Proteomic remodeling of outer membrane vesicles in antibiotic-resistant Helicobacter pylori reveals adaptive stress responses
Abstract
Background: Antibiotic resistance in Helicobacter pylori has become a major obstacle to successful eradication therapy worldwide. Although outer membrane vesicles (OMVs) are increasingly recognized as key mediators of bacterial adaptation and host interaction, their contribution to antibiotic resistance in H. pylori remains poorly understood.
Methods: Metronidazole and levofloxacin-resistant derivatives of the H. pylori G27 strain were generated by stepwise antibiotic exposure. OMVs isolated from susceptible and resistant strains were characterized by transmission electron microscopy and dynamic light scattering, followed by comparative LC-MS/MS analysis of whole-cell and OMV proteomes. Functional annotation and enrichment analyses were performed to identify resistance-associated biological processes.
Results: Comparative proteomic analysis revealed remodeling of both cellular and OMV-associated protein profiles following acquisition of antibiotic resistance. While 236 proteins were shared among all strains, distinct resistance-associated protein signatures were identified in the levofloxacin- and metronidazole-resistant derivatives. Functional enrichment highlighted pathways associated with membrane transport, oxidative stress response, metabolic adaptation, and cellular envelope organization. OMV proteomes differed from their corresponding whole-cell proteomes, a pattern consistent with, though not proof of, selective protein packaging. Conserved vesicle-associated…
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