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Article

Regulation of Botulinum neurotoxin half‑life through the ubiquitin‑proteasome system

  • Authors:
    • Hae-Seul Choi
    • Hye-Rim Seo
    • Miso Choi
    • Hwa-Yeong Kim
    • Sun-Kyu Jin
    • Myunghoon Lee
    • Kwang-Hyun Baek
  • View Affiliations / Copyright

    Affiliations: Department of Bioconvergence, CHA University, Seongnam, Gyeonggi 13488, Republic of Korea, Alkemier Inc., Seoul 05855, Republic of Korea, Department of Biomedical Science, CHA University, Seongnam, Gyeonggi 13488, Republic of Korea
  • Article Number: 268
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    Published online on: July 23, 2025
       https://doi.org/10.3892/mmr.2025.13633
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Abstract

Botulinum neurotoxin (BoNT), renowned for its potency, is used in both therapeutic and cosmetic applications; however, it is constrained by a relatively short half‑life and limited duration of efficacy. The present study investigated the role of the ubiquitin‑proteasome system in BoNT degradation and evaluated strategies to extend its half‑life by targeting specific lysine residues. Ubiquitination was observed in the light chains of BoNT/A1 (K335 and K417), BoNT/A2 (K335) and BoNT/E (K62 and K288), which were identified as key ubiquitination sites. The substitution of these lysine residues to arginine inhibited ubiquitination, improving protein stability and extending the half‑life of BoNT. These findings offer a potential strategy to enhance the therapeutic efficacy of BoNT by prolonging its stability, paving the way for future advancements in BoNT‑based treatments.
View Figures

Figure 1

Ubiquitination of BoNT/A1, BoNT/A2
and BoNT/E-LCs. (A) BoNT/A1-LC, (B) BoNT/A2-LC and (C) BoNT/E-LC
were analyzed in the presence of the proteasome inhibitor MG132.
Cells were transfected with the indicated BoNT-LC constructs and
HA-tagged ubiquitin, followed by IP using the anti-Flag antibody
and WB with anti-HA to detect ubiquitinated proteins. Enhanced
ubiquitination was observed for all BoNT types under proteasome
inhibition. WB, western blotting; BoNT, Botulinum
neurotoxin; WCL, whole cell lysate; IP, immunoprecipitation; HA,
hemagglutinin; Ub, ubiquitin; LC, light chain.

Figure 2

Ubiquitination levels of WT and
lysine mutant forms of BoNT-LCs. (A) Protein is composed of an LC
(gray) and heavy chain (black and dark gray). The heavy chain is
further divided into HN (black) and HC (C-terminal of heavy chain)
(dark gray) regions. Mutation sites were selected based on
ubiquitin prediction analysis and mutated accordingly. BoNT/A1,
BoNT/A2 and BoNT/E are represented. (B) Ubiquitination levels of WT
and K212R, K301R, K320R, K330R, K335R, K340R and K417R mutants of
BoNT/A1-LC. (C) Ubiquitination levels of WT and the K335R mutant of
BoNT/A2-LC. (D) Ubiquitination levels of WT and K3R, K62R, K85R,
K230R, K281R, K288R, K342R, K413R and K419R mutants of BoNT/E-LC.
Short exposure images were used to avoid signal saturation and
clearly visualize differences in ubiquitination levels between
wild-type and mutant proteins. WT, wild type; BoNT,
Botulinum neurotoxin; LC, light chain; HN, N-terminus of
heavy chain HC; C-terminus of heavy chain; WCL, whole cell lysate;
IP, immunoprecipitation; HA, hemagglutinin; Ub, ubiquitin.

