Reengineering of an Artificial Protein Cage for Efficient Packaging of Active Enzymes.
enzymes
host‐guest systems
nanotechnology
protein engineering
synthetic biology
Journal
Small (Weinheim an der Bergstrasse, Germany)
ISSN: 1613-6829
Titre abrégé: Small
Pays: Germany
ID NLM: 101235338
Informations de publication
Date de publication:
13 May 2024
13 May 2024
Historique:
revised:
01
04
2024
received:
05
01
2024
medline:
13
5
2024
pubmed:
13
5
2024
entrez:
13
5
2024
Statut:
aheadofprint
Résumé
Protein cages that readily encapsulate active enzymes of interest present useful nanotools for delivery and catalysis, wherein those with programmable disassembly characteristics serve as particularly attractive platforms. Here, a general guest packaging system based on an artificial protein cage, TRAP-cage, the disassembly of which can be induced by the addition of reducing agents, is established. In this system, TRAP-cage with SpyCatcher moieties in the lumen is prepared using genetic modification of the protein building block and assembled into a cage structure with either monovalent gold ions or molecular crosslinkers. The resulting protein cage can efficiently capture guest proteins equipped with a SpyTag by simply mixing them in an aqueous solution. This post-assembly loading system, which circumvents the exposure of guests to thiol-reactive crosslinkers, enables the packaging of enzymes possessing a catalytic cysteine or a metal cofactor while retaining their catalytic activity.
Identifiants
pubmed: 38738740
doi: 10.1002/smll.202312286
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2312286Subventions
Organisme : Narodowe Centrum Nauki
ID : 2016/20/W/NZ1/00095
Organisme : Narodowe Centrum Nauki
ID : 2019/34/A/NZ1/00196
Organisme : Narodowe Centrum Nauki
ID : 2021/41/N/NZ1/02635
Organisme : The open-access publication of this article was funded by the Priority Research Area BioS under the program 'Initiative of Excellence - Research University' at the Jagiellonian University in Krakow.
Informations de copyright
© 2024 The Authors. Small published by Wiley‐VCH GmbH.
Références
a) W.‐S. Ryu, in Molecular Virology of Human Pathogenic Viruses (Ed.: W.‐S. Ryu), Academic Press, Boston, 2017, pp. 227–246;
b) J. R. Mesters, J. Tan, R. Hilgenfeld, Curr. Opin. Struct. Biol. 2006, 16, 776.
a) T. O. Yeates, C. A. Kerfeld, S. Heinhorst, G. C. Cannon, J. M. Shively, Nat. Rev. Microbiol. 2008, 6, 681;
b) C. A. Kerfeld, C. Aussignargues, J. Zarzycki, F. Cai, M. Sutter, Nat. Rev. Microbiol. 2018, 16, 277;
c) R. Ladenstein, M. Fischer, A. Bacher, FEBS J. 2013, 280, 2537.
a) Y. Wang, T. Douglas, Curr. Opin. Colloid Interface Sci. 2021, 51, 101395;
b) Y. Wang, T. Douglas, J. Mater. Chem. B 2023, 11, 3567.
a) T. G. W. Edwardson, M. D. Levasseur, S. Tetter, A. Steinauer, M. Hori, D. Hilvert, Chem. Rev. 2022, 122, 9145;
b) W. M. Aumiller, M. Uchida, T. Douglas, Chem. Soc. Rev. 2018, 47, 3433.
a) C. H. Abrahamson, B. J. Palmero, N. W. Kennedy, D. Tullman‐Ercek, Annu. Rev. Biophys. 2023, 52, 553;
b) D. P. Patterson, P. E. Prevelige, T. Douglas, ACS Nano 2012, 6, 5000;
c) I. J. Minten, V. I. Claessen, K. Blank, A. E. Rowan, R. J. M. Nolte, J. J. L. M. Cornelissen, Chem. Sci. 2011, 2, 358;
d) Y. Azuma, R. Zschoche, M. Tinzl, D. Hilvert, Angew. Chem. 2016, 128, 1555.
a) J. E. Padilla, C. Colovos, T. O. Yeates, Proc. Natl. Acad. Sci. U. S. A. 2001, 98, 2217;
b) Y.‐T. Lai, D. Cascio, T. O. Yeates, Science 2012, 336, 1129;
c) N. P. King, J. B. Bale, W. Sheffler, D. E. McNamara, S. Gonen, T. Gonen, T. O. Yeates, D. Baker, Nature 2014, 510, 103;
d) J. B. Bale, S. Gonen, Y. Liu, W. Sheffler, D. Ellis, C. Thomas, D. Cascio, T. O. Yeates, T. Gonen, N. P. King, D. Baker, Science 2016, 353, 389;
e) D. J. E. Huard, K. M. Kane, F. A. Tezcan, Nat. Chem. Biol. 2013, 9, 169;
f) E. Golub, R. H. Subramanian, J. Esselborn, R. G. Alberstein, J. B. Bailey, J. A. Chiong, X. Yan, T. Booth, T. S. Baker, F. A. Tezcan, Nature 2020, 578, 172;
g) I. Stupka, J. G. Heddle, Curr. Opin. Struct. Biol. 2020, 64, 66;
h) K. Majsterkiewicz, Y. Azuma, J. G. Heddle, Nanoscale Adv. 2020, 2, 2255;
i) J. Aupič, F. Lapenta, Z. Strmšek, E. Merljak, T. Plaper, R. Jerala, Sci. Adv. 2022, 8, eabm8243;
j) A. Sciore, M. Su, P. Koldewey, J. D. Eschweiler, K. A. Diffley, B. M. Linhares, B. T. Ruotolo, J. C. A. Bardwell, G. Skiniotis, E. N. G. Marsh, Proc. Natl. Acad. Sci. USA 2016, 113, 8681;
k) A. S. Cristie‐David, J. Chen, D. B. Nowak, A. L. Bondy, K. Sun, S. I. Park, M. M. Banaszak Holl, M. Su, E. N. G. Marsh, J. Am. Chem. Soc. 2019, 141, 9207.
