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ProteomicsMounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin
Bacteria have evolved effectors or toxins to outcompete other bacteria or to hijack host cell pathways. One broad family of bacterial polymorphic toxins regroups multidomain proteins with a modular organization, that comprise a C-terminal toxin domain fused to a N-terminal domain that adapt to the d...
ORGANISM(S): Escherichia coli Bacteria 
2021-11-30 | PXD028652 | Pride
Re-arrangement hot spot Spike Cross-linking Polymorphic toxin Β-roll Chaperone Autocleavage Vgrg Architecture 
ProteomicseXL-MS: An enhanced Cross-Linking Mass Spectrometry Workflow to Study Protein Complexes.
The analysis of proteins and protein complexes by cross-linking mass spectrometry (XL-MS) has expanded in the last dec-ade. However, mostly used approaches suffer important limitations in term of efficiency and sensitivity. We describe here a new workflow based on the advanced use of the trifunction...
ORGANISM(S): Oryctolagus cuniculus (Rabbit) 
2021-08-11 | PXD010422 | Pride
Creatine kinase Mass spectrometry Cross-link Monoavidin biotin affinty enrichment Click chemistry 
ProteomicsSalmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop
Rearrangement hot spots (Rhs) proteins are members of the broad family of polymorphic toxins. Polymorphic toxins are modular proteins composed of an N-terminal region that specifies their mode of secretion into the medium or into the target cell, a central delivery module and a C-terminal domain tha...
ORGANISM(S): Homo sapiens (Human) Escherichia coli Bacteria 
2023-03-11 | PXD033100 | Pride
Elongation factor Adpribosylation Toxin Rearrangement hot spots T6ss P-loop Modification Translation 
ProteomicsA simplified in vivo cross-linking mass spectrometry strategy for proteome-wide studies.
Chemical cross-linking (XL) coupled to mass spectrometry (MS) has become a powerful approach to probe the structure of protein assemblies. Although most of the applications concerned purified complexes, latest developments focus on large-scale in vivo studies. Pushing in this direction, we describe ...
ORGANISM(S): Neisseria meningitidis Bacteria 
2021-02-25 | PXD021553 | Pride
Click-chemistry Mass spectrometry Structural biology In vivo biochemistry Cross-linking 
ProteomicsCore–sheath coupling controls flagellar curvature and motility in Leptospira
Spirochete pathogens are among the most invasive bacteria known, causing syphilis, Lyme disease, and leptospirosis. Their tissue penetration depends on periplasmic flagellar filaments that, unlike other bacterial flagella, are encased in a spirochete-specific multi-protein sheath and deform the cell...
ORGANISM(S): Leptospira interrogans serovar Manilae 
2026-07-14 | PXD077813 | Pride
Cryoem Bottom up Flagella Leptospira Lc-ms/ms 
ProteomicsDe novo sequencing of antibody light chain proteoforms from patients with multiple myeloma
In multiple myeloma diseases, monoclonal immunoglobulin light chains (LCs) are abundantly produced, with as a consequence in some cases the formation of deposits affecting various organs, such as kidney, while in other cases to remain soluble up to concentrations of several g.L-1 in plasma. The exac...
ORGANISM(S): Homo sapiens (Human) 
2021-08-11 | PXD025884 | Pride
Proteoforms Top-down proteomics Antibody Bottom-up proteomics De novo sequencing Light chain disease 
ProteomicsCryo-EM structures of type IV pili complexed with nanobodies reveal immune escape mechanisms
Type IV pili (T4P) are prevalent, polymeric surface structures in pathogenic bacteria, making them ideal targets for effective vaccines. However, bacteria have evolved efficient strategies to evade type IV pili-directed antibody responses. Neisseria meningitidis are prototypical type IV pili-expr...
ORGANISM(S): Neisseria meningitidis 
2024-02-29 | PXD046119 | Pride
Pili Neisseria meningitidis 
ProteomicsCore-dependent sheath architecture dictates Leptospira endoflagellar curvature
Spirochete bacteria include some of the most invasive human pathogens, causing diseases such as syphilis, Lyme disease, and leptospirosis that collectively affect millions of people annually. Their unique ability to penetrate tissues and cross biological barriers depends on periplasmic flagellar fil...
ORGANISM(S): Leptospira biflexa 
2026-07-14 | PXD073467 | Pride
Structural biology Xl-ms Leptospira endoflagellum 
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