Abstract
Antibodies are useful biomolecules applied in many biomedical applications. The selectivity and specificity of antibodies against the target antigens have gained wide interest for both diagnostic and therapeutic applications. The antibodies are capable of functioning as target-specific carriers to allow site-specific delivery of payloads. However, the challenge has always revolved around the ability to attach designer proteins, enzymes, or drugs to the antibody molecule. The conventional approach involves the use of chemical-based modifications with the introduction of chemical linkers and alteration of chemical functional groups to initiate a covalent attachment of molecules to the antibodies. However, the use of chemically modified strategies to attach antibodies to various molecules has provided several setbacks throughout the years. The major consideration involves the conjugation efficiency, the yield of conjugated product recovered post-conjugation, and more importantly the effects to the antibody-binding sites. Therefore, the introduction of bioconjugation approaches utilizing biologically active enzymes to initiate conjugation processes provided researchers with a much-anticipated alternative that was less toxic to the native proteins. This chapter focuses on the application of biologically inspired enzymes that have been used successfully to conjugate proteins or drugs to antibodies in a “green” manner. The enzymes highlighted in this chapter would include sortase, transglutaminase, and formylglycine-generating enzymes. The chapter also highlights the applications of these methods to generate conjugates that have been applied either for diagnostic or therapeutic application.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Acchione M, Kwon H, Jochheim CM et al (2012) Impact of linker and conjugation chemistry on antigen binding, Fc receptor binding and thermal stability of model antibody-drug conjugates. MAbs 4:362–372
Agarwal P, Bertozzi CR (2015) Site-specific antibody–drug conjugates: the nexus of bioorthogonal chemistry, protein engineering, and drug development. Bioconjug Chem 26:176–192
Akkapeddi P, Azizi S-A, Freedy AM et al (2016) Construction of homogeneous antibody–drug conjugates using site-selective protein chemistry. Chem Sci 7:2954–2963
Alberts B, Johnson A, Lewis J et al (2002) The adaptive immune system. Garland Science, New York
Ando H, Adachi M, Umeda K et al (1989) Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric Biol Chem 53:2613–2617
Appel MJ, Bertozzi CR (2014) Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications. ACS Chem Biol 10:72–84
Autuori F, Farrace MG, Oliverio S et al (1998) “Tissue” transglutaminase and apoptosis. Adv Biochem Eng Biotechnol 62:129–136
Badescu G, Bryant P, Bird M et al (2014) Bridging disulfides for stable and defined antibody drug conjugates. Bioconjug Chem 25:1124–1136
Bailon P, Won C-Y (2009) PEG-modified biopharmaceuticals. Expert Opin Drug Deliv 6:1–16
Basle E, Joubert N, Pucheault M (2010) Protein chemical modification on endogenous amino acids. Chem Biol 17:213–227
Beerli RR, Hell T, Merkel AS et al (2015) Sortase enzyme-mediated generation of site-specifically conjugated antibody drug conjugates with high in vitro and in vivo potency. PLoS One 10:e0131177
Behrens CR, Liu B (2014) Methods for site-specific drug conjugation to antibodies. MAbs 6:46–53
Boylan NJ, Zhou W, Proos RJ et al (2013) Conjugation site heterogeneity causes variable electrostatic properties in Fc conjugates. Bioconjug Chem 24:1008–1016
Brotzel F, Mayr H (2007) Nucleophilicities of amino acids and peptides. Org Biomol Chem 5:3814–3820
