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TitleMechanistic basis of choline import involved in teichoic acids and lipopolysaccharide modification.
Journal, issue, pagesSci Adv, Vol. 8, Issue 9, Page eabm1122, Year 2022
Publish dateMar 4, 2022
AuthorsNatalie Bärland / Anne-Stéphanie Rueff / Gonzalo Cebrero / Cedric A J Hutter / Markus A Seeger / Jan-Willem Veening / Camilo Perez /
PubMed AbstractPhosphocholine molecules decorating bacterial cell wall teichoic acids and outer-membrane lipopolysaccharide have fundamental roles in adhesion to host cells, immune evasion, and persistence. ...Phosphocholine molecules decorating bacterial cell wall teichoic acids and outer-membrane lipopolysaccharide have fundamental roles in adhesion to host cells, immune evasion, and persistence. Bacteria carrying the operon that performs phosphocholine decoration synthesize phosphocholine after uptake of the choline precursor by LicB, a conserved transporter among divergent species. is a prominent pathogen where phosphocholine decoration plays a fundamental role in virulence. Here, we present cryo-electron microscopy and crystal structures of LicB, revealing distinct conformational states and describing architectural and mechanistic elements essential to choline import. Together with in vitro and in vivo functional characterization, we found that LicB displays proton-coupled import activity and promiscuous selectivity involved in adaptation to choline deprivation conditions, and describe LicB inhibition by synthetic nanobodies (sybodies). Our results provide previously unknown insights into the molecular mechanism of a key transporter involved in bacterial pathogenesis and establish a basis for inhibition of the phosphocholine modification pathway across bacterial phyla.
External linksSci Adv / PubMed:35235350 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.75 - 3.8 Å
Structure data

13268

7paf

EMDB-13268, PDB-7paf:
Streptococcus pneumoniae choline importer LicB in lipid nanodiscs
Method: EM (single particle) / Resolution: 3.75 Å

PDB-7b0k:
membrane protein structure
Method: X-RAY DIFFRACTION / Resolution: 3.8 Å

Chemicals

ChemComp-CHT:
CHOLINE ION

ChemComp-PGT:
(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipid*YM

Source
  • streptococcus pneumoniae tigr4 (bacteria)
  • synthetic construct (others)
  • streptococcus pneumoniae (bacteria)
KeywordsTRANSPORT PROTEIN / choline transporter / Importer / Choline / nanodisc / Nanobody

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