Figure 3

Protein stability of WT and lysine
mutant forms of BoNT-LCs. (A) CHX chase assay comparing protein
stability of BoNT/A1-LC WT and K212R, K301R, K320R, K330R, K335R,
K340R and K417R mutants. Protein levels were analyzed by WB. (B)
CHX chase assay of BoNT/A2-LC WT and K335R mutant. (C) CHX chase
assay of BoNT/E-LC WT, K62R and K288R mutants. WB was carried out
to compare protein expression levels of WT and mutant forms under
identical experimental conditions. Short exposure images were used
to avoid signal saturation and clearly visualize differences in
Flag-BoNT transfected cells. *P<0.05 and **P<0.01. WT, wild
type; BoNT, Botulinum neurotoxin; LC, light chain; CHX,
cycloheximide; WB, western blotting.
View References

1 

Bach K and Simman R: The multispecialty toxin: A literature review of botulinum toxin. Plast Reconstr Surg Glob Open. 10:e42282022. View Article : Google Scholar : PubMed/NCBI

2 

Yeo JC, Tay FP, Bennion R, Loss O, Maignel J, Pons L, Foster K, Beard M and Bard F: Botulinum toxin intoxication requires retrograde transport and membrane translocation at the ER in RenVM neurons. Elife. 12:RP928062024. View Article : Google Scholar : PubMed/NCBI

3 

Joensuu M, Syed P, Saber SH, Lanoue V, Wallis TP, Rae J, Blum A, Gormal RS, Small C, Sanders S, et al: Presynaptic targeting of botulinum neurotoxin type A requires a tripartite PSG-Syt1-SV2 plasma membrane nanocluster for synaptic vesicle entry. EMBO J. 42:e1120952023. View Article : Google Scholar : PubMed/NCBI

4 

Matak I, Bölcskei K, Bach-Rojecky L and Helyes Z: Mechanisms of Botulinum toxin type A action on pain. Toxins (Basel). 11:4592019. View Article : Google Scholar : PubMed/NCBI

5 

Montecucco C, Schiavo G and Rossetto O: The mechanism of action of tetanus and botulinum neurotoxins. Arch Toxicol Suppl. 18:342–354. 1996. View Article : Google Scholar : PubMed/NCBI

6 

Eleopra R, Tugnoli V, Quatrale R, Rossetto O and Montecucco C: Different types of botulinum toxin in humans. Mov Disord. 19 (Suppl 8):S53–S59. 2004. View Article : Google Scholar : PubMed/NCBI

7 

Dressler D and Johnson EA: Botulinum toxin therapy: Past, present and future developments. J Neural Transm (Vienna). 129:829–833. 2022. View Article : Google Scholar : PubMed/NCBI

8 

Pirazzini M, Rossetto O, Eleopra R and Montecucco C: Botulinum neurotoxins: Biology, pharmacology, and toxicology. Pharmacol Rev. 69:200–235. 2017. View Article : Google Scholar : PubMed/NCBI

9 

Wang J, Meng J, Lawrence GW, Zurawski TH, Sasse A, Bodeker MO, Gilmore MA, Fernández-Salas E, Francis J, Steward LE, et al: Novel chimeras of botulinum neurotoxins A and E unveil contributions from the binding, translocation, and protease domains to their functional characteristics. J Biol Chem. 283:16993–17002. 2008. View Article : Google Scholar : PubMed/NCBI

10 

Jackson JL, Kuriyama A and Hayashino Y: Botulinum toxin A for prophylactic treatment of migraine and tension headaches in adults: A meta-analysis. JAMA. 307:1736–1745. 2012. View Article : Google Scholar : PubMed/NCBI

11 

Atraszkiewicz D, Ito R and Bahra A: The efficacy of botulinum toxin type-A for intractable chronic migraine patients with no pain-free time. Br J Pain. 16:41–49. 2022. View Article : Google Scholar : PubMed/NCBI

12 

Lang H, Peng C, Wu K, Chen X, Jiang X, He L and Chen N: Efficacy and safety of onabotulinumtoxinA in the treatment of medication overuse headache: A systematic review. Front Neurol. 15:14531832024. View Article : Google Scholar : PubMed/NCBI

13 

Morra ME, Elgebaly A, Elmaraezy A, Khalil AM, Altibi AM, Vu TL, Mostafa MR, Huy NT and Hirayama K: Therapeutic efficacy and safety of Botulinum toxin A therapy in trigeminal neuralgia: A systematic review and meta-analysis of randomized controlled trials. J Headache Pain. 17:632016. View Article : Google Scholar : PubMed/NCBI

