Daniel Roderer
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View article: Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells
Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells Open
Fusobacterium nucleatum is overrepresented in the colon microbiome of colorectal cancer patients and has been associated with tumor growth enhancement and metastasis. A pivotal pathogenic factor, the autotransporter adhesin Fap2, facilitat…
View article: Characterization of the direct and indirect inhibition of apoptosis by full-length recombinant Bcl-xL monomers
Characterization of the direct and indirect inhibition of apoptosis by full-length recombinant Bcl-xL monomers Open
The Bcl-2 protein Bcl-xL is an inhibitor of intrinsic apoptosis which either directly inhibits the pore-forming Bcl-2 proteins, like Bax or Bak, or indirectly inhibits pore formation by sequestering the pro-apoptotic BH3-only activators. T…
View article: Structural basis for immune cell binding of <i>Fusobacterium nucleatum</i> via the trimeric autotransporter adhesin CbpF
Structural basis for immune cell binding of <i>Fusobacterium nucleatum</i> via the trimeric autotransporter adhesin CbpF Open
Fusobacterium nucleatum (Fn), a commensal in the human oral cavity, is overrepresented in the colon microbiota of colorectal cancer (CRC) patients and is linked to tumor chemoresistance, metastasis, and a poor therapeutic prognosis. Fn pro…
View article: Multistate kinetics of the syringe-like injection mechanism of Tc toxins
Multistate kinetics of the syringe-like injection mechanism of Tc toxins Open
Tc toxins are pore-forming virulence factors of many pathogenic bacteria. Following pH-induced conformational changes, they perforate the target membrane like a syringe to translocate toxic enzymes into a cell. Although this complex transf…
View article: Structural basis for immune cell binding of<i>Fusobacterium nucleatum</i>via the trimeric autotransporter adhesin CbpF
Structural basis for immune cell binding of<i>Fusobacterium nucleatum</i>via the trimeric autotransporter adhesin CbpF Open
Fusobacterium nucleatum (Fn), a commensal in the human oral cavity, is overrepresented in the colon microbiota of colorectal cancer (CRC) patients and is linked to tumor chemoresistance, metastasis, and a poor therapeutic prognosis. Fn pro…
View article: C. perfringens enterotoxin-claudin pore complex: Models for structure, mechanism of pore assembly and cation permeability
C. perfringens enterotoxin-claudin pore complex: Models for structure, mechanism of pore assembly and cation permeability Open
The pore-forming Clostridium perfringens enterotoxin (CPE), a common cause of foodborne diseases, facilitates Ca 2+ influx in enterocytes, leading to cell damage. Upon binding to certain claudins (e.g. claudin-4), CPE forms oligomeric pore…
View article: Nucleoside diphosphate kinase A (NME1) catalyzes its own oligophosphorylation
Nucleoside diphosphate kinase A (NME1) catalyzes its own oligophosphorylation Open
Protein phosphorylation is a central regulatory mechanism in eukaryotic cell signaling, and was recently expanded to include protein pyrophosphorylation and protein polyphosphorylation. Here, we report the discovery of yet another mode of …
View article: Structural basis of<i>Fusobacterium nucleatum</i>adhesin Fap2 interaction with receptors on cancer and immune cells
Structural basis of<i>Fusobacterium nucleatum</i>adhesin Fap2 interaction with receptors on cancer and immune cells Open
The intestinal microbiome (IM) is decisive for the human host’s health. Numerous microbiota drive the progression of colorectal cancer (CRC), the third-most common cancer worldwide. The Gram-negative Fusobacterium nucleatum (Fn) is overrep…
View article: Multi-state kinetics of the syringe-like injection mechanism of Tc toxins
Multi-state kinetics of the syringe-like injection mechanism of Tc toxins Open
Tc toxins are virulence factors of many insects and human pathogenic bacteria. They attach as soluble prepores to receptors on host cells and following acidification in the late endosome, perforate the cell membrane like a syringe to trans…
View article: Spatial N-glycan rearrangement on α<sub>5</sub>β<sub>1</sub>integrin nucleates galectin-3 oligomers to determine endocytic fate
Spatial N-glycan rearrangement on α<sub>5</sub>β<sub>1</sub>integrin nucleates galectin-3 oligomers to determine endocytic fate Open
Summary Membrane glycoproteins frequently adopt different conformations when altering between active and inactive states. Here, we discover a molecular switch that exploits dynamic spatial rearrangements of N-glycans during such conformati…
View article: Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin
Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin Open
