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Surface antigens of Extended-Spectrum Beta-Lactamase (ESBL)-producing Klebsiella pneumoniae represent a diverse group of molecular structures on the bacterial exterior, including capsular polysaccharides (K-antigens), lipopolysaccharides (O-antigens), fimbriae, and outer membrane proteins (OMPs) [1, 2]. These components are essential for the pathogen's virulence, facilitating host cell adhesion, biofilm formation, and evasion of the host immune system through mechanisms like anti-phagocytic capsule production [2, 3]. In ESBL-producing strains, these surface structures often coexist with antibiotic resistance mechanisms, such as modified porins (e.g., OmpK36) that restrict drug entry, complicating treatment [3, 4]. Therapeutic strategies targeting these antigens include monoclonal antibodies designed to promote opsonophagocytosis and vaccines aimed at inducing protective immunity against prevalent serotypes [4, 5]. Additionally, bacteriophage therapies utilize these surface molecules as receptors for viral attachment and subsequent bacterial lysis [6]. Understanding the composition and variability of these antigens is crucial for developing precision medicines against multidrug-resistant Klebsiella infections [1, 3].
Therapeutic agents targeting these antigens work by neutralizing virulence factors, promoting opsonophagocytosis by immune cells, or disrupting the structural integrity of the bacterial outer membrane to facilitate antibiotic entry or direct lysis.
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