14 

Naumann M, Boo LM, Ackerman AH and Gallagher CJ: Immunogenicity of botulinum toxins. J Neural Transm (Vienna). 120:275–290. 2013. View Article : Google Scholar : PubMed/NCBI

15 

Mejia NI, Vuong KD and Jankovic J: Long-term botulinum toxin efficacy, safety, and immunogenicity. Mov Disord. 20:592–597. 2005. View Article : Google Scholar : PubMed/NCBI

16 

Yu M, Wu J, Shi J and Farokhzad OC: Nanotechnology for protein delivery: Overview and perspectives. J Control Release. 240:24–37. 2016. View Article : Google Scholar : PubMed/NCBI

17 

Strohl WR: Fusion proteins for half-life extension of biologics as a strategy to make biobetters. BioDrugs. 29:215–239. 2015. View Article : Google Scholar : PubMed/NCBI

18 

Kontermann RE: Strategies to extend plasma half-lives of recombinant antibodies. BioDrugs. 23:93–109. 2009. View Article : Google Scholar : PubMed/NCBI

19 

Sokalingam S, Raghunathan G, Soundrarajan N and Lee SG: A study on the effect of surface lysine to arginine mutagenesis on protein stability and structure using green fluorescent protein. PLoS One. 7:e404102012. View Article : Google Scholar : PubMed/NCBI

20 

Austerberry JI, Thistlethwaite A, Fisher K, Golovanov AP, Pluen A, Esfandiary R, van der Walle CF, Warwicker J, Derrick JP and Curtis R: Arginine to lysine mutations increase the aggregation stability of a single-chain variable fragment through unfolded-state interactions. Biochemistry. 58:3413–3421. 2019. View Article : Google Scholar : PubMed/NCBI

21 

Hershko A and Ciechanover A: The ubiquitin system. Annu Rev Biochem. 67:425–479. 1998. View Article : Google Scholar : PubMed/NCBI

22 

Park J, Cho J and Song EJ: Ubiquitin-proteasome system (UPS) as a target for anticancer treatment. Arch Pharm Res. 43:1144–1161. 2020. View Article : Google Scholar : PubMed/NCBI

23 

Kim Y, Kim EK, Chey Y, Song MJ and Jang HH: Targeted protein degradation: Principles and applications of the proteasome. Cells. 12:18462023. View Article : Google Scholar : PubMed/NCBI

24 

Sun M and Zhang X: Current methodologies in protein ubiquitination characterization: From ubiquitinated protein to ubiquitin chain architecture. Cell Biosci. 12:1262022. View Article : Google Scholar : PubMed/NCBI

25 

He M, Zhou Z, Shah AA, Zou H, Tao J, Chen Q and Wan Y: The emerging role of deubiquitinating enzymes in genomic integrity, diseases, and therapeutics. Cell Biosci. 6:622016. View Article : Google Scholar : PubMed/NCBI

26 

Wang J, Zhou Q, Ding J, Yin T, Ye P and Zhang Y: The conceivable functions of protein ubiquitination and deubiquitination in reproduction. Front Physiol. 13:8862612022. View Article : Google Scholar : PubMed/NCBI

27 

Cai B and Jiang X: Computational methods for ubiquitination site prediction using physicochemical properties of protein sequences. BMC Bioinformatics. BMC Bioinformatics. 17:1162016. View Article : Google Scholar : PubMed/NCBI

28 

Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, Tunyasuvunakool K, Bates R, Žídek A, Potapenko A, et al: Highly accurate protein structure prediction with AlphaFold. Nature. 596:583–589. 2021. View Article : Google Scholar : PubMed/NCBI

29 

Serrera-Figallo MA, Ruiz-de-León-Hernández G, Torres-Lagares D, Castro-Araya A, Torres-Ferrerosa O, Hernández-Pacheco E and Gutierrez-Perez JL: Use of botulinum toxin in orofacial clinical practice. Toxins (Basel). 11:1122020. View Article : Google Scholar

30 

Wollmer MA, Magid M, Kruger THC and Finzi E: Treatment of depression with botulinum toxin. Toxins (Basel). 14:3832022. View Article : Google Scholar : PubMed/NCBI

