Interaction of lipopolysaccharides at intermolecular sites of the periplasmic Lpt transport assembly - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Scientific Reports Année : 2017

Interaction of lipopolysaccharides at intermolecular sites of the periplasmic Lpt transport assembly

Résumé

Transport of lipopolysaccharides (LPS) to the surface of the outer membrane is essential for viability of Gram-negative bacteria. Periplasmic LptC and LptA proteins of the LPS transport system (Lpt) are responsible for LPS transfer between the Lpt inner and outer membrane complexes. Here, using a monomeric E. coli LptA mutant, we first show in vivo that a stable LptA oligomeric form is not strictly essential for bacteria. The LptC-LptA complex was characterized by a combination of SAXS and NMR methods and a low resolution model of the complex was determined. We were then able to observe interaction of LPS with LptC, the monomeric LptA mutant as well as with the LptC-LptA complex. A LptC-LPS complex was built based on NMR data in which the lipid moiety of the LPS is buried at the interface of the two β-jellyrolls of the LptC dimer. The selectivity of LPS for this intermolecular surface and the observation of such cavities at homo- or heteromolecular interfaces in LptC and LptA suggests that intermolecular sites are essential for binding LPS during its transport.

Dates et versions

hal-01593515 , version 1 (26-09-2017)

Identifiants

Citer

Cédric Laguri, Paola Sperandeo, Kevin Pounot, Isabel Ayala, Alba Silipo, et al.. Interaction of lipopolysaccharides at intermolecular sites of the periplasmic Lpt transport assembly. Scientific Reports, 2017, 7 (1), pp.9715. ⟨10.1038/s41598-017-10136-0⟩. ⟨hal-01593515⟩
130 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More