ArticleFrontiers in cellular and infection microbiology2025
Enhancing the structural stability of P29-targeted monoclonal antibodies via β-hydroxybutyrylation modification improves their therapeutic performance in alveolar echinococcosis.
Article in Frontiers in cellular and infection microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background: Alveolar echinococcosis (AE), a severe parasitic infection often likened to "parasitic cancer", still lacks effective treatments. Although our earlier ork on the P29 monoclonal antibody (P29 mAb) against the parasite-derived P29 antigen showed potential, its efficacy remained limited, prompting the need for improved biologic agents. Methods: We applied β-hydroxybutyrylation (Kbhb) modification to engineer an enhanced antibody, P29 mAb Results: The modified antibody retained high antigen-binding affinity (KD = 343 pM) and exhibited markedly increased resistance to proteolytic degradation, with a 1.75-fold improvement in serum persistence after 5 weeks. Furthermore, in a murine model of AE, P29 mAb Conclusion: Our results establish a novel connection between protein engineering and antiparasitic therapy, illustrating that Kbhb modification not only augments the efficacy of anti-AE antibodies but also offers a versatile strategy for enhancing antibody stability and half-life. This offers a potential strategy for developing new treatments against neglected zoonotic diseases via tailored post-translational modifications.
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