradyzoite stage of the parasite. Withdrawal from cell cycle progression, proinflammatory responses, reduced availability of nutrients and extracellular adenosine can indeed induce tachyzoite-to-bradyzoite differentiation and tissue cyst formation. In contrast, high glycolytic activity as indicated by increased lactate secretion can inhibit bradyzoite formation. These examples argue for the intriguing possibility that after dissemination within its host, T. gondii can sense its cellular microenvironment to initiate the developmental program towards the bradyzoite stage in distinct cells. This may also explain the predominant localization of T. gondii in neural and muscular tissues during chronic toxoplasmosis."],["dc.identifier.doi","10.15698/mic2017.07.579"],["dc.identifier.pmid","28706936"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14539"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58893"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2311-2638"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Impact of the host on Toxoplasma stage differentiation."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","196"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Memorias do Instituto Oswaldo Cruz"],["dc.bibliographiccitation.lastpage","200"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Lüder, Carsten"],["dc.contributor.author","Groß, Uwe"],["dc.contributor.author","Fonseca Ferreira-da-Silva, Marialice da"],["dc.contributor.author","Mendonça Rodrigues, Renata"],["dc.contributor.author","Ferreira de Andrade, Elisabete"],["dc.contributor.author","Carvalho, Laís de"],["dc.contributor.author","Santos Barbosa, Helene"],["dc.date.accessioned","2011-03-10T15:14:02Z"],["dc.date.accessioned","2021-10-27T13:22:34Z"],["dc.date.available","2011-03-10T15:14:02Z"],["dc.date.available","2021-10-27T13:22:34Z"],["dc.date.issued","2009"],["dc.description.abstract","Although the predilection for Toxoplasma gondii to form cysts in the nervous system and skeletal and heart muscles has been described for more than fifty years, skeletal muscle cells (SkMCs) have not been explored as a host cell type to study the Toxoplasma-host cell interaction and investigate the intracellular development of the parasite. Morphological aspects of the initial events in the Toxoplasma-SkMC interaction were analysed and suggest that there are different processes of protozoan adhesion and invasion and of the subsequent fate of the parasite inside the parasitophorous vacuole (PV). Using scanning electron microscopy,Toxoplasma tachyzoites from the mouse-virulent RH strain were found to be attached to SkMCs by the anterior or posterior region of the body, with or without expansion of the SkMC membrane. This suggests that different types of parasite internalization occurred. Asynchronous multiplication and differentiation of T. gondii were observed. Importantly, intracellular parasites were seen to display high amounts of amylopectin granules in their cytoplasm, indicating that tachyzoites of the RH strain were able to differentiate spontaneously into bradyzoites in SkMCs. This stage conversion occurred in approximately 3% of the PVs. This is particularly intriguing as tachyzoites of virulent Toxoplasma strains are not thought to be prone to cyst formation. We discuss whether biological differences in host cells are crucial to Toxoplasma stage conversion and suggest that important questions concerning the host cell type and its relevance in Toxoplasma differentiation are still unanswered."],["dc.identifier.doi","10.1590/S0074-02762009000200012"],["dc.identifier.fs","396270"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5960"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92106"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","1678-8060"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","Spontaneous stage differentiation of mouse-virulent Toxoplasma gondii RH parasites in skeletal muscle cells: an ultrastructural evaluation."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","104"],["dc.bibliographiccitation.journal","Parasites & Vectors"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Jimenez-Ruiz, Antonio"],["dc.contributor.author","Fernando Alzate, Juan"],["dc.contributor.author","MacLeod, Ewan Thomas"],["dc.contributor.author","Lueder, Carsten Guenter Kurt"],["dc.contributor.author","Fasel, Nicolas"],["dc.contributor.author","Hurd, Hilary"],["dc.date.accessioned","2018-11-07T08:37:01Z"],["dc.date.available","2018-11-07T08:37:01Z"],["dc.date.issued","2010"],["dc.description.abstract","The execution of the apoptotic death program in metazoans is characterized by a sequence of morphological and biochemical changes that include cell shrinkage, presentation of phosphatidylserine at the cell surface, mitochondrial alterations, chromatin condensation, nuclear fragmentation, membrane blebbing and the formation of apoptotic bodies. Methodologies for measuring apoptosis are based on these markers. Except for membrane blebbing and formation of apoptotic bodies, all other events have been observed in most protozoan parasites undergoing cell death. However, while techniques exist to detect these markers, they are often optimised for metazoan cells and therefore may not pick up subtle differences between the events occurring in unicellular organisms and multicellular organisms. In this review we discuss the markers most frequently used to analyze cell death in protozoan parasites, paying special attention to changes in cell morphology, mitochondrial activity, chromatin structure and plasma membrane structure/permeability. Regarding classical regulators/executors of apoptosis, we have reviewed the present knowledge of caspase-like and nuclease activities."],["dc.description.sponsorship","Ministerio de Educacion y Ciencia, Spain [SAF 2006-12713-CO2-O2]"],["dc.identifier.doi","10.1186/1756-3305-3-104"],["dc.identifier.isi","000284705400001"],["dc.identifier.pmid","21062457"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5781"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18434"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1756-3305"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","Apoptotic markers in protozoan parasites"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e81069"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Tareen, Abdul Malik"],["dc.contributor.author","Lueder, Carsten Guenter Kurt"],["dc.contributor.author","Zautner, Andreas Erich"],["dc.contributor.author","Gross, Uwe"],["dc.contributor.author","Heimesaat, Markus M."],["dc.contributor.author","Bereswill, Stefan"],["dc.contributor.author","Lugert, Raimond"],["dc.date.accessioned","2018-11-07T09:17:27Z"],["dc.date.available","2018-11-07T09:17:27Z"],["dc.date.issued","2013"],["dc.description.abstract","Adherence of Campylobacter jejuni to its particular host cells is mediated by several