Agarwal AK, Gude RP, Kalraiya RD (2014) Regulation of melanoma metastasis to lungs by cell surface lysosome associated membrane protein-1 (LAMP1) via galectin-3. Biochem Biophys Res Commun 449(3):332–337. https://doi.org/10.1016/j.bbrc.2014.05.028
Alessandrini F, Pezzè L, Ciribilli Y (2017) LAMPs: shedding light on cancer biology. Semin Oncol 44(4):239–253. https://doi.org/10.1053/j.seminoncol.2017.10.013
Arora A, Ha C, Park CB (2004) Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett 564(1–2):121–125. https://doi.org/10.1016/S0014-5793(04)00326-6
Brinson RG, Marino JP, Delaglio F, Arbogast LW, Evans RM, Kearsley A, Gingras G, Ghasriani H, Aubin Y, Pierens GK, Jia X, Mobli M, Grant HG, Keizer DW, Schweimer K, Ståhle J, Widmalm G, Zartler ER, Lawrence CW et al (2018) Enabling adoption of 2D-NMR for the higher order structure assessment of monoclonal antibody therapeutics. mAbs 11(1):94–105. https://doi.org/10.1080/19420862.2018.1544454
Cameron B, Dabdoubi T, Berthou-Soulié L, Gagnaire M, Arnould I, Severac A, Soubrier F, Morales J, Leighton PA, Harriman W, Ching K, Abdiche Y, Radošević K, Bouquin T (2020) Complementary epitopes and favorable developability of monoclonal anti-LAMP1 antibodies generated using two transgenic animal platforms. PLoS ONE 15(7):e0235815. https://doi.org/10.1371/journal.pone.0235815
Cerofolini L, Ravera E, Fischer C, Trovato A, Sacco F, Palinsky W, Angiuoni G, Fragai M, Baroni F (2023) Integration of NMR spectroscopy in an analytical workflow to evaluate the effects of oxidative stress on abituzumab: beyond the fingerprint of mAbs. Anal Chem 95(24):9199–9206. https://doi.org/10.1021/acs.analchem.3c00317
Clark L, Dikiy I, Rosenbaum DM, Gardner KH (2018) On the use of Pichia pastoris for isotopic labeling of human GPCRs for NMR studies. J Biomol NMR 71(4):203–211. https://doi.org/10.1007/s10858-018-0204-3
de Marco A (2009) Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. Microb Cell Fact 8(1):26. https://doi.org/10.1186/1475-2859-8-26
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277–293. https://doi.org/10.1007/BF00197809
Dopp JL, Reuel NF (2020) Simple, functional, inexpensive cell extract for in vitro prototyping of proteins with disulfide bonds. Biochem Eng J 164:107790. https://doi.org/10.1016/j.bej.2020.107790
Etezady-Esfarjani T, Hiller S, Villalba C, Wüthrich K (2007) Cell-free protein synthesis of perdeuterated proteins for NMR studies. J Biomol NMR 39(3):229–238. https://doi.org/10.1007/s10858-007-9188-0
Favier A, Brutscher B (2019) NMRlib: user-friendly pulse sequence tools for Bruker NMR spectrometers. J Biomol NMR 73(5):199–211. https://doi.org/10.1007/s10858-019-00249-1
Gaciarz A, Veijola J, Uchida Y, Saaranen MJ, Wang C, Hörkkö S, Ruddock LW (2016) Systematic screening of soluble expression ofantibody fragments in the cytoplasm of E. Coli. Microb Cell Fact 15(1):22. https://doi.org/10.1186/s12934-016-0419-5
Gad W, Nair MG, Belle KV, Wahni K, Greve HD, Ginderachter JAV, Vandenbussche G, Endo Y, Artis D, Messens J (2013) The Quiescin Sulfhydryl Oxidase (hQSOX1b) Tunes the Expression of Resistin-Like Molecule Alpha (RELM-α or mFIZZ1) in a Wheat Germ Cell-Free Extract. PLOS ONE 8(1):e55621. https://doi.org/10.1371/journal.pone.0055621