Brun M-P, Gauzy-Lazo L (2013) Protocols for lysine conjugation. In: L D (ed) Antibody-drug conjugates. Methods in molecular biology (Methods and protocols). Humana Press, Totowa, pp 173–187
Cal PM, Bernardes GJ, Gois PM (2014) Cysteine-selective reactions for antibody conjugation. Angew Chem Int Ed 53:10585–10587
Caminschi I, Lahoud MH, Shortman K (2009) Enhancing immune responses by targeting antigen to DC. Eur J Immunol 39:931–938
Carlson BL, Ballister ER, Skordalakes E et al (2008) Function and structure of a prokaryotic formylglycine-generating enzyme. J Biol Chem 283:20117–20125
Carrico IS, Carlson BL, Bertozzi CR (2007) Introducing genetically encoded aldehydes into proteins. Nat Chem Biol 3:321–322
Cascioferro S, Totsika M, Schillaci D (2014) Sortase A: an ideal target for anti-virulence drug development. Microb Pathog 77:105–112
Chalker JM, Bernardes GJ, Lin YA et al (2009) Chemical modification of proteins at cysteine: opportunities in chemistry and biology. Chem Asian J 4:630–640
Chapman AP (2002) PEGylated antibodies and antibody fragments for improved therapy: a review. Adv Drug Deliv Rev 54:531–545
Chen JS, Mehta K (1999) Tissue transglutaminase: an enzyme with a split personality. Int J Biochem Cell Biol 31:817–836
Chen I, Dorr BM, Liu DR (2011) A general strategy for the evolution of bond-forming enzymes using yeast display. Proc Natl Acad Sci 108:11399–11404
Chen L, Cohen J, Song X et al (2016) Improved variants of Srt A for site-specific conjugation on antibodies and proteins with high efficiency. Sci Rep 6:31899
Chih HW, Gikanga B, Yang Y et al (2011) Identification of amino acid residues responsible for the release of free drug from an antibody–drug conjugate utilizing lysine–succinimidyl ester chemistry. J Pharm Sci 100:2518–2525
Cohen JD, Zou P, Ting AY (2012) Site-specific protein modification using lipoic acid ligase and bis-aryl hydrazone formation. ChemBioChem 13:888–894
Comfort D, Clubb RT (2004) A comparative genome analysis identifies distinct sorting pathways in gram-positive bacteria. Infect Immun 72:2710–2722
Coquerel Y, Boddaert T, Presset M et al (2010) Ideas in chemistry and molecular sciences: advances in synthetic chemistry. Wiley, Weinheim
Coussons P, Price N, Kelly S et al (1992) Factors that govern the specificity of transglutaminase-catalyzed modification of proteins and peptides. Biochem J 282:929–930
Cowan AJ, Laszlo GS, Estey EH et al (2013) Antibody-based therapy of acute myeloid leukemia with gemtuzumab ozogamicin. Front Biosci (Landmark Edition) 18:1311
Crankshaw MW, Grant GA (2001) Modification of cysteine. Curr Protoc Protein Sci 3:15.1.1–15.1.18
Dale JW (2012) Understanding microbes: an introduction to a small world. Wiley, New York
Del Duca S, Verderio E, Serafini-Fracassini D et al (2014) The plant extracellular transglutaminase: what mammal analogues tell. Amino Acids 46:777–792
Dennler P, Chiotellis A, Fischer E et al (2014) Transglutaminase-based chemo-enzymatic conjugation approach yields homogeneous antibody–drug conjugates. Bioconjug Chem 25:569–578
Dennler P, Fischer E, Schibli R (2015) Antibody conjugates: from heterogeneous populations to defined reagents. Antibodies 4:197–224
Dierks T, Schmidt B, Von Figura K (1997) Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Proc Natl Acad Sci 94:11963–11968
Dimitrov DS (2010) Therapeutic antibodies, vaccines and antibodyomes. MAbs 2:347–356
Dorywalska M, Strop P, Melton-Witt JA et al (2015) Site-dependent degradation of a non-cleavable auristatin-based linker-payload in rodent plasma and its effect on ADC efficacy. PLoS One 10:e0132282
Dozier JK, Khatwani SL, Wollack JW et al (2014) Engineering protein farnesyltransferase for enzymatic protein labeling applications. Bioconjug Chem 25:1203–1212