Tc toxins deliver toxic enzymes into host cells by a unique injection mechanism. One of these enzymes is the actin ADP-ribosyltransferase TccC3, whose activity leads to the clustering of the cellular cytoskeleton and ultimately cell death.…
View article: Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin
Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin Open
Tc toxins deliver toxic enzymes into host cells by a unique injection mechanism. One of these enzymes is TccC3, an ADP-ribosyltransferase from Photorhabdus luminescens . Once TccC3 is translocated into the target cell, the enzyme ADP-ribos…
View article: Site‐specific <i>N</i>‐glycan profiles of α<sub>5</sub>β<sub>1</sub> integrin from rat liver
Site‐specific <i>N</i>‐glycan profiles of α<sub>5</sub>β<sub>1</sub> integrin from rat liver Open
Background Information Like most other cell surface proteins, α 5 β 1 integrin is glycosylated, which is required for its various activities in ways that mostly remain to be determined. Results Here, we have established the first comprehen…
View article: Glycan-dependent cell adhesion mechanism of Tc toxins
Glycan-dependent cell adhesion mechanism of Tc toxins Open
Toxin complex (Tc) toxins are virulence factors of pathogenic bacteria. Tcs are composed of three subunits: TcA, TcB and TcC. TcA facilitates receptor–toxin interaction and membrane permeation, TcB and TcC form a toxin-encapsulating cocoon…
View article: Glycan-dependent two-step cell adhesion mechanism of Tc toxins
Glycan-dependent two-step cell adhesion mechanism of Tc toxins Open
Toxin complex (Tc) toxins are virulence factors widespread in insect and human bacterial pathogens. Tcs are composed of three subunits: TcA, TcB and TcC. TcA facilitates receptor-toxin interaction and membrane permeation, TcB and TcC form …
View article: Towards the application of Tc toxins as a universal protein translocation system
Towards the application of Tc toxins as a universal protein translocation system Open
Tc toxins are bacterial protein complexes that inject cytotoxic enzymes into target cells using a syringe-like mechanism. Tc toxins are composed of a membrane translocator and a cocoon that encapsulates a toxic enzyme. The toxic enzyme var…
View article: Structure of a Tc holotoxin pore provides insights into the translocation mechanism
Structure of a Tc holotoxin pore provides insights into the translocation mechanism Open
Tc toxins are modular toxin systems of insect and human pathogenic bacteria. They are composed of a 1.4-MDa pentameric membrane translocator (TcA) and a 250-kDa cocoon (TcB and TcC) encapsulating the 30-kDa toxic enzyme (C terminus of TcC)…
View article: Common architecture of Tc toxins from human and insect pathogenic bacteria
Common architecture of Tc toxins from human and insect pathogenic bacteria Open
The pore formation and translocation machinery of Tc toxins is conserved; in contrast, the outer shell is structurally variable.
View article: Towards the application of Tc toxins as a universal protein translocation system
Towards the application of Tc toxins as a universal protein translocation system Open
Tc toxins are large bacterial protein complexes that inject cytotoxic enzymes into target cells using a sophisticated syringe-like mechanism. Tc toxins are composed of a membrane translocator and a cocoon that encapsulates a toxic enzyme. …
View article: SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM
SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM Open
Selecting particles from digital micrographs is an essential step in single-particle electron cryomicroscopy (cryo-EM). As manual selection of complete datasets—typically comprising thousands of particles—is a tedious and time-consuming pr…
View article: Conserved architecture of Tc toxins from human and insect pathogenic bacteria
Conserved architecture of Tc toxins from human and insect pathogenic bacteria Open
Tc toxin complexes use a syringe-like mechanism to penetrate the membrane and translocate a toxic enzyme into the host cytosol. They are composed of three components: TcA, TcB and TcC. Until recently, low-resolution structures of TcA from …
View article: Structure of a Tc holotoxin pore provides insights into the translocation mechanism
Structure of a Tc holotoxin pore provides insights into the translocation mechanism Open
Tc toxins are modular toxin systems that are composed of a pentameric membrane translocator (TcA) and a cocoon (TcB and TcC) encapsulating the toxic enzyme. Binding of Tcs to target cells and a pH shift trigger the conformational transitio…
View article: Assembly mechanism of the α-pore–forming toxin cytolysin A from <i>Escherichia coli</i>
Assembly mechanism of the α-pore–forming toxin cytolysin A from <i>Escherichia coli</i> Open
The cytolytic toxin cytolysin A (ClyA) from Escherichia coli is probably one of the best-characterized examples of bacterial, α-pore–forming toxins (α-PFTs). Like other PFTs, ClyA exists in a soluble, monomeric form that assembles to an an…