A. A. Antson, J. Otridge, A. M. Brzozowski, E. J. Dodson, G. G. Dodson, K. S. Wilson, T. M. Smith, M. Yang, T. Kurecki, P. Gollnick, Nature 1995, 374, 693.
a) A. D. Malay, N. Miyazaki, A. Biela, S. Chakraborti, K. Majsterkiewicz, I. Stupka, C. S. Kaplan, A. Kowalczyk, B. M. A. G. Piette, G. K. A. Hochberg, D. Wu, T. P. Wrobel, A. Fineberg, M. S. Kushwah, M. Kelemen, P. Vavpetič, P. Pelicon, P. Kukura, J. L. P. Benesch, K. Iwasaki, J. G. Heddle, Nature 2019, 569, 438;
b) M. Imamura, T. Uchihashi, T. Ando, A. Leifert, U. Simon, A. D. Malay, J. G. Heddle, Nano Lett. 2015, 15, 1331;
c) A. D. Malay, J. G. Heddle, S. Tomita, K. Iwasaki, N. Miyazaki, K. Sumitomo, H. Yanagi, I. Yamashita, Y. Uraoka, Nano Lett. 2012, 12, 2056.
A. Naskalska, K. Borzęcka‐Solarz, J. Różycki, I. Stupka, M. Bochenek, E. Pyza, J. G. Heddle, Biomacromolecules 2021, 22, 4146.
I. Stupka, Y. Azuma, A. P. Biela, M. Imamura, S. Scheuring, E. Pyza, O. Woźnicka, D. P. Maskell, J. G. Heddle, Sci. Adv. 2022, 8, eabj9424.
N. H. Hopcroft, A. Manfredo, A. L. Wendt, A. M. Brzozowski, P. Gollnick, A. A. Antson, J. Mol. Biol. 2004, 338, 43.
Y. Azuma, M. Herger, D. Hilvert, J. Am. Chem. Soc. 2018, 140, 558.
B. Zakeri, J. O. Fierer, E. Celik, E. C. Chittock, U. Schwarz‐Linek, V. T. Moy, M. Howarth, Proc. Natl. Acad. Sci. USA 2012, 109, E690.
a) J.‐D. Pédelacq, S. Cabantous, T. Tran, T. C. Terwilliger, G. S. Waldo, Nat. Biotechnol. 2006, 24, 79;
b) D. A. Zacharias, J. D. Violin, A. C. Newton, R. Y. Tsien, Science 2002, 296, 913.
L. Li, J. O. Fierer, T. A. Rapoport, M. Howarth, J. Mol. Biol. 2014, 426, 309.
a) C. E. Correnti, M. M. Gewe, C. Mehlin, A. D. Bandaranayake, W. A. Johnsen, P. B. Rupert, M.‐Y. Brusniak, M. Clarke, S. E. Burke, W. De Van Der Schueren, K. Pilat, S. M. Turnbaugh, D. May, A. Watson, M. K. Chan, C. D. Bahl, J. M. Olson, R. K. Strong, Nat. Struct. Mol. Biol. 2018, 25, 270;
b) L. D. Cabrita, D. Gilis, A. L. Robertson, Y. Dehouck, M. Rooman, S. P. Bottomley, Protein Sci. 2007, 16, 2360;
c) R. B. Kapust, J. Tözsér, J. D. Fox, D. E. Anderson, S. Cherry, T. D. Copeland, D. S. Waugh, Protein Eng. Des. Sel. 2001, 14, 993.
Y. Azuma, D. L. V. Bader, D. Hilvert, J. Am. Chem. Soc. 2018, 140, 860.
Q. Wu, H. L. Ploegh, M. C. Truttmann, ACS Chem. Biol. 2017, 12, 664.
B. Sjöblom, M. Polentarutti, K. Djinović‐Carugo, Proc. Natl. Acad. Sci. USA 2009, 106, 10609.
S. Qazi, H. M. Miettinen, R. A. Wilkinson, K. McCoy, T. Douglas, B. Wiedenheft, Mol. Pharmaceutics 2016, 13, 1191.
G. S. Salvesen, V. M. Dixit, Cell 1997, 91, 443.
a) G. Barnea, W. Strapps, G. Herrada, Y. Berman, J. Ong, B. Kloss, R. Axel, K. J. Lee, Proc. Natl. Acad. Sci. USA 2008, 105, 64;
b) H. K. Chung, M. Z. Lin, Nat. Methods 2020, 17, 885.