Nanobodies as novel agents for disease diagnosis and therapy

International Journal of Nanomedicine

Volumn 8, Issue , 2013, Pages 4215-4227

  Siontorou, Christina G ^a  

^a UNIVERSITY OF PIRAEUS   (Greece)

Author keywords

Antibody expression; Formatting; Heavy chain antibodies; Molecular display; Nanobodies

Indexed keywords

EPITOPE; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2; IMMUNOGLOBULIN G3; IMMUNOGLOBULIN G4; NANOBODY;

AFFINITY CHROMATOGRAPHY; ANTIGEN BINDING; ARTIODACTYLA; CELLULAR DISTRIBUTION; DISEASE COURSE; HEAVY CHAIN; IMMUNOMODULATION; IMMUNOTHERAPY; MOLECULAR IMAGING; NONHUMAN; POINT MUTATION; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN EXPRESSION; REVIEW;

ANTIBODY EXPRESSION; FORMATTING; HEAVY CHAIN ANTIBODIES; MOLECULAR DISPLAY; NANOBODIES;

ANIMALS; CAMELS; DRUG DELIVERY SYSTEMS; IMMUNOGLOBULIN HEAVY CHAINS; MOLECULAR IMAGING; NANOMEDICINE; SINGLE-DOMAIN ANTIBODIES;

EID: 84887328669     PISSN: 11769114     EISSN: 11782013     Source Type: Journal    
DOI: 10.2147/IJN.S39428     Document Type: Review

References (84)

