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ORIGINAL RESEARCH article

Front. Microbiol.
Sec. Infectious Agents and Disease
Volume 15 - 2024 | doi: 10.3389/fmicb.2024.1512451

Structural and functional analysis of the Helicobacter pylori lipoprotein chaperone LolA

Provisionally accepted
Karina Persson Karina Persson 1,2,3*Deepika Jaiman Deepika Jaiman 1,2,3
  • 1 Centre for Microbial Research, Faculty of Medicine, Umeå University, Umeå, Västerbotten, Sweden
  • 2 Department of Chemistry, Faculty of Science and Technology, Umeå University, Umeå, Västerbotten, Sweden
  • 3 Umeå University, Umeå, Sweden

The final, formatted version of the article will be published soon.

    Lipoproteins are crucial for maintaining the structural integrity of bacterial membranes. In Gramnegative bacteria the Lol (localization of lipoproteins) system facilitates the transport of these proteins from the inner membrane to the outer membrane. In Helicobacter pylori, an ε-proteobacterium, lipoprotein transport differs significantly from the canonical and well-studied system in Escherichia coli, particularly due to the absence of LolB and the use of a LolF homodimer instead of the LolCE heterodimer. This study presents the crystal structure of the H. pylori lipoprotein chaperone LolA (LolA-HP) and its interaction with lipopeptide antibiotics like polymyxin B and colistin. Isothermal titration calorimetry revealed that, unlike LolA from Vibrio cholerae and Porphyromonas gingivalis, LolA-HP does not bind to these antibiotics. Structural comparisons showed that LolA-HP has a deeper hydrophobic cleft but lacks the negative electrostatic potential critical for binding polymyxins. These findings offer insights into the structural diversity of LolA across bacterial species and its potential as a target for antibacterial agents.

    Keywords: lipoprotein transport, lola, polymyxin, ITC, crystal structure, ε-Proteobacteria

    Received: 16 Oct 2024; Accepted: 25 Nov 2024.

    Copyright: © 2024 Persson and Jaiman. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Karina Persson, Centre for Microbial Research, Faculty of Medicine, Umeå University, Umeå, 901 87, Västerbotten, Sweden

    Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.