31 

Park J and Park HJ: Botulinum toxin for the treatment of neuropathic pain. Toxins (Basel). 9:2602017. View Article : Google Scholar : PubMed/NCBI

32 

Anandan C and Jankovic J: Botulinum toxin in movement disorders: An update. Toxins (Basel). 13:422021. View Article : Google Scholar : PubMed/NCBI

33 

Cohen JL, Green LJ, Beer KR, Liu Y and Gallagher CJ: Prior botulinum toxin treatment does not impact efficacy or safety in clinical trials: Analysis of daxibotulinumtoxinA for injection in the SAKURA program. Dermatol Surg. 47:511–515. 2021. View Article : Google Scholar : PubMed/NCBI

34 

Ascher B, Rzany B, Kestemont P, Hilton S, Heckmann M, Bodokh I, Noah EM, Boineau D, Kerscher M, Volteau M, et al: Liquid formulation of abobotulinumtoxinA: A 6-month, phase 3, double-blind, randomized, placebo-controlled study of a single treatment, ready-to-use toxin for moderate-to-severe glabellar lines. Aesthet Surg J. 40:93–104. 2020. View Article : Google Scholar : PubMed/NCBI

35 

Nestor MS, Arnold D and Fischer DL: The mechanisms of action and use of botulinum neurotoxin type A in aesthetics: Key clinical postulates II. J Cosmet Dermatol. 11:2785–2804. 2020. View Article : Google Scholar : PubMed/NCBI

36 

Yoelin SG, Dhawan SS, Vitarella D, Ahmad W, Hasan F and Abushakra S: Safety and efficacy of EB-001, a novel type E botulinum toxin, in subjects with glabellar frown lines: Results of a phase 2, randomized, placebo-controlled, ascending-dose study. Plast Reconstr Surg. 142:847e–855e. 2018. View Article : Google Scholar : PubMed/NCBI

37 

Swaminathan S and Eswaramoorthy S: Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat Struct Biol. 7:693–699. 2000. View Article : Google Scholar : PubMed/NCBI

38 

Tsai YC, Maditz R, Kuo CL, Fishman PS, Shoemaker CB, Oyler GA and Weissman AM: Targeting botulinum neurotoxin persistence by the ubiquitin-proteasome system. Proc Natl Acad Sci USA. 107:16554–16559. 2010. View Article : Google Scholar : PubMed/NCBI

39 

Sen E, Kota KP, Panchal RG, Bavari S and Kiris E: Screening of a focused ubiquitin-proteasome pathway inhibitor library identifies small molecules as novel modulators of Botulinum neurotoxin type A toxicity. Front Pharmacol. 12:7639502021. View Article : Google Scholar : PubMed/NCBI

40 

Shoemaker CB and Oyler GA: Persistence of Botulinum neurotoxin inactivation of nerve function. Curr Top Microbiol Immunol. 364:179–196. 2013.PubMed/NCBI

41 

Kapuria V, Peterson LF, Fang D, Bornmann WG, Talpaz M and Donato NJ: Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis. Cancer Res. 70:9265–9276. 2010. View Article : Google Scholar : PubMed/NCBI

42 

Larbret F, Biber P, Dubois N, Ivanov S, Lafanechere L, Tartare-Deckert S and Deckert M: Deubiquitinase inhibitors impair leukemic cell migration through cofilin oxidation and alteration of actin reorganization. Front Pharmacol. 12:7782162022. View Article : Google Scholar : PubMed/NCBI

43 

Breidenbach MA and Brunger AT: Substrate recognition strategy for botulinum neurotoxin serotype A. Nature. 432:925–929. 2004. View Article : Google Scholar : PubMed/NCBI

44 

Gardner AP, Barbieri JT and Pellett S: How Botulinum neurotoxin light chain A1 maintains stable association with the intracellular neuronal plasma membrane. Toxins (Basel). 14:8142022. View Article : Google Scholar : PubMed/NCBI

45 

Lacy DB, Tepp W, Cohen AC, DasGupta BR and Stevens RC: Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nat Struct Biol. 5:898–902. 1998. View Article : Google Scholar : PubMed/NCBI