1. Elbakri A, Nelson PN, Abu Odeh RO. The state of antibody therapy. Hum Immunol. 2010;71(12):1243-1250.
2. Beckman RA, Weiner LM, Davis HM. Antibody constructs in cancer therapy: protein engineering strategies to improve exposure in solid tumors. Cancer. 2007;109(2):170-179.
3. Natsume A, Niwa R, Satoh M. Improving effector functions of antibodies for cancer treatment: Enhancing ADCC and CDC. Drug Des Devel Ther. 2009;3:7-16.
4. Iyer U, Kadambi VJ. Antibody drug conjugates-Trojan horses in the war on cancer. J Pharmacol Toxicol Methods. 2011;64(3):207-212.
5. Hughes B. Antibody-drug conjugates for cancer: poised to deliver? Nat Rev Drug Discov. 2010;9(9):665-667.
6. Litvak-Greenfeld D, Benhar I. Risks and untoward toxicities of antibody-based immunoconjugates. Adv Drug Deliv Rev. 2012;64(15): 1782-1799.
7. Hildebrandt IJ, Gambhir SS. Molecular imaging applications for immunology. Clin Immunol. 2004;111(2):210-224.
8. Borrebaeck CA, Malmborg AC, Furebring C, et al. Kinetic analysis of recombinant antibody-antigen interactions: relation between structural domains and antigen binding. Biotechnology (NY). 1992;10(6):697-698.
9. Lin S, Houston-Cummings NR, Prinz B, et al. A novel fragment of antigen binding (Fab) surface display platform using glycoengineered Pichia pastoris. J Immunol Methods. 2012;375(1-2):159-165.
10. Adams GP, Schier R, McCall AM, et al. High affinity restricts the localization and tumor penetration of single-chain fv antibody molecules. Cancer Res. 2001;61(12):4750-4755.
11. Nguyen A, Reyes AE, Zhang M, et al. The pharmacokinetics of an albumin-binding Fab (AB. Fab) can be modulated as a function of affinity for albumin. Protein Eng Des Sel. 2006;19(7):291-297.
12. Hamers-Casterman C, Atarhouch T, Muyldermans S, et al. Naturally occurring antibodies devoid of light chains. Nature. 1993;363(6428): 446-448.
13. Greenberg AS, Avila D, Hughes M, Hughes A, McKinney EC, Flajnik MF. A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks. Nature. 1995;374(6518):168-173.
14. Nuttall SD, Krishnan UV, Hattarki M, De Gori R, Irving RA, Hudson PJ. Isolation of the new antigen receptor from wobbegong sharks, and use as a scaffold for the display of protein loop libraries. Mol Immunol. 2001;38(4):313-326.
15. Muyldermans S. Nanobodies: natural single-domain antibodies. Annu Rev Biochem. 2013;82:775-797.
16. Mogoutov A, Kahane B. Data search strategy for science and technology emergence: a scalable and evolutionary query for nanotechnology tracking. Res Policy. 2007;36:893-903.
17. Siontorou CG, Batzias FA. Innovation in biotechnology: moving from academic research to product development-the case of biosensors. Crit Rev Biotechnol. 2010;30(2):79-98.
18. Leydesdorff L, Rafols I. A global map of science based on the ISI subject categories. J Am Soc Inf Sci Technol. 2009;60:348-362.
19. Muyldermans S, Atarhouch T, Saldanha J, Barbosa JA, Hamers R. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 1994;7(9):1129-1135.
20. Desmyter A, Transue TR, Ghahroudi MA, et al. Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme. Nat Struct Biol. 1996;3(9):803-811.
21. van der Linden RH, Frenken LG, de Geus B, et al. Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies. Biochim Biophys Acta. 1999;1431(1):37-46.
22. Vu KB, Ghahroudi MA, Wyns L, Muyldermans S. Comparison of llama VH sequences from conventional and heavy chain antibodies. Mol Immunol. 1997;34(16-17):1121-1131.
23. Arbabi Ghahroudi M, Desmyter A, Wyns L, Hamers R, Muyldermans S. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 1997;414(3):521-526.
24. Lauwereys M, Arbabi Ghahroudi M, Desmyter A, et al. Potent enzyme inhibitors derived from dromedary heavy-chain antibodies. EMBO J. 1998;17(13):3512-3520.
25. Spinelli S, Frenken LG, Hermans P, et al. Camelid heavy-chain variable domains provide efficient combining sites to haptens. Biochemistry. 2000;39(6):1217-1222.
26. Frenken LG, van der Linden RH, Hermans PW, et al. Isolation of antigen specific llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae. J Biotechnol. 2000;78(1):11-21.
27. Pérez JM, Renisio JG, Prompers JJ, et al. Thermal unfolding of a llama antibody fragment: a two-state reversible process. Biochemistry. 2001;40(1):74-83.
28. Dumoulin M, Conrath K, Van Meirhaeghe A, et al. Single-domain antibody fragments with high conformational stability. Protein Sci. 2002;11(3):500-515.
29. Muruganandam A, Tanha J, Narang S, Stanimirovic D. Selection of phage-displayed llama single-domain antibodies that transmigrate across human blood-brain barrier endothelium. FASEB J. 2002;16(2): 240-242.
30. Verheesen P, ten Haaft MR, Lindner N, Verrips CT, de Haard JJ. Beneficial properties of single-domain antibody fragments for application in immunoaffinity purification and immuno-perfusion chromatography. Biochim Biophys Acta. 2003;1624(1-3):21-28.
31. Stanfield RL, Dooley H, Flajnik MF, Wilson IA. Crystal structure of a shark single-domain antibody V region in complex with lysozyme. Science. 2004;305(5691):1770-1773.
32. Stijlemans B, Conrath K, Cortez-Retamozo V, et al. Efficient targeting of conserved cryptic epitopes of infectious agents by single domain antibodies. African trypanosomes as paradigm. J Biol Chem. 2004;279(2):1256-1261.
33. Cortez-Retamozo V, Backmann N, Senter PD, et al. Efficient cancer therapy with a nanobody-based conjugate. Cancer Res. 2004;64(8):2853-2857.