pathogen proteins. We screened a transposon-based mutant library of C. jejuni in order to identify clones with an invasion deficient phenotype towards Caco2 cells and detected a mutant with the transposon insertion in gene cj0268c. In vitro characterization of a generated non-random mutant, the mutant complemented with an intact copy of cj0268c and parental strain NCTC 11168 confirmed the relevance of Cj0268c in the invasion process, in particular regarding adherence to host cells. Whereas Cj0268c does not impact autoagglutination or motility of C. jejuni, heterologous expression in E. coli strain DH5 alpha enhanced the potential of the complemented E. coli strain to adhere to Caco2 cells significantly and, thus, indicates that Cj0268c does not need to interact with other C. jejuni proteins to develop its adherence-mediating phenotype. Flow cytometric measurements of E. coli expressing Cj0268c indicate a localization of the protein in the periplasmic space with no access of its C-terminus to the bacterial surface. Since a respective knockout mutant possesses clearly reduced resistance to Triton X-100 treatment, Cj0268c contributes to the stability of the bacterial cell wall. Finally, we could show that the presence of cj0268c seems to be ubiquitous in isolates of C. jejuni and does not correlate with specific clonal groups regarding pathogenicity or pathogen metabolism."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2013"],["dc.identifier.doi","10.1371/journal.pone.0081069"],["dc.identifier.isi","000327546400048"],["dc.identifier.pmid","24303031"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9509"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28175"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","The Campylobacter jejuni Cj0268c Protein Is Required for Adhesion and Invasion In Vitro"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","7229"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific reports"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Swierzy, Izabela J."],["dc.contributor.author","Händel, Ulrike"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Jarek, Michael"],["dc.contributor.author","Scharfe, Maren"],["dc.contributor.author","Schlüter, Dirk"],["dc.contributor.author","Lüder, Carsten G. K."],["dc.date.accessioned","2019-07-09T11:43:39Z"],["dc.date.available","2019-07-09T11:43:39Z"],["dc.date.issued","2017-08-03"],["dc.description.abstract","The apicomplexan parasite Toxoplasma gondii infects various cell types in avian and mammalian hosts including humans. Infection of immunocompetent hosts is mostly asymptomatic or benign, but leads to development of largely dormant bradyzoites that persist predominantly within neurons and muscle cells. Here we have analyzed the impact of the host cell type on the co-transcriptomes of host and parasite using high-throughput RNA sequencing. Murine cortical neurons and astrocytes, skeletal muscle cells (SkMCs) and fibroblasts differed by more than 16,200 differentially expressed genes (DEGs) before and after infection with T. gondii. However, only a few hundred of them were regulated by infection and these largely diverged in neurons, SkMCs, astrocytes and fibroblasts indicating host cell type-specific transcriptional responses after infection. The heterogeneous transcriptomes of host cells before and during infection coincided with ~5,400 DEGs in T. gondii residing in different cell types. Finally, we identified gene clusters in both T. gondii and its host, which correlated with the predominant parasite persistence in neurons or SkMCs as compared to astrocytes or fibroblasts. Thus, heterogeneous expression profiles of different host cell types and the parasites' ability to adapting to them may govern the parasite-host cell interaction during toxoplasmosis."],["dc.identifier.doi","10.1038/s41598-017-07838-w"],["dc.identifier.pmid","28775382"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14610"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58935"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Divergent co-transcriptomes of different host cells infected with Toxoplasma gondii reveal cell type-specific host-parasite interactions."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Immunology"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Nast, Roswitha"],["dc.contributor.author","Choepak, Tenzin"],["dc.contributor.author","Lüder, Carsten G. K."],["dc.date.accessioned","2021-04-14T08:32:39Z"],["dc.date.available","2021-04-14T08:32:39Z"],["dc.date.issued","2020"],["dc.description.abstract","Host defense against the human pathogen Toxoplasma gondii depends on secretion of interferon (IFN)-γ and subsequent activation of monocytic cells to combat intracellular parasites. Previous studies have shown that T. gondii evades IFN-γ-mediated immunity by secreting the effector TgIST into the host cell where it binds to STAT1, strengthens its DNA binding activity and recruits the Mi-2/NuRD complex to STAT1-responsive promoters. Here we investigated the impact of the host chromatin environment on parasite interference with IFN-γ-induced gene expression. Luciferase reporters under control of primary and secondary IFN-γ response promoters were only inhibited by T. gondii when they were stably integrated into the host genome but not when expressed from a plasmid vector. Absence of CpG islands upstream and/or downstream of the transcriptional start site allowed more vigorous up-regulation by IFN-γ as compared to CpG-rich promoters. Remarkably, it also favored parasite interference with IFN-γ-induced gene expression indicating that nucleosome occupancy at IFN-γ-responsive promoters is important. Promoter DNA of IFN-γ-responsive genes remained largely non-methylated in T. gondii-infected cells, and inhibition of DNA methylation did not impact parasite interference with host responses. IFN-γ up-regulated histone marks H4ac, H3K9ac, and H3K4me3 but down-regulated H3S10p at primary and secondary response promoters. Infection with T. gondii abolished histone modification, whereas total nuclear activities of histone acetyl transferases and histone deacetylases were not altered. Taken together, our study reveals a critical impact of the host chromatin landscape at IFN-γ-activated promoters on their inhibition by T. gondii with a comprehensive blockade of histone modifications at parasite-inactivated promoters."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2020"],["dc.identifier.doi","10.3389/fimmu.2020.581241"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17577"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83974"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1664-3224"],["dc.rights","CC BY 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Epigenetic Control of IFN-γ Host Responses During Infection With Toxoplasma gondii"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]