Site-Specific Antibody Labeling Using Phosphopantetheinyl Transferase-Catalyzed Ligation.
4′-Phosphopantetheinyl transferase
Antibody–drug conjugates
Bioorthogonal chemistry
Enzymatic ligation
Enzymatic modification
Protein tags
Site-specific conjugation
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:
2019
2019
Historique:
entrez:
5
6
2019
pubmed:
5
6
2019
medline:
19
3
2020
Statut:
ppublish
Résumé
4'-Phosphopantetheinyl transferases (PPTases) have been employed by researchers as versatile biocatalysts for the site-specific modification of numerous protein targets with structurally diverse molecules. Here we describe the use of these enzymes for the production of homogeneous antibody-drug conjugates (ADCs), which have garnered much attention as innovative anticancer drugs. The exceptionally broad substrate tolerance of PPTases allows for one-step and two-step conjugation strategies for site-specific ADC synthesis. While one-step conjugation involves direct coupling of a drug molecule to an antibody, two-step conjugation provides increased flexibility and efficiency of the conjugation process by first attaching a bioorthogonal chemical handle that is then used for drug molecule attachment in a second step. The aim of this chapter is to outline detailed protocols for both labeling procedures, as well as to provide guidance on enzyme and substrate preparation.
Identifiants
pubmed: 31161512
doi: 10.1007/978-1-4939-9546-2_13
doi:
Substances chimiques
Antibodies
0
Antineoplastic Agents
0
Bacterial Proteins
0
Immunoconjugates
0
Recombinant Proteins
0
phosphopantetheinyl transferase
0
Transferases (Other Substituted Phosphate Groups)
EC 2.7.8.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
237-278Références
Prescher JA, Bertozzi CR (2005) Chemistry in living systems. Nat Chem Biol 1(1):13–21
doi: 10.1038/nchembio0605-13
Hinner MJ, Johnsson K (2010) How to obtain labeled proteins and what to do with them. Curr Opin Biotechnol 21(6):766–776
doi: 10.1016/j.copbio.2010.09.011
Foley TL, Burkart MD (2007) Site-specific protein modification: advances and applications. Curr Opin Chem Biol 11(1):12–19
doi: 10.1016/j.cbpa.2006.11.036
Lotze J, Reinhardt U, Seitz O, Beck-Sickinger AG (2016) Peptide-tags for site-specific protein labelling in vitro and in vivo. Mol Biosyst 12(6):1731–1745
doi: 10.1039/C6MB00023A
Pakhomov AA, Martynov VI (2008) GFP family: structural insights into spectral tuning. Chem Biol 15(8):755–764
doi: 10.1016/j.chembiol.2008.07.009
Tsien RY (1998) The green fluorescent protein. Annu Rev Biochem 67:509–544
doi: 10.1146/annurev.biochem.67.1.509
Zhang G, Gurtu V, Kain SR (1996) An enhanced green fluorescent protein allows sensitive detection of gene transfer in mammalian cells. Biochem Biophys Res Commun 227(3):707–711
doi: 10.1006/bbrc.1996.1573
Los GV et al (2008) HaloTag: a novel protein labeling technology for cell imaging and protein analysis. ACS Chem Biol 3(6):373–382
doi: 10.1021/cb800025k
Sun X et al (2011) Development of SNAP-tag fluorogenic probes for wash-free fluorescence imaging. Chembiochem 12(14):2217–2226
doi: 10.1002/cbic.201100173
Gautier A et al (2008) An engineered protein tag for multiprotein labeling in living cells. Chem Biol 15(2):128–136
doi: 10.1016/j.chembiol.2008.01.007
Liu CC, Schultz PG (2010) Adding new chemistries to the genetic code. Annu Rev Biochem 79:413–444
doi: 10.1146/annurev.biochem.052308.105824
Junutula JR et al (2008) Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index. Nat Biotechnol 26(8):925–932
doi: 10.1038/nbt.1480
Shen BQ et al (2012) Conjugation site modulates the in vivo stability and therapeutic activity of antibody-drug conjugates. Nat Biotechnol 30(2):184–189
doi: 10.1038/nbt.2108
Griffin BA, Adams SR, Tsien RY (1998) Specific covalent labeling of recombinant protein molecules inside live cells. Science 281(5374):269–272
doi: 10.1126/science.281.5374.269
Halo TL, Appelbaum J, Hobert EM, Balkin DM, Schepartz A (2009) Selective recognition of protein tetraserine motifs with a cell-permeable, pro-fluorescent bis-boronic acid. J Am Chem Soc 131(2):438–439
doi: 10.1021/ja807872s
Goldsmith CR, Jaworski J, Sheng M, Lippard SJ (2006) Selective labeling of extracellular proteins containing polyhistidine sequences by a fluorescein-nitrilotriacetic acid conjugate. J Am Chem Soc 128(2):418–419
doi: 10.1021/ja0559754
Ojida A et al (2006) Oligo-Asp tag/Zn(II) complex probe as a new pair for labeling and fluorescence imaging of proteins. J Am Chem Soc 128(32):10452–10459
doi: 10.1021/ja0618604
Franz KJ, Nitz M, Imperiali B (2003) Lanthanide-binding tags as versatile protein coexpression probes. Chembiochem 4(4):265–271
doi: 10.1002/cbic.200390046
Sletten EM, Bertozzi CR (2009) Bioorthogonal chemistry: fishing for selectivity in a sea of functionality. Angew Chem 48(38):6974–6998
doi: 10.1002/anie.200900942
Rashidian M, Dozier JK, Distefano MD (2013) Enzymatic labeling of proteins: techniques and approaches. Bioconjug Chem 24(8):1277–1294