46 

Kumaran D, Rawat R, Ahmed SA and Swaminathan S: Substrate binding mode and its implication on drug design for botulinum neurotoxin A. PLoS Pathog. 4:e10001652008. View Article : Google Scholar : PubMed/NCBI

47 

Atassi MZ and Oshima M: Structure, activity, and immune (T and B cell) recognition of botulinum neurotoxins. Crit Rev Immunol. 19:219–260. 1999.PubMed/NCBI

48 

Cai F, Adrion CB and Keller JE: Comparison of extracellular and intracellular potency of Botulinum neurotoxins. Infect Immun. 74:5617–5624. 2006. View Article : Google Scholar : PubMed/NCBI

49 

Gao Y, Joshi M, Zhao Z and Mitragotri S: PEGylated therapeutics in the clinic. Bioeng Transl Med. 9:e106002023. View Article : Google Scholar : PubMed/NCBI

50 

Sleep D: Albumin and its application in drug delivery. Expert Opin Drug Deliv. 12:793–812. 2015. View Article : Google Scholar : PubMed/NCBI

51 

Kim A, Oh MS, Lee GH, Song S, Byun MS, Choi D, Yu BY and Lee H: Understanding the pharmacokinetic journey of Fc-fusion protein, rhIL-7-hyFc using complementary approach of two analytical methods, accelerator mass spectrometry and ELISA. Antib Ther. 7:105–113. 2024.PubMed/NCBI

52 

Finley D: Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem. 78:477–513. 2009. View Article : Google Scholar : PubMed/NCBI

53 

Mizushima N and Levine B: Autophagy in human diseases. N Engl J Med. 383:1564–1576. 2020. View Article : Google Scholar : PubMed/NCBI

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Copy and paste a formatted citation
Spandidos Publications style
Choi H, Seo H, Choi M, Kim H, Jin S, Lee M and Baek K: Regulation of <em>Botulinum</em> neurotoxin half‑life through the ubiquitin‑proteasome system. Mol Med Rep 32: 268, 2025.
APA
Choi, H., Seo, H., Choi, M., Kim, H., Jin, S., Lee, M., & Baek, K. (2025). Regulation of <em>Botulinum</em> neurotoxin half‑life through the ubiquitin‑proteasome system. Molecular Medicine Reports, 32, 268. https://doi.org/10.3892/mmr.2025.13633
MLA
Choi, H., Seo, H., Choi, M., Kim, H., Jin, S., Lee, M., Baek, K."Regulation of <em>Botulinum</em> neurotoxin half‑life through the ubiquitin‑proteasome system". Molecular Medicine Reports 32.4 (2025): 268.
Chicago
Choi, H., Seo, H., Choi, M., Kim, H., Jin, S., Lee, M., Baek, K."Regulation of <em>Botulinum</em> neurotoxin half‑life through the ubiquitin‑proteasome system". Molecular Medicine Reports 32, no. 4 (2025): 268. https://doi.org/10.3892/mmr.2025.13633
Copy and paste a formatted citation
x
Spandidos Publications style
Choi H, Seo H, Choi M, Kim H, Jin S, Lee M and Baek K: Regulation of <em>Botulinum</em> neurotoxin half‑life through the ubiquitin‑proteasome system. Mol Med Rep 32: 268, 2025.
APA
Choi, H., Seo, H., Choi, M., Kim, H., Jin, S., Lee, M., & Baek, K. (2025). Regulation of <em>Botulinum</em> neurotoxin half‑life through the ubiquitin‑proteasome system. Molecular Medicine Reports, 32, 268. https://doi.org/10.3892/mmr.2025.13633
MLA
Choi, H., Seo, H., Choi, M., Kim, H., Jin, S., Lee, M., Baek, K."Regulation of <em>Botulinum</em> neurotoxin half‑life through the ubiquitin‑proteasome system". Molecular Medicine Reports 32.4 (2025): 268.
Chicago
Choi, H., Seo, H., Choi, M., Kim, H., Jin, S., Lee, M., Baek, K."Regulation of <em>Botulinum</em> neurotoxin half‑life through the ubiquitin‑proteasome system". Molecular Medicine Reports 32, no. 4 (2025): 268. https://doi.org/10.3892/mmr.2025.13633
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