Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structures of type IV pili complexed with nanobodies reveal immune escape mechanisms.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 2414, Year 2024
Publish date	Mar 18, 2024
Authors	David Fernandez-Martinez / Youxin Kong / Sylvie Goussard / Agustin Zavala / Pauline Gastineau / Martial Rey / Gabriel Ayme / Julia Chamot-Rooke / Pierre Lafaye / Matthijn Vos / Ariel Mechaly / Guillaume Duménil /
PubMed Abstract	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 (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-expressing Gram-negative bacteria responsible for life threatening sepsis and meningitis. This species has evolved several genetic strategies to modify the surface of its type IV pili, changing pilin subunit amino acid sequence, nature of glycosylation and phosphoforms, but how these modifications affect antibody binding at the structural level is still unknown. Here, to explore this question, we determine cryo-electron microscopy (cryo-EM) structures of pili of different sequence types with sufficiently high resolution to visualize posttranslational modifications. We then generate nanobodies directed against type IV pili which alter pilus function in vitro and in vivo. Cyro-EM in combination with molecular dynamics simulation of the nanobody-pilus complexes reveals how the different types of pili surface modifications alter nanobody binding. Our findings shed light on the impressive complementarity between the different strategies used by bacteria to avoid antibody binding. Importantly, we also show that structural information can be used to make informed modifications in nanobodies as countermeasures to these immune evasion mechanisms.
External links	Nat Commun / PubMed:38499587 / PubMed Central
Methods	EM (helical sym.)
Resolution	2.51 - 3.15 Å
Structure data	17375 8p2v EMDB-17375, PDB-8p2v: Neisseria meningitidis Type IV pilus SB-GATDH variant Method: EM (helical sym.) / Resolution: 2.99 Å 17384 8p36 EMDB-17384, PDB-8p36: Neisseria meningitidis Type IV pilus SB-DATDH variant Method: EM (helical sym.) / Resolution: 2.51 Å 17386 8p3b EMDB-17386, PDB-8p3b: Neisseria meningitidis Type IV pilus SA-GATDH variant Method: EM (helical sym.) / Resolution: 3.15 Å 17683 8pij EMDB-17683, PDB-8pij: Neisseria meningitidis Type IV pilus SB-GATDH variant bound to the C24 nanobody Method: EM (helical sym.) / Resolution: 2.9 Å 17695 8piz EMDB-17695, PDB-8piz: Neisseria meningitidis Type IV pilus SB-DATDH variant bound to the C24 nanobody Method: EM (helical sym.) / Resolution: 2.75 Å 17718 8pjp EMDB-17718, PDB-8pjp: Neisseria meningitidis PilE, SB-GATDH variant, bound to the F10 nanobody Method: EM (helical sym.) / Resolution: 2.92 Å
Chemicals	ChemComp-G3P: SN-GLYCEROL-3-PHOSPHATE ChemComp, No image ChemComp-WKE: Unknown entry ChemComp-B6D: 2,4-bisacetamido-2,4,6-trideoxy-beta-D-glucopyranose
Source	neisseria meningitidis 8013 (bacteria) vicugna pacos (alpaca)
Keywords	PROTEIN FIBRIL / Pilin / Extracellular / Adhesion / Aggregation / Pilus