Gagné D, Sarker M, Gingras G, Hodgson DJ, Frahm G, Creskey M, Lorbetskie B, Bigelow S, Wang J, Zhang X, Johnston MJW, Lu H, Aubin Y (2023) Strategies for the production of isotopically labelled Fab fragments of therapeutic antibodies in Komagataella phaffii (Pichia pastoris) and Escherichia coli for NMR studies. PLoS ONE 18:e0294406. https://doi.org/10.1371/journal.pone.0294406
Gardner KH, Kay LE (1998) The Use of 2 h, 13c, 15n multidimensional nmr gto study the structure and dynamics of proteins. Annu Rev BioPhys BioMol Struct 27(1):357–406. https://doi.org/10.1146/annurev.biophys.27.1.357
Garrett DS, Seok Y-J, Liao D-I, Peterkofsky A, Gronenborn AM, Clore GM (1997) Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Biochemistry 36(9):2517–2530. https://doi.org/10.1021/bi962924y
Ghasriani H, Ahmadi S, Hodgson DJ, Aubin Y (2022) Backbone and side-chain resonance assignments of the NISTmAb-scFv and antigen-binding study. Biomol NMR Assignments 16(2):391–398. https://doi.org/10.1007/s12104-022-10109-z
Gupta SK, Shukla P (2017) Microbial platform technology for recombinant antibody fragment production: a review. Crit Rev Microbiol 43(1):31–42. https://doi.org/10.3109/1040841X.2016.1150959
Han B, Liu Y, Ginzinger SW, Wishart DS (2011) SHIFTX2: significantly improved protein chemical shift prediction. J Biomol NMR 50(1):43–57. https://doi.org/10.1007/s10858-011-9478-4
Hsu C-C, Thomas OR, Overton TW (2016) Periplasmic expression in and release of fab fragments from Escherichia coli using stress minimization. J Chem Technol Biotechnol 91(3):815–822. https://doi.org/10.1002/jctb.4672
Ikura M, Kay LE, Bax A (1990) A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. application to calmodulin. Biochemistry 29(19):4659–4667. https://doi.org/10.1021/bi00471a022
Imbert L, Lenoir-Capello R, Crublet E, Vallet A, Awad R, Ayala I, Juillan-Binard C, Mayerhofer H (2021) In vitro production of perdeuterated proteins in H2O for biomolecular NMR studies. In: Chen Y. W., Yiu C.-P. B. (eds) Structural genomics: general applications. Springer, Berlin, pp 127–149. https://doi.org/10.1007/978-1-0716-0892-0_8
Kai L, Dötsch V, Kaldenhoff R, Bernhard F (2013) Artificial environments for the Co-translational stabilization of cell-free expressed proteins. PLoS ONE. https://doi.org/10.1371/journal.pone.0056637
Kaplon H, Crescioli S, Chenoweth A, Visweswaraiah J, Reichert JM (2023) Antibodies to watch in 2023. mAbs 15(1):2153410. https://doi.org/10.1080/19420862.2022.2153410
Katz JJ, Crespi HL (1966) Deuterated organisms: cultivation and uses. Science 151(3715):1187–1194. https://doi.org/10.1126/science.151.3715.1187
Kigawa T (2010) Cell-free protein preparation through prokaryotic transcription–translation methods. In: Endo Y, Takai K, Ueda T (eds) Cell-free protein production: methods and protocols. Humana Press, Totowa, pp 1–10. https://doi.org/10.1007/978-1-60327-331-2_1
Kigawa T, Yabuki T, Matsuda N, Matsuda T, Nakajima R, Tanaka A, Yokoyama S (2004) Preparation of Escherichia coli cell extract for highly productive cell-free protein expression. J Struct Funct Genomics 5(1):63–68. https://doi.org/10.1023/B:JSFG.0000029204.57846.7d
Kim DM, Choi CY (1996) A semicontinuous prokaryotic coupled transcription/translation system using a dialysis membrane. Biotechnol Prog 12(5):645–649. https://doi.org/10.1021/bp960052l