Drake PM, Albers AE, Baker J et al (2014) Aldehyde tag coupled with HIPS chemistry enables the production of ADCs conjugated site-specifically to different antibody regions with distinct in vivo efficacy and PK outcomes. Bioconjug Chem 25:1331–1341
Dramsi S, Trieu-Cuot P, Bierne H (2005) Sorting sortases: a nomenclature proposal for the various sortases of gram-positive bacteria. Res Microbiol 156:289–297
Duarte JN, Cragnolini JJ, Swee LK, Bilate AM, Bader J, Ingram JR, Rashidfarrokhi A, Fang T, Schiepers A, Hanke L (2016) Generation of Immunity against Pathogens via Single-Domain Antibody–Antigen Constructs. J Immunol 197(12): 4838–4847
Farias SE, Strop P, Delaria K et al (2014) Mass spectrometric characterization of transglutaminase based site-specific antibody–drug conjugates. Bioconjug Chem 25:240–250
Fierer JO, Veggiani G, Howarth M (2014) SpyLigase peptide–peptide ligation polymerizes affibodies to enhance magnetic cancer cell capture. Proc Natl Acad Sci 111:E1176–E1181
Folk J, Cole P (1966) Mechanism of action of Guinea pig liver transglutaminase I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity. J Biol Chem 241:5518–5525
Frenzel A, Schirrmann T, Hust M (2016) Phage display-derived human antibodies in clinical development and therapy. MAbs 8:1177–1194
Garandeau C, Réglier-Poupet H, Dubail I et al (2002) The sortase SrtA of Listeria monocytogenes is involved in processing of internalin and in virulence. Infect Immun 70:1382–1390
Gong H, Holcomb I, Ooi A et al (2016) Simple method to prepare oligonucleotide-conjugated antibodies and its application in multiplex protein detection in single cells. Bioconjug Chem 27:217–225
Griffin M, Casadio R, Bergamini CM (2002) Transglutaminases: nature’s biological glues. Biochem J 368:377–396
Grünewald J, Klock HE, Cellitti SE et al (2015) Efficient preparation of site-specific antibody–drug conjugates using phosphopantetheinyl transferases. Bioconjug Chem 26:2554–2562
Gundersen MT, Keillor JW, Pelletier JN (2014) Microbial transglutaminase displays broad acyl-acceptor substrate specificity. Appl Microbiol Biotechnol 98:219–230
Hagemeyer CE, Alt K, Johnston AP et al (2015) Particle generation, functionalization and sortase A–mediated modification with targeting of single-chain antibodies for diagnostic and therapeutic use. Nat Protoc 10:90–105
Hamann PR, Hinman LM, Hollander I et al (2002) Gemtuzumab ozogamicin, a potent and selective anti-CD33 antibody− calicheamicin conjugate for treatment of acute myeloid leukemia. Bioconjug Chem 13:47–58
Hofer T, Skeffington LR, Chapman CM et al (2009) Molecularly defined antibody conjugation through a selenocysteine interface. Biochemistry 48:12047–12057
Hull EA, Livanos M, Miranda E et al (2014) Homogeneous bispecifics by disulfide bridging. Bioconjug Chem 25:1395–1401
Ikura K, Sasaki R, Motoki M (1992) Use of transglutaminase in quality-improvement and processing of food proteins. Comments. Agric Food Chem 2:389–407
Ismail NF, Lim TS (2016) Site-specific scFv labelling with invertase via Sortase A mechanism as a platform for antibody-antigen detection using the personal glucose meter. Sci Rep 6:19338
Jackson DY (2016) Processes for constructing homogeneous antibody drug conjugates. Org Process Res Dev 20:852–866
Jazayeri MH, Amani H, Pourfatollah AA et al (2016) Various methods of gold nanoparticles (GNPs) conjugation to antibodies. Sens Biosensing Res 9:17–22
Jeger S, Zimmermann K, Blanc A et al (2010) Site-specific and stoichiometric modification of antibodies by bacterial transglutaminase. Angew Chem Int Ed 49:9995–9997
