Engineering Tissue Inhibitors of Metalloproteinases Using Yeast Surface Display.
Directed evolution
Enzyme inhibitors
Fluorescent-activated cell sorting
Matrix metalloproteinase
Rational design of proteins
Tissue inhibitor of metalloproteinase
Yeast surface display
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
28
4
2022
pubmed:
29
4
2022
medline:
3
5
2022
Statut:
ppublish
Résumé
Yeast surface display (YSD) has been extensively used for protein design, engineering, and directed evolution in the past two decades. Here, we describe methods for directed evolution of tissue inhibitors of metalloproteinase (TIMP), the natural inhibitors of matrix metalloproteinases (MMPs), through design and generation of a combinatorial library of TIMP mutants and screening the targeted TIMP library of variants toward MMP binding using YSD. This protocol can be adopted to other natural enzyme inhibitors and similar protein binders such as antibodies.
Identifiants
pubmed: 35482200
doi: 10.1007/978-1-0716-2285-8_19
doi:
Substances chimiques
Tissue Inhibitor of Metalloproteinases
0
Matrix Metalloproteinases
EC 3.4.24.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
361-385Subventions
Organisme : NIGMS NIH HHS
ID : P20 GM103650
Pays : United States
Informations de copyright
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Boder ET, Raeeszadeh-Sarmazdeh M, Price JV (2012) Engineering antibodies by yeast display. Arch Biochem Biophys 526(2):99–106. https://doi.org/10.1016/j.abb.2012.03.009
doi: 10.1016/j.abb.2012.03.009
pubmed: 22450168
Boder ET, Wittrup KD (1997) Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol 15(6):553–557. https://doi.org/10.1038/nbt0697-553
doi: 10.1038/nbt0697-553
pubmed: 9181578
Pepper LR, Cho YK, Boder ET, Shusta EV (2008) A decade of yeast surface display technology: where are we now? Comb Chem High Throughput Screen 11(2):127–134. https://doi.org/10.2174/138620708783744516
doi: 10.2174/138620708783744516
pubmed: 18336206
pmcid: 2681324
Cherf GM, Cochran JR (2015) Applications of yeast surface display for protein engineering. Methods Mol Biol 1319:155–175. https://doi.org/10.1007/978-1-4939-2748-7_8
doi: 10.1007/978-1-4939-2748-7_8
pubmed: 26060074
pmcid: 4544684
Boder ET, Wittrup KD (2000) Yeast surface display for directed evolution of protein expression, affinity, and stability. Methods Enzymol 328:430–444. https://doi.org/10.1016/s0076-6879(00)28410-3
doi: 10.1016/s0076-6879(00)28410-3
pubmed: 11075358
Chao G, Lau WL, Hackel BJ, Sazinsky SL, Lippow SM, Wittrup KD (2006) Isolating and engineering human antibodies using yeast surface display. Nat Protoc 1(2):755–768. https://doi.org/10.1038/nprot.2006.94
doi: 10.1038/nprot.2006.94
pubmed: 17406305
Egeblad M, Werb Z (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2(3):161–174. https://doi.org/10.1038/nrc745
doi: 10.1038/nrc745
pubmed: 11990853
Raeeszadeh-Sarmazdeh M, Do LD, Hritz BG (2020) Metalloproteinases and their inhibitors: potential for the development of new therapeutics. Cells 9(5):1313. https://doi.org/10.3390/cells9051313
doi: 10.3390/cells9051313
pmcid: 7290391
Radisky ES, Raeeszadeh-Sarmazdeh M, Radisky DC (2017) Therapeutic potential of matrix metalloproteinase inhibition in breast cancer. J Cell Biochem 118(11):3531–3548. https://doi.org/10.1002/jcb.26185
doi: 10.1002/jcb.26185
pubmed: 28585723
pmcid: 5621753
Raeeszadeh-Sarmazdeh M, Greene KA, Sankaran B, Downey GP, Radisky DC, Radisky ES (2019) Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition. J Biol Chem 294(24):9476–9488. https://doi.org/10.1074/jbc.RA119.008321
doi: 10.1074/jbc.RA119.008321
pubmed: 31040180
pmcid: 6579469
Arkadash V, Yosef G, Shirian J, Cohen I, Horev Y, Grossman M, Sagi I, Radisky ES, Shifman JM, Papo N (2017) Development of high affinity and high specificity inhibitors of matrix metalloproteinase 14 through computational design and directed evolution. J Biol Chem 292(8):3481–3495. https://doi.org/10.1074/jbc.M116.756718
doi: 10.1074/jbc.M116.756718
pubmed: 28087697
pmcid: 5336179
Shirian J, Arkadash V, Cohen I, Sapir T, Radisky ES, Papo N, Shifman JM (2018) Converting a broad matrix metalloproteinase family inhibitor into a specific inhibitor of MMP-9 and MMP-14. FEBS Lett 592(7):1122–1134. https://doi.org/10.1002/1873-3468.13016
doi: 10.1002/1873-3468.13016
pubmed: 29473954
pmcid: 5903968
Yosef G, Arkadash V, Papo N (2018) Targeting the MMP-14/MMP-2/integrin alphavbeta3 axis with multispecific N-TIMP2-based antagonists for cancer therapy. J Biol Chem 293(34):13310–13326. https://doi.org/10.1074/jbc.RA118.004406
doi: 10.1074/jbc.RA118.004406
pubmed: 29986882
pmcid: 6109916
Van Deventer JA, Wittrup KD (2014) Yeast surface display for antibody isolation: library construction, library screening, and affinity maturation. Methods Mol Biol 1131:151–181. https://doi.org/10.1007/978-1-62703-992-5_10
doi: 10.1007/978-1-62703-992-5_10
pubmed: 24515465