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Snoopligase-catalyzed molecular glue enables efficient generation of hyperoligomerized TRAIL variant with enhanced antitumor effect.

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Title: Snoopligase-catalyzed molecular glue enables efficient generation of hyperoligomerized TRAIL variant with enhanced antitumor effect.
Authors: She, Tianshan1 (AUTHOR), Yang, Fen1 (AUTHOR), Chen, Shiyuan1 (AUTHOR), Yang, Hao1,2,3 (AUTHOR), Tao, Ze1,2,3 (AUTHOR), Xing, Huimin1 (AUTHOR), Chen, Jie1 (AUTHOR), Chang, Huansheng1 (AUTHOR), Lu, Hongyu1 (AUTHOR), Su, Tao3 (AUTHOR), Jin, Youmei3 (AUTHOR), Zhong, Yi3 (AUTHOR), Cheng, Jingqiu1,2,3 (AUTHOR), Zhu, Hong1,4 (AUTHOR) zhuhong938@wchscu.cn, Lu, Xiaofeng1,2,3 (AUTHOR) xiaofenglu@scu.edu.cn
Source: Journal of Controlled Release. Sep2023, Vol. 361, p856-870. 15p.
Subjects: TRAIL protein, Escherichia coli, Liposomes, Peptides, Glue, Clinical medicine
Abstract: Clinical application of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is predominantly limited by its inefficient apoptosis induction in tumor cells, which might be improved by using molecular superglue-mediated hyperoligomerization to increase its valency. Here, the minimal superglue peptide pairs, including Snoopligase-catalyzed SnoopTagJr/SnoopDogTag and SpyStapler-catalyzed SpyTag/SpyBDTag, were individually fused at the N- or C-terminus of the TRAIL promoter to produce superglue-fusion TRAIL variants. Similar to native trivalent TRAIL, these superglue-fusion TRAIL variants were highly expressed in Escherichia coli (E. coli) and spontaneously trimerized. In the presence of Snoopligase or SpyStapler, the trivalent superglue-fusion TRAIL variants were predominantly crosslinked into hexavalent TRAIL variants. Nevertheless, Snoopligase was more efficient than SpyStapler in the production of hexavalent TRAIL variants. In particular, Snoopligase-catalyzed trivalent TRAIL variants with N-terminal fusion of SnoopTagJr/SnoopDogTag produced hexavalent SnHexaTR with the highest yield (∼70%). The in vitro cytotoxicity of SnHexaTR was 10–40 times greater than that of TRAIL in several tumor cells. In addition, compared to trivalent TRAIL, hexavalent SnHexaTR showed a longer serum half-life and greater tumor uptake, which resulted in eradication of 50% of tumor xenografts of TRAIL-sensitive COLO 205. In mice bearing TRAIL-resistant HT-29 tumor xenografts, hexavalent SnHexaTR combined with bortezomib encapsulated in liposomes also showed robust tumor growth suppression, indicating that hyperoligomerization mediated by minimal molecular superglue significantly increased the cytotoxicity and antitumor effect of TRAIL. As a novel anticancer agent candidate, the hexavalent SnHexaTR has great potential for clinical application in cancer therapy. [Display omitted] • TRAIL variants with superglue fusion are highly expressed in E. coli. • Trivalent TRAIL were predominantly crosslinked into hexavalent TRAIL by both Snoopligase and SpyStapler. • Snoopligase is more effective than SpyStapler in hexavalent TRAIL crosslinking. • Hexavalent TRAIL exerts better pharmacokinetics and greater antitumor effect than trivalent TRAIL. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Controlled Release is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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Header DbId: egs
DbLabel: Engineering Source
An: 171829904
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
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  Label: Title
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  Data: Snoopligase-catalyzed molecular glue enables efficient generation of hyperoligomerized TRAIL variant with enhanced antitumor effect.