Jevševar S, Kusterle M, Kenig M (2012) PEGylation of antibody fragments for half-life extension. In: Antibody methods and protocols. Springer, New York, pp 233–246
Johansson L, Gafvelin G, Arnér ES (2005) Selenocysteine in proteins—properties and biotechnological use. Biochim Biophys Acta 1726:1–13
Johnston MV, Adams HP, Fatemi A (2016) Neurobiology of disease. Oxford University Press, Oxford/New York
Jones MW, Strickland RA, Schumacher FF et al (2012) Polymeric dibromomaleimides as extremely efficient disulfide bridging bioconjugation and pegylation agents. J Am Chem Soc 134:1847–1852
Josten A, Haalck L, Spener F et al (2000) Use of microbial transglutaminase for the enzymatic biotinylation of antibodies. J Immunol Methods 240:47–54
Junutula JR, Raab H, Clark S et al (2008) Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index. Nat Biotechnol 26:925–932
Kamiya N, Mori Y (2015) Substrate engineering of microbial transglutaminase for site-specific protein modification and bioconjugation. In: Hitomi K, Kojima S, Fesus L (eds) Transglutaminases. Springer, Tokyo, pp 373–383
Kamiya N, Takazawa T, Tanaka T et al (2003) Site-specific cross-linking of functional proteins by transglutamination. Enzym Microb Technol 33:492–496
Kieliszek M, Misiewicz A (2014) Microbial transglutaminase and its application in the food industry. A review. Folia Microbiol (Praha) 59:241–250
Kim HJ, Ha S, Lee HY et al (2015) ROSics: chemistry and proteomics of cysteine modifications in redox biology. Mass Spectrom Rev 34:184–208
Kline T, Steiner AR, Penta K et al (2015) Methods to make homogenous antibody drug conjugates. Pharm Res 32:3480–3493
Köhler G, Milstein C (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256:495–497
Koniev O, Wagner A (2015) Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation. Chem Soc Rev 44:5495–5551
Kornberger P, Skerra A (2014) Sortase-catalyzed in vitro functionalization of a HER2-specific recombinant Fab for tumor targeting of the plant cytotoxin gelonin. MAbs 6:354–366
Landgrebe J, Dierks T, Schmidt B et al (2003) The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro-to eukaryotes. Gene 316:47–56
Lee JH, Song C, Kim DH et al (2013) Glutamine (Q)-peptide screening for transglutaminase reaction using mRNA display. Biotechnol Bioeng 110:353–362
Levary DA, Parthasarathy R, Boder ET et al (2011) Protein-protein fusion catalyzed by sortase A. PLoS One 6:e18342
Li X, Yang J, Rader C (2014) Antibody conjugation via one and two C-terminal selenocysteines. Methods 65:133–138
Li W, Prabakaran P, Chen W et al (2016) Antibody aggregation: insights from sequence and structure. Antibodies 5:19
Lin C-W, 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 128:4542–4543
Lorand L, Graham RM (2003) Transglutaminases: crosslinking enzymes with pleiotropic functions. Mol Cell Biol 4:140–156
Luciano FB, Arntfield S (2012) Use of transglutaminases in foods and potential utilization of plants as a transglutaminase source–review. Biotemas 25:1–11
Mariathasan S, Tan M-W (2017) Antibody–antibiotic conjugates: a novel therapeutic platform against bacterial infections. Trends Mol Med 23:135–149
Mazmanian SK, Liu G, Ton-That H et al (1999) Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285:760–763
McAuley A, Jacob J, Kolvenbach CG et al (2008) Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain. Protein Sci 17:95–106
McCombs JR, Owen SC (2015) Antibody drug conjugates: design and selection of linker, payload and conjugation chemistry. AAPS J 17:339–351
McCracken MN, Radu CG (2015) Targeted noninvasive imaging of the innate immune response. Proc Natl Acad Sci 112:5868–5869
McDonagh CF, Turcott E, Westendorf L et al (2006) Engineered antibody–drug conjugates with defined sites and stoichiometries of drug attachment. Protein Eng Des Sel 19:299–307
