Elizabethkingia species are emerging opportunistic pathogens responsible for life-threatening nosocomial infections. Their intrinsic multidrug resistance severely limits effective antibiotic treatment, necessitating urgent development of novel therapeutic strategies. Among potential targets, outer membrane protein A (OmpA) family proteins have drawn increasing interest. However, the functional roles of OmpA family proteins in Elizabethkingia remain entirely uncharacterized, leaving their potential as targeted therapeutics unresolved. In this study, we identified a group of putative OmpA family proteins in Elizabethkingia miricola strain FL160902 and systematically investigated the contributions of five OmpA members to bacterial physiology and virulence. Targeted gene deletions revealed marked functional divergence among these paralogs. Specifically, OmpA-1 and OmpA-3 were identified as master virulence determinants; their deletion resulted in impaired serum resistance, reduced cell adhesion capacity, and diminished in vivo lethality. Their deletion also induced extensive physiological dysregulation, including enhanced biofilm formation, increased surface hydrophobicity, and heightened susceptibility to oxidative stress. In contrast, deletions of ompA-2, ompA-4, and ompA-5 resulted only in partial attenuation of virulence traits and restricted changes to specific physiological phenotypes. Collectively, these findings establish a functional hierarchy within the OmpA proteins and position OmpA-1 and OmpA-3 as high-priority molecular targets for developing precision therapeutics against this life-threatening, multidrug-resistant pathogen.
Liu et al. (Sat,) studied this question.
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