doi: 10.1021/bc400102w
Sunbul M, Yin J (2009) Site specific protein labeling by enzymatic posttranslational modification. Org Biomol Chem 7(17):3361–3371
doi: 10.1039/b908687k
Vivero-Pol L, George N, Krumm H, Johnsson K, Johnsson N (2005) Multicolor imaging of cell surface proteins. J Am Chem Soc 127(37):12770–12771
doi: 10.1021/ja0533850
Ishitsuka Y et al (2015) Evaluation of genetically encoded chemical tags as orthogonal fluorophore labeling tools for single-molecule FRET applications. J Phys Chem B 119(22):6611–6619
doi: 10.1021/acs.jpcb.5b03584
Lin CW, Ting AY (2006) Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells. J Am Chem Soc 128(14):4542–4543
doi: 10.1021/ja0604111
Fernandez-Suarez M et al (2007) Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes. Nat Biotechnol 25(12):1483–1487
doi: 10.1038/nbt1355
Mao H, Hart SA, Schink A, Pollok BA (2004) Sortase-mediated protein ligation: a new method for protein engineering. J Am Chem Soc 126(9):2670–2671
doi: 10.1021/ja039915e
La Clair JJ, Foley TL, Schegg TR, Regan CM, Burkart MD (2004) Manipulation of carrier proteins in antibiotic biosynthesis. Chem Biol 11(2):195–201
doi: 10.1016/j.chembiol.2004.02.010
Yin J, Liu F, Li X, Walsh CT (2004) Labeling proteins with small molecules by site-specific posttranslational modification. J Am Chem Soc 126(25):7754–7755
doi: 10.1021/ja047749k
George N, Pick H, Vogel H, Johnsson N, Johnsson K (2004) Specific labeling of cell surface proteins with chemically diverse compounds. J Am Chem Soc 126(29):8896–8897
doi: 10.1021/ja048396s
Reuter K, Mofid MR, Marahiel MA, Ficner R (1999) Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4′-phosphopantetheinyl transferase superfamily. EMBO J 18(23):6823–6831
doi: 10.1093/emboj/18.23.6823
Lambalot RH et al (1996) A new enzyme superfamily – the phosphopantetheinyl transferases. Chem Biol 3(11):923–936
doi: 10.1016/S1074-5521(96)90181-7
Zhou Z et al (2007) Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases. ACS Chem Biol 2(5):337–346
doi: 10.1021/cb700054k
Yin J et al (2005) Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase. Proc Natl Acad Sci U S A 102(44):15815–15820
doi: 10.1073/pnas.0507705102
Ou W et al (2011) Site-specific protein modifications through pyrroline-carboxy-lysine residues. Proc Natl Acad Sci U S A 108(26):10437–10442
doi: 10.1073/pnas.1105197108
Grunewald J et al (2014) Site-specific dual labeling of proteins by using small orthogonal tags at neutral pH. Chembiochem 15(12):1787–1791
doi: 10.1002/cbic.201402204
Zhou Z, Koglin A, Wang Y, McMahon AP, Walsh CT (2008) An eight residue fragment of an acyl carrier protein suffices for post-translational introduction of fluorescent pantetheinyl arms in protein modification in vitro and in vivo. J Am Chem Soc 130(30):9925–9930
doi: 10.1021/ja802657n
De Nadai T et al (2016) Precursor and mature NGF live tracking: one versus many at a time in the axons. Sci Rep 6:20272
doi: 10.1038/srep20272
Pippig DA, Baumann F, Strackharn M, Aschenbrenner D, Gaub HE (2014) Protein-DNA chimeras for nano assembly. ACS Nano 8(7):6551–6555
doi: 10.1021/nn501644w
Wilmes S et al (2015) Receptor dimerization dynamics as a regulatory valve for plasticity of type I interferon signaling. J Cell Biol 209(4):579–593
doi: 10.1083/jcb.201412049
Marchetti L et al (2014) Site-specific labeling of neurotrophins and their receptors via short and versatile peptide tags. PLoS One 9(11):e113708
doi: 10.1371/journal.pone.0113708
Waichman S et al (2010) Functional immobilization and patterning of proteins by an enzymatic transfer reaction. Anal Chem 82(4):1478–1485
doi: 10.1021/ac902608a
Grunewald J et al (2015) Efficient preparation of site-specific antibody-drug conjugates using phosphopantetheinyl transferases. Bioconjug Chem 26(12):2554–2562
doi: 10.1021/acs.bioconjchem.5b00558
Sieber SA, Walsh CT, Marahiel MA (2003) Loading peptidyl-coenzyme A onto peptidyl carrier proteins: a novel approach in characterizing macrocyclization by thioesterase domains. J Am Chem Soc 125(36):10862–10866
doi: 10.1021/ja0361852
Grunewald J et al (2017) Optimization of an enzymatic antibody-drug conjugation approach based on coenzyme A analogs. Bioconjug Chem 28(7):1906–1915
doi: 10.1021/acs.bioconjchem.7b00236
Meier JL, Mercer AC, Rivera H Jr, Burkart MD (2006) Synthesis and evaluation of bioorthogonal pantetheine analogues for in vivo protein modification. J Am Chem Soc 128(37):12174–12184
doi: 10.1021/ja063217n
Carter P et al (1992) Humanization of an anti-p185HER2 antibody for human cancer therapy. Proc Natl Acad Sci U S A 89(10):4285–4289
doi: 10.1073/pnas.89.10.4285
Strop P et al (2013) Location matters: site of conjugation modulates stability and pharmacokinetics of antibody drug conjugates. Chem Biol 20(2):161–167
doi: 10.1016/j.chembiol.2013.01.010
Rashidian M et al (2013) A highly efficient catalyst for oxime ligation and hydrazone-oxime exchange suitable for bioconjugation. Bioconjug Chem 24(3):333–342
doi: 10.1021/bc3004167