a polymorphic helix of a salmonella needle protein

Frontiers

Bacterial pathogens utilize a myriad of mechanisms to invade mammalian hosts damage tissue sites and evade the immune system One essential strategy of Gram-negative bacteria is the secretion of virulence factors through both inner and outer membranes to reach a potential target Most secretion systems are harbored in mobile elements including transposons plasmids pathogenicity islands

ERC Weakinteract

2020-5-21Our group is running an ERC project (Starting Grant to A Loquet) for the period 2015-2020 The project is called Weakinteract for "Weak interactions in self-organizations studied by NMR spectroscopy in the supramolecular solid-state" This project is related to the development of solid-state NMR methods to tackle complex supramolecular assemblies in the fields of biology and chemistry

Propulsive nanomachines: the convergent evolution of

The three domains of life independently evolved propulsive nanomachines (A) Top: Cartoon of Chlamydomonas reinhardtii to illustrate how cilia whip (left) or undulate non-reciprocally (right) to propel unicellular eukaryotic microbes Bottom: Cilia are hundreds of nanometers wide membrane-embedded and use ATP hydrolysis along the length of their structure to drive a beating motion at tens of

Bacterial flagellar motor: Current Biology

There is a homologous structure called the needle structure assembled by the same kind of transport apparatus used by pathogenic species (such as Salmonella) to inject virulence factors into eukaryotic cells Some argue that the flagellar rotary motor evolved from the needle structure but it was probably the other way around since

Investigations of binding mode insight in Salmonella

2017-1-1Salmonella typhi is a Gram-negative pathogen that utilizes type three secretion systems (TTSS) to translocate virulence factors into host cells This causes a wide variety of diseases mainly gastroenteritis and typhoid fever in both humans and animals Salmonella invasive protein D (SipD) is a tip protein attached to the needle protein and interacts with translocon complex

Institut fr Struktur

A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion Research output: SCORING: Contribution to journal › SCORING: Journal articles › Research › peer-review Control of type III protein secretion using a

Recognition of Bacteria by Inflammasomes

2019-7-17Inflammasomes are cytosolic multiprotein complexes that assemble in response to a variety of infectious and noxious insults Inflammasomes play a critical role in the initiation of innate immune responses primarily by serving as platforms for the activation of inflammatory caspase proteases One such caspase CASPASE-1 (CASP1) initiates innate immune responses by cleaving pro-IL-1β and

Type IV Pilin Proteins: Versatile Molecular Modules

Type IV pili (T4P) are multifunctional protein fibers produced on the surfaces of a wide variety of bacteria and archaea The major subunit of T4P is the type IV pilin and structurally related proteins are found as components of the type II secretion (T2S) system where they are called pseudopilins of DNA uptake/competence systems in both Gram-negative and Gram-positive species and of

Investigations of binding mode insight in Salmonella

2017-1-1Salmonella typhi is a Gram-negative pathogen that utilizes type three secretion systems (TTSS) to translocate virulence factors into host cells This causes a wide variety of diseases mainly gastroenteritis and typhoid fever in both humans and animals Salmonella invasive protein D (SipD) is a tip protein attached to the needle protein and interacts with translocon complex

PspA Family Fusion Proteins Delivered by Attenuated

Pneumococcal surface protein A (PspA) is highly immunogenic and can induce a protective immune response against pneumococcal infection PspA is divided into two major families based on serological variability: family 1 and family 2 To provide broad protection PspA proteins from pneumococcal strains Rx1 (family 1) and EF5668 (family 2) were combined to form two PspA fusion proteins PspA/Rx1

310618065

A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion: A protein secreted by the type III secretion system controls needle filament assembly: Salmonella stimulates pro-inflammatory signalling through p21-activated kinases bypassing innate immune receptors: Typhoid toxin 2014:

Towards capture of dynamic assembly and action of

2020-4-1Structures of the Salmonella needle polymer PrgI (SctF) have been determined in isolation [21 • 39] and also from intact NC particles showing an 11-start helical polymer with the N-terminal helix on the outside and the C-terminal helix lining the channel however how this was assembled within the injectisome and especially the role of PrgJ

[PDF] Assembly of the bacterial type III secretion

2020-8-2Many bacteria that live in contact with eukaryotic hosts whether as symbionts or as pathogens have evolved mechanisms that manipulate host cell behaviour to their benefit One such mechanism the type III secretion system is employed by Gram-negative bacterial species to inject effector proteins into host cells This function is reflected by the overall shape of the machinery which

