التفاصيل البيبلوغرافية
| العنوان: |
Structural and functional analysis of the Helicobacter pylori lipoprotein chaperone LolA. |
| المؤلفون: |
Jaiman, Deepika, Persson, Karina |
| المصدر: |
Frontiers in Microbiology; 2025, p1-8, 8p |
| مصطلحات موضوعية: |
LIPOPEPTIDE antibiotics, ISOTHERMAL titration calorimetry, VIBRIO cholerae, ANTIBACTERIAL agents, BACTERIAL cell walls, HELICOBACTER pylori |
| مستخلص: |
Lipoproteins are crucial for maintaining the structural integrity of bacterial membranes. In Gram-negative bacteria, the localization of lipoprotein (Lol) 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 such as 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. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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