McFarland JM, Rabuka D (2015) Recent advances in chemoenzymatic bioconjugation methods. Org Chem Insights 5:7–14
McLaughlin J, LoRusso P (2016) Antibody–Drug Conjugates (ADCs) in clinical development. In: Olivier KJ Jr, Hurvitz SA (eds) Antibody-drug conjugates: fundamentals, drug development, and clinical outcomes to target cancer. Wiley, Hoboken, pp 321–344
Mindt TL, Jungi V, Wyss S et al (2007) Modification of different IgG1 antibodies via glutamine and lysine using bacterial and human tissue transglutaminase. Bioconjug Chem 19:271–278
Motoki M, Nio N (1983) Crosslinking between different food proteins by transglutaminase. J Food Sci 48:561–566
Navarre WW, Schneewind O (1994) Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in Gram-positive bacteria. Mol Microbiol 14:115–121
Ohtsuka T, Ota M, Nio N et al (2000) Comparison of substrate specificities of transglutaminases using synthetic peptides as acyl donors. Biosci Biotechnol Biochem 64:2608–2613
Okeley NM, Toki BE, Zhang X et al (2013) Metabolic engineering of monoclonal antibody carbohydrates for antibody–drug conjugation. Bioconjug Chem 24:1650–1655
Ornes S (2013) Antibody–drug conjugates. Proc Natl Acad Sci U S A 110:13695
Pallen MJ, Lam AC, Antonio M et al (2001) An embarrassment of sortases–a richness of substrates? Trends Microbiol 9:97–101
Panowski S, Bhakta S, Raab H et al (2014) Site-specific antibody drug conjugates for cancer therapy. MAbs 6:34–45
Parthasarathy R, Subramanian S, Boder ET (2007) Sortase A as a novel molecular “stapler” for sequence-specific protein conjugation. Bioconjug Chem 18:469–476
Pasut G, Veronese FM (2012) State of the art in PEGylation: the great versatility achieved after forty years of research. J Control Release 161:461–472
Perez HL, Cardarelli PM, Deshpande S et al (2014) Antibody–drug conjugates: current status and future directions. Drug Discov Today 19:869–881
Perry AM, Ton-That H, Mazmanian SK et al (2002) Anchoring of surface proteins to the cell wall of Staphylococcus aureus III Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring. J Biol Chem 277:16241–16248
Pharma F (2010) FDA: Pfizer voluntarily withdraws cancer treatment Mylotarg from US market [Online]. Available: https://www.fiercepharma.com/pharma/fda-pfizer-voluntarily-withdraws-cancer-treatment-mylotarg-from-u-s-market. Accessed June 21 2010
Rachel NM, Pelletier JN (2013) Biotechnological applications of transglutaminases. Biomol Ther 3:870–888
Rashidian M, Dozier JK, Distefano MD (2013) Enzymatic labeling of proteins: techniques and approaches. Bioconjug Chem 24:1277–1294
Rickert M, Strop P, Lui V et al (2016) Production of soluble and active microbial transglutaminase in Escherichia coli for site-specific antibody drug conjugation. Protein Sci 25:442–455
Roux KJ, Kim DI, Raida M et al (2012) A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells. J Cell Biol 196:801–810
Rowland A, Pietersz GA, McKenzie IF (1993) Preclinical investigation of the antitumour effects of anti-CD19-idarubicin immunoconjugates. Cancer Immunol Immunother 37:195–202
Sakamoto T, Sawamoto S, Tanaka T et al (2010) Enzyme-mediated site-specific antibody-protein modification using a ZZ domain as a linker. Bioconjug Chem 21:2227–2233
Schroeder DD, Tankersky DL, Lundblad JL (1981) A new preparation of modified immune serum globulin (human) suitable for intravenous administration. Vox Sang 40:383–394
Schumacher D, Hackenberger CP, Leonhardt H et al (2016) Current status: site-specific antibody drug conjugates. J Clin Immunol 36:100–107