Medscape

HiFocus Helix™ electrode insertion: surgical approach July 15 2015 [ MEDLINE Abstract] Effects of HIV-1 infection on malaria parasitemia in milo sub-location western Kenya July 15 2015 [ MEDLINE Abstract] Fatal non-thrombotic pulmonary embolization in a patient with undiagnosed factitious disorder July 12 2015 [ MEDLINE Abstract]

Institut fr Struktur

A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion Research output: SCORING: Contribution to journal › SCORING: Journal articles › Research › peer-review Control of type III protein secretion using a

Bacterial flagellar motor: Current Biology

There is a homologous structure called the needle structure assembled by the same kind of transport apparatus used by pathogenic species (such as Salmonella) to inject virulence factors into eukaryotic cells Some argue that the flagellar rotary motor evolved from the needle structure but it was probably the other way around since

Structure of a type III secretion needle at 7

Using FTIR of the Salmonella typhimurium needle protein (PrgI*) soluble or polymerized into needles as well as solid state nuclear magnetic resonance (ssNMR) of the latter Poyraz et al provided evidence for a change in secondary structure from α-helix to β-structure within the C

James Tolchard

A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion PLOS Biology July 1 2019 Type III protein-secretion machines are essential for the interactions of many pathogenic or symbiotic bacterial species with their respective eukaryotic hosts

Frontiers

Bacterial pathogens utilize a myriad of mechanisms to invade mammalian hosts damage tissue sites and evade the immune system One essential strategy of Gram-negative bacteria is the secretion of virulence factors through both inner and outer membranes to reach a potential target Most secretion systems are harbored in mobile elements including transposons plasmids pathogenicity islands

NMR characterization of the interaction of the

A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion Guo EZ Desrosiers DC Zalesak J Tolchard J Berbon M Habenstein B Marlovits T Loquet A Galn JE PLoS Biol 17(7):e3000351 01 Jul 2019

PNAS

2011-1-24Ribbon-helix-helix protein copG family DUF1338 PF07063 Protein of unknown function (DUF1338) Herpes_U59 PF04529 Herpesvirus U59 protein IBD PF10416 Transcription-initiator DNA-binding domain IBD DUF2462 PF09495 Protein of unknown function (DUF2462) PCEMA1 PF07418 Acidic phosphoprotein precursor PCEMA1 Mus7 PF09462 Mus7/MMS22 family S_layer_N

A polymorphic helix of a Salmonella needle protein

2019-7-1A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion More specifically these studies reveal an important role for a polymorphic helix of the needle filament protein and the residues that line the lumen of its central channel in the control of type III secretion PMCID: PMC6625726

A polymorphic helix of a Salmonella needle protein relays

2019-7-12RESEARCH ARTICLE A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion Emily Z Guo1☯ Daniel C Desrosiers1☯ Jan Zalesak2 James Tolchard ID 3 Me lanie Berbon 3 Birgit Habenstein ID 3 Thomas Marlovits2 4 5 Antoine Loquet ID Jorge E Gala n ID 1*

310618065

A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion: A protein secreted by the type III secretion system controls needle filament assembly: Salmonella stimulates pro-inflammatory signalling through p21-activated kinases bypassing innate immune receptors: Typhoid toxin 2014:

NMR Characterization of the Interaction of the

2010-4-27A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion PLOS Biology 2019 17 (7) e3000351 DOI: 10 1371/journal pbio 3000351 Wagner Iwan Grin Silke Malmsheimer Nidhi Singh Claudia E Torres-Vargas Sibel Westerhausen

A polymorphic helix of a Salmonella needle protein

A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion More specifically these studies reveal an important role for a polymorphic helix of the needle filament protein and the residues that line the lumen of its central channel in

In Situ Structure of an Intact Lipopolysaccharide

Here in this study we have solved the missing structure of the RsaA NTD bound to the O-antigen of the LPS using single-particle electron cryomicroscopy (cryo-EM) Using native mass spectrometry (MS) we studied the calcium (Ca 2+) dependence and stoichiometry of sugar binding to RsaA allowing us to estimate the length of the native O-antigen and understand the architecture of the cellular LPS