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  Data: <searchLink fieldCode="AR" term="%22She%2C+Tianshan%22">She, Tianshan</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Yang%2C+Fen%22">Yang, Fen</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Chen%2C+Shiyuan%22">Chen, Shiyuan</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Yang%2C+Hao%22">Yang, Hao</searchLink><relatesTo>1,2,3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Tao%2C+Ze%22">Tao, Ze</searchLink><relatesTo>1,2,3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Xing%2C+Huimin%22">Xing, Huimin</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Chen%2C+Jie%22">Chen, Jie</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Chang%2C+Huansheng%22">Chang, Huansheng</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lu%2C+Hongyu%22">Lu, Hongyu</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Su%2C+Tao%22">Su, Tao</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Jin%2C+Youmei%22">Jin, Youmei</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zhong%2C+Yi%22">Zhong, Yi</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Cheng%2C+Jingqiu%22">Cheng, Jingqiu</searchLink><relatesTo>1,2,3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zhu%2C+Hong%22">Zhu, Hong</searchLink><relatesTo>1,4</relatesTo> (AUTHOR)<i> zhuhong938@wchscu.cn</i><br /><searchLink fieldCode="AR" term="%22Lu%2C+Xiaofeng%22">Lu, Xiaofeng</searchLink><relatesTo>1,2,3</relatesTo> (AUTHOR)<i> xiaofenglu@scu.edu.cn</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Controlled+Release%22">Journal of Controlled Release</searchLink>. Sep2023, Vol. 361, p856-870. 15p.
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  Data: <searchLink fieldCode="DE" term="%22TRAIL+protein%22">TRAIL protein</searchLink><br /><searchLink fieldCode="DE" term="%22Escherichia+coli%22">Escherichia coli</searchLink><br /><searchLink fieldCode="DE" term="%22Liposomes%22">Liposomes</searchLink><br /><searchLink fieldCode="DE" term="%22Peptides%22">Peptides</searchLink><br /><searchLink fieldCode="DE" term="%22Glue%22">Glue</searchLink><br /><searchLink fieldCode="DE" term="%22Clinical+medicine%22">Clinical medicine</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Clinical application of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is predominantly limited by its inefficient apoptosis induction in tumor cells, which might be improved by using molecular superglue-mediated hyperoligomerization to increase its valency. Here, the minimal superglue peptide pairs, including Snoopligase-catalyzed SnoopTagJr/SnoopDogTag and SpyStapler-catalyzed SpyTag/SpyBDTag, were individually fused at the N- or C-terminus of the TRAIL promoter to produce superglue-fusion TRAIL variants. Similar to native trivalent TRAIL, these superglue-fusion TRAIL variants were highly expressed in Escherichia coli (E. coli) and spontaneously trimerized. In the presence of Snoopligase or SpyStapler, the trivalent superglue-fusion TRAIL variants were predominantly crosslinked into hexavalent TRAIL variants. Nevertheless, Snoopligase was more efficient than SpyStapler in the production of hexavalent TRAIL variants. In particular, Snoopligase-catalyzed trivalent TRAIL variants with N-terminal fusion of SnoopTagJr/SnoopDogTag produced hexavalent SnHexaTR with the highest yield (∼70%). The in vitro cytotoxicity of SnHexaTR was 10–40 times greater than that of TRAIL in several tumor cells. In addition, compared to trivalent TRAIL, hexavalent SnHexaTR showed a longer serum half-life and greater tumor uptake, which resulted in eradication of 50% of tumor xenografts of TRAIL-sensitive COLO 205. In mice bearing TRAIL-resistant HT-29 tumor xenografts, hexavalent SnHexaTR combined with bortezomib encapsulated in liposomes also showed robust tumor growth suppression, indicating that hyperoligomerization mediated by minimal molecular superglue significantly increased the cytotoxicity and antitumor effect of TRAIL. As a novel anticancer agent candidate, the hexavalent SnHexaTR has great potential for clinical application in cancer therapy. [Display omitted] • TRAIL variants with superglue fusion are highly expressed in E. coli. • Trivalent TRAIL were predominantly crosslinked into hexavalent TRAIL by both Snoopligase and SpyStapler. • Snoopligase is more effective than SpyStapler in hexavalent TRAIL crosslinking. • Hexavalent TRAIL exerts better pharmacokinetics and greater antitumor effect than trivalent TRAIL. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Controlled Release is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.jconrel.2023.07.042
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 15
        StartPage: 856
    Subjects:
      – SubjectFull: TRAIL protein
        Type: general
      – SubjectFull: Escherichia coli
        Type: general
      – SubjectFull: Liposomes
        Type: general
      – SubjectFull: Peptides
        Type: general
      – SubjectFull: Glue
        Type: general
      – SubjectFull: Clinical medicine
        Type: general
    Titles:
      – TitleFull: Snoopligase-catalyzed molecular glue enables efficient generation of hyperoligomerized TRAIL variant with enhanced antitumor effect.
        Type: main
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          Dates:
            – D: 01
              M: 09
              Text: Sep2023
              Type: published
              Y: 2023
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              Value: 361
          Titles:
            – TitleFull: Journal of Controlled Release
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