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A new class of penicillin-binding protein inhibitors to address drug-resistant Neisseria gonorrhoeae

Uehara, T.; Zulli, A. L.; Miller, B.; Avery, L. M.; Boyd, S. A.; Chatwin, C. L.; Chu, G.-H.; Drager, A. S.; Edwards, M.; Emeigh Hart, S. G.; Myers, C. L.; Rongala, G.; Stevenson, A.; Uehara, K.; Yi, F.; Wang, B.; Liu, Z.; Wang, M.; Zhao, Z.; Zhou, X.; Zhao, H.; Tkavc, R.; Jerse, A. E.; Stratton, C. M.; Bala, S.; Davies, C.; Pevear, D. C.; Burns, C. J.; Daigle, D. M.; Condon, S. M.

2024-12-27 microbiology
10.1101/2024.12.27.630553 bioRxiv
Show abstract

{beta}-Lactams are the most widely used antibiotics for the treatment of bacterial infections because of their proven track record of safety and efficacy. However, susceptibility to {beta}-lactam antibiotics is continually eroded by resistance mechanisms. Emerging multidrug-resistant (MDR) Neisseria gonorrhoeae strains possessing altered penA alleles (encoding PBP2) pose a global health emergency as they threaten the utility of ceftriaxone, the last remaining outpatient antibiotic. Here we disclose a novel benzoxaborinine-based penicillin-binding protein inhibitor series (boro-PBPi) that is envisioned to address penA-mediated resistance while offering protection against evolution and expansion of {beta}-lactamases. Optimization of boro-PBPi led to the identification of compound 21 (VNRX-14079) that exhibits potent antibacterial activity against MDR N. gonorrhoeae achieved by high affinity binding to the PBP2 target. Boro-PBPi/PBP2 complex structures confirmed covalent interaction of the boron atom with Ser310 and the importance of the {beta}3-{beta}4 loop for improved affinity. 21 elicits bactericidal activity, a low frequency of resistance, a good safety profile, suitable pharmacokinetic properties, and in vivo efficacy in a murine infection model against ceftriaxone-resistant N. gonorrhoeae. 21 is a promising anti-gonorrhea agent poised for further advancement.

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