Senter PD, Sievers EL (2012) The discovery and development of brentuximab vedotin for use in relapsed Hodgkin lymphoma and systemic anaplastic large cell lymphoma. Nat Biotechnol 30:631–637
Sesay MA (2003) Monoclonal antibody conjugation via chemical modification. Biopharm Int 16:32–39
Sharkey RM, Goldenberg DM (2008) Use of antibodies and immunoconjugates for the therapy of more accessible cancers. Adv Drug Deliv Rev 60:1407–1420
Shinya A, Yamashita K, Kohno H et al (2000) Involvement of transglutaminase in the receptor-mediated endocytosis of mouse peritoneal macrophages. Biol Pharm Bull 23:1511–1513
Siegmund V, Schmelz S, Dickgiesser S et al (2015) Locked by design: a conformationally constrained transglutaminase tag enables efficient site-specific conjugation. Angew Chem Int Ed 54:13420–13424
Siegmund V, Piater B, Zakeri B et al (2016) Spontaneous isopeptide bond formation as a powerful tool for engineering site-specific antibody-drug conjugates. Sci Rep 6:39291
Smith EL, Giddens JP, Iavarone AT et al (2014) Chemoenzymatic Fc glycosylation via engineered aldehyde tags. Bioconjug Chem 25:788–795
Sochaj AM, Świderska KW, Otlewski J (2015) Current methods for the synthesis of homogeneous antibody–drug conjugates. Biotechnol Adv 33:775–784
Spolaore B, Raboni S, Satwekar AA et al (2016) Site-specific transglutaminase-mediated conjugation of interferon α-2b at glutamine or lysine residues. Bioconjug Chem 27:2695–2706
Steffen W, Ko FC, Patel J et al (2017) Discovery of a microbial transglutaminase enabling highly site-specific labeling of proteins. J Biol Chem 292:15622–15635
Stephanopoulos N, Francis MB (2011) Choosing an effective protein bioconjugation strategy. Nat Chem Biol 7:876–884
Strop P (2014) Versatility of microbial transglutaminase. Bioconjug Chem 25:855–862
Strop P, Dorywalska MG, Rajpal A et al (2012 November 22) Engineered polypeptide conjugates and methods for making thereof using transglutaminase. PCT/IB2011/054899
Strop P, Liu S-H, Dorywalska M et al (2013) Location matters: site of conjugation modulates stability and pharmacokinetics of antibody drug conjugates. Chem Biol 20:161–167
Strop P, Tran T-T, Dorywalska M et al (2016) RN927C, a site-specific trop-2 antibody–drug conjugate (ADC) with enhanced stability, is highly efficacious in preclinical solid tumor models. Mol Cancer Ther 15:2698–2708
Sueda S, Yoneda S, Hayashi H (2011) Site-specific labeling of proteins by using biotin protein ligase conjugated with fluorophores. ChemBioChem 12:1367–1375
Suedhoff T, Birckbichler P, Lee K et al (1990) Differential expression of transglutaminase in human erythroleukemia cells in response to retinoic acid. Cancer Res 50:7830–7834
Sugimura Y, Hosono M, Wada F et al (2006) Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library identification of peptide substrates for TGASE 2 and factor XIIIA. J Biol Chem 281:17699–17706
Sugimura Y, Yokoyama K, Nio N et al (2008) Identification of preferred substrate sequences of microbial transglutaminase from Streptomyces mobaraensis using a phage-displayed peptide library. Arch Biochem Biophys 477:379–383
Sun MM, Beam KS, Cerveny CG et al (2005) Reduction− alkylation strategies for the modification of specific monoclonal antibody disulfides. Bioconjug Chem 16:1282–1290
Swee LK, Guimaraes CP, Sehrawat S et al (2013) Sortase-mediated modification of αDEC205 affords optimization of antigen presentation and immunization against a set of viral epitopes. Proc Natl Acad Sci 110:1428–1433
Ta H, Prabhu S, Leitner E et al (2011) Enzymatic single-chain antibody tagging: a universal approach to targeted molecular imaging and cell homing in cardiovascular disease. Circ Res 109:365–373
Tesfaw A, Assefa F (2014) Applications of transglutaminase in textile, wool, and leather processing. Int J Tex Sci 3:64–69