Kunert R, Reinhart D (2016) Advances in recombinant antibody manufacturing. Appl Microbiol Biotechnol 100(8):3451–3461. https://doi.org/10.1007/s00253-016-7388-9
Lescop E, Schanda P, Brutscher B (2007) A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. J Magn Reson 187(1):163–169. https://doi.org/10.1016/j.jmr.2007.04.002
Lobstein J, Emrich CA, Jeans C, Faulkner M, Riggs P, Berkmen M (2012) SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm. Microb Cell Fact 11(1):753. https://doi.org/10.1186/1475-2859-11-56
Marino JP, Brinson RG, Hudgens JW, Ladner JE, Gallagher DT, Gallagher ES, Arbogast LW, Huang RY-C (2015) Emerging technologies to assess the higher order structure of monoclonal antibodies. ACS Symposium Series 1202(2):17–43. https://doi.org/10.1021/bk-2015-1202.ch002
Matsuda T, Watanabe S, Kigawa T (2013) Cell-free synthesis system suitable for disulfide-containing proteins. Biochem Biophys Res Commun 431(2):296–301. https://doi.org/10.1016/j.bbrc.2012.12.107
Matsuda T, Ito T, Takemoto C, Katsura K, Ikeda M, Wakiyama M, Kukimoto-Niino M, Yokoyama S, Kurosawa Y, Shirouzu M (2018) Cell-free synthesis of functional antibody fragments to provide a structural basis for antibody–antigen interaction. PLoS ONE 13(2):e0193158. https://doi.org/10.1371/journal.pone.0193158
Michel E, Wüthrich K (2012) Cell-free expression of disulfide-containing eukaryotic proteins for structural biology: cell-free expression of disulfide-containing proteins. FEBS J 279(17):3176–3184. https://doi.org/10.1111/j.1742-4658.2012.08697.x
Mishra A, Mody RS, Pandey A, Somani S (2018) An improved refolding process for antibody’s fragments (Brevet AU2016307976A1). https://patents.google.com/patent/AU2016307976A1/en
Missiakas D, Georgopoulos C, Raina S (1994) The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J 13(8):2013–2020
Morgan WD, Kragt A, Feeney J (2000) Expression of deuterium-isotope-labelled protein in the yeast Pichia pastoris for NMR studies. J Biomol NMR 17(4):337–347. https://doi.org/10.1023/A:1008313530207
Nakamoto H, Bardwell JCA (2004) Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim Biophys Acta (BBA) - Mol Cell Res 1694(1):111–119. https://doi.org/10.1016/j.bbamcr.2004.02.012
Pratt C (1980) Kinetics and regulation of cell-free alkaline phosphatase synthesis. J Bacteriol 143(3):1265–1274. https://doi.org/10.1128/jb.143.3.1265-1274.1980
Pruvost T, Mathieu M, Dubois S, Maillère B, Vigne E, Nozach H (2023) Deciphering cross-species reactivity of LAMP-1 antibodies using deep mutational epitope mapping and alphafold. mAbs 15(1):2175311. https://doi.org/10.1080/19420862.2023.2175311
Rietsch A, Belin D, Martin N, Beckwith J (1996) An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc Natl Acad Sci USA 93(23):13048–13053. https://doi.org/10.1073/pnas.93.23.13048
Sawasaki T, Hasegawa Y, Tsuchimochi M, Kamura N, Ogasawara T, Kuroita T, Endo Y (2002) A bilayer cell-free protein synthesis system for high-throughput screening of gene products. FEBS Lett 514(1):102–105. https://doi.org/10.1016/S0014-5793(02)02329-3
Schmidt E, Güntert P (2012) A new algorithm for reliable and general NMR resonance assignment. J Am Chem Soc 134(30):12817–12829.
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