Enterobacteriaceae, Gram-negative bacilli found mainly in the intestinal flora of mammals, include species that represent a major cause of death from bacterial infection. These bacteria are surrounded by an envelope containing lipopolysaccharide that protects them from detergents and antibiotics.
The team of Raffaele Ieva (LMGM) together with collaborators from the LMGM (Yves Quentin), the IPBS (Julien Marcoux), and at the University of Warwick in UK (Robin Corey and Phillip Stansfeld), have identified a new component (called LptM) of the molecular machine that assembles lipopolysaccharide in the bacterial envelope. The researches have shown that LptM primes the machinery of lipopolysaccharide assembly by mimicking the binding of its natural substrate.
This study reveals a potential “Achilles heel” to exploit for the screening of new antimicrobial therapies.
Figure : Close-up view of the lipopolysaccharide transport site in the LptD structure: biochemical assays and structural prediction show that lipoprotein LptM occupies the lipopolysaccharide transport site with its lipid tails.
© Robin Corey and Raffaele Ieva
More information :
LptM promotes oxidative maturation of the lipopolysaccharide translocon by substrate binding mimicry. Authors : Yiying Yang, Haoxiang Chen, Robin A. Corey, Violette Morales, Yves Quentin, Carine Froment, Anne Caumont-Sarcos, Cécile Albenne, Odile Burlet-Schiltz, David Ranava, Phillip J. Stansfeld, Julien Marcoux, Raffaele Ieva. Nature Communications 2023 Oct 11; 14(1):6368. doi: 10.1038/s41467-023-42007-w. PMID: 37821449
CNRS-Biologie: https://www.insb.cnrs.fr/fr/cnrsinfo/decouverte-dun-nouveau-composant-dans-la-construction-de-lenveloppe-des-enterobacteries-un
Contact : Raffaele Ieva