Theile CS, Witte MD, Blom AE et al (2013) Site-specific N-terminal labeling of proteins using sortase-mediated reactions. Nat Protoc 8:1800
Tong H, Zhang L, Kaspar A et al (2013) Peptide-conjugation induced conformational changes in human IgG1 observed by optimized negative-staining and individual-particle electron tomography. Sci Rep 3:1089
Torres M, Casadevall A (2008) The immunoglobulin constant region contributes to affinity and specificity. Trends Immunol 29:91–97
Tsuchikama K, An Z (2016) Antibody-drug conjugates: recent advances in conjugation and linker chemistries. Protein Cell 9(1):1–14
van de Donk NW, Dhimolea E (2012) Brentuximab vedotin. MAbs 4:458–465 Taylor & Francis
von Behring E, Kitasato S (1890) The mechanism of immunity in animals to diphtheria and tetanus. Deutsche Med Wochenschr 16:1113–1114
Wagner K, Kwakkenbos MJ, Claassen YB et al (2014) Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity. Proc Natl Acad Sci 111:16820–16825
Wakankar AA, Feeney MB, Rivera J et al (2010) Physicochemical stability of the antibody− drug conjugate trastuzumab-DM1: changes due to modification and conjugation processes. Bioconjug Chem 21:1588–1595
Wen X, Wu Q-P, Lu Y et al (2001) Poly (ethylene glycol)-conjugated anti-EGF receptor antibody C225 with radiometal chelator attached to the termini of polymer chains. Bioconjug Chem 12:545–553
Williamson DJ, Fascione MA, Webb ME et al (2012) Efficient N-terminal labeling of proteins by use of sortase. Angew Chem Int Ed 51:9377–9380
Witte MD, Cragnolini JJ, Dougan SK et al (2012) Preparation of unnatural N-to-N and C-to-C protein fusions. Proc Natl Acad Sci 109:11993–11998
Witte MD, Theile C, Wu T et al (2013) Production of unnaturally linked chimeric proteins using a combination of sortase-catalyzed transpeptidation and click chemistry. Nat Protoc 8:1808
Wu P, Shui W, Carlson BL et al (2009) Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag. Proc Natl Acad Sci 106:3000–3005
Yokoyama K, Nio N, Kikuchi Y (2004) Properties and applications of microbial transglutaminase. Appl Microbiol Biotechnol 64:447–454
Yokoyama K, Utsumi H, Nakamura T et al (2010) Screening for improved activity of a transglutaminase from Streptomyces mobaraensis created by a novel rational mutagenesis and random mutagenesis. Appl Microbiol Biotechnol 87:2087–2096
York D, Baker J, Holder PG et al (2016) Generating aldehyde-tagged antibodies with high titers and high formylglycine yields by supplementing culture media with copper (II). BMC Biotechnol 16:23
Younes A, Bartlett NL, Leonard JP et al (2010) Brentuximab vedotin (SGN-35) for relapsed CD30-positive lymphomas. N Engl J Med 363:1812–1821
Zuberbühler K, Casi G, Bernardes GJ et al (2012) Fucose-specific conjugation of hydrazide derivatives to a vascular-targeting monoclonal antibody in IgG format. Chem Commun 48:7100–7102
Acknowledgment
The authors would like to acknowledge the support of the Malaysian Ministry of Education through the Higher Institution Centre of Excellence (HICoE) Grant (Grant No.311/CIPPM/44001005) and Universiti Sains Malaysia RUI Grant (1001/CABR/8011045).
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Chan, S.K., Choong, Y.S., Gan, C.Y., Lim, T.S. (2018). Chemoenzymatic Bioconjugation of Antibodies: Linking Proteins for Biomedical Applications. In: Kuddus, M. (eds) Enzymes in Food Technology. Springer, Singapore. https://doi.org/10.1007/978-981-13-1933-4_18
Download citation
DOI: https://doi.org/10.1007/978-981-13-1933-4_18
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-13-1932-7
Online ISBN: 978-981-13-1933-4
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)