34. Zhang J, Tanha J, Hirama T, et al. Pentamerization of single-domain antibodies from phage libraries: a novel strategy for the rapid generation of high-avidity antibody reagents. J Mol Biol. 2004;335(1):49-56.
35. Pleschberger M, Saerens D, Weigert S, et al. An S-layer heavy chain camel antibody fusion protein for generation of a nanopatterned sensing layer to detect the prostate-specific antigen by surface plasmon resonance technology. Bioconjug Chem. 2004;15(3):664-671.
36. Joosten V, Roelofs MS, van den Dries N, et al. Production of bifunctional proteins by Aspergillus awamori: llama variable heavy chain antibody fragment (V(HH) R9 coupled to Arthromyces ramosus peroxidase (ARP). J Biotechnol. 2005;120(4):347-359.
37. Dolk E, van der Vaart M, Lutje Hulsik D, et al. Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo. Appl Environ Microbiol. 2005;71(1):442-450.
38. van der Vaart JM, Pant N, Wolvers D, et al. Reduction in morbidity of rotavirus induced diarrhoea in mice by yeast produced monovalent llama-derived antibody fragments. Vaccine. 2006;24(19):4130-4137.
39. Rothbauer U, Zolghadr K, Tillib S, et al. Targeting and tracing antigens in live cells with fluorescent nanobodies. Nat Methods. 2006;3(11): 887-889.
40. Rahbarizadeh F, Rasaee MJ, Forouzandeh M, Allameh AA. Over expression of anti-MUC1single-domain antibody fragments in the yeast Pichia pastoris. Mol Immunol. 2006;43(5):426-435.
41. Coppieters K, Dreier T, Silence K, et al. Formatted anti-tumor necrosis factor alpha VHH proteins derived from camelids show superior potency and targeting to inflamed joints in a murine model of collagen-induced arthritis. Arthritis Rheum. 2006;54(6):1856-1866.
42. Harrison RA, Hasson SS, Harmsen M, Laing GD, Conrath K, Theakston RD. Neutralisation of venom-induced haemorrhage by IgG from camels and llamas immunised with viper venom and also by endogenous, non-IgG components in camelid sera. Toxicon. 2006;47(3):364-368.
43. El Khattabi M, Adams H, Heezius E, et al. Llama single-chain antibody that blocks lipopolysaccharide binding and signaling: prospects for therapeutic applications. Clin Vaccine Immunol. 2006;13(10):1079-1086.
44. Gueorguieva D, Li S, Walsh N, Mukerji A, Tanha J, Pandey S. Identification of single-domain, Bax-specific intrabodies that confer resistance to mammalian cells against oxidative-stress-induced apoptosis. FASEB J. 2006;20(14):2636-2638.
45. Harmsen MM, van Solt CB, Fijten HP, et al. Passive immunization of guinea pigs with llama single-domain antibody fragments against foot-and-mouth disease. Vet Microbiol. 2007;120(3-4):193-206.
46. Roovers RC, Laeremans T, Huang L, et al. Efficient inhibition of EGFR signaling and of tumour growth by antagonistic anti-EFGR Nanobodies. Cancer Immunol Immunother. 2007;56(3):303-317.
47. Koch-Nolte F, Reyelt J, Schössow B, et al. Single domain antibodies from llama effectively and specifically block T cell ecto-ADP-ribosyltransferase ART2.2in vivo. FASEB J. 2007;21(13):3490-3498.
48. Achour I, Cavelier P, Tichit M, Bouchier C, Lafaye P, Rougeon F. Tetrameric and homodimeric camelid IgGs originate from the same IgH locus. J Immunol. 2008;181(3):2001-2009.
49. Huang L, Gainkam LO, Caveliers V, et al. SPECT imaging with 99mTc-labeled EGFR-specific nanobody for in vivo monitoring of EGFR expression. Mol Imaging Biol. 2008;10(3):167-175.
50. Vuchelen A, O'Day E, De Genst E, et al. (1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein. Biomol NMR Assign. 2009;3(2):231-233.
51. Klooster R, Eman MR, le Duc Q, et al. Selection and characterization of KDEL-specific VHH antibody fragments and their application in the study of ER resident protein expression. J Immunol Methods. 2009;342(1-2):1-12.
52. Van den Abbeele A, De Clercq S, De Ganck A, et al. A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction. Cell Mol Life Sci. 2010;67(9):1519-1535.
53. Flajnik MF, Kasahara M. Origin and evolution of the adaptive immune system: genetic events and selective pressures. Nat Rev Genet. 2010;11(1):47-59.
54. Kirchhofer A, Helma J, Schmidthals K, et al. Modulation of protein properties in living cells using nanobodies. Nat Struct Mol Biol. 2010;17(1):133-138.
55. Domanska K, Vanderhaegen S, Srinivasan V, et al. Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant. Proc Natl Acad Sci U S A. 2011;108(4): 1314-1319.
56. Rasmussen SG, Choi HJ, Fung JJ, et al. Structure of a nanobody-stabilized active state of the β(2) adrenoceptor. Nature. 2011;469(7329): 175-180.
57. Caussinus E, Kanca O, Affolter M. Fluorescent fusion protein knockout mediated by anti-GFP nanobody. Nat Struct Mol Biol. 2012;19(1): 117-121.
58. Broisat A, Hernot S, Toczek J, et al. Nanobodies targeting mouse/human VCAM1 for the nuclear imaging of atherosclerotic lesions. Circ Res. 2012;110(7):927-937.
59. Padlan EA. Anatomy of the antibody molecule. Mol Immunol. 1994;31(3):169-217.
60. Reiter Y, Schuck P, Boyd LF, Plaksin D. An antibody single-domain phage display library of a native heavy chain variable region: isolation of functional single-domain VH molecules with a unique interface. J Mol Biol. 1999;290(3):685-698.
61. Holt LJ, Herring C, Jespers LS, Woolven BP, Tomlinson IM. Domain antibodies: proteins for therapy. Trends Biotechnol. 2003;21(11): 484-490.
62. Nguyen VK, Desmyter A, Muyldermans S. Functional heavy-chain antibodies in Camelidae. Adv Immunol. 2001;79:261-296.
63. Govaert J, Pellis M, Deschacht N, et al. Dual beneficial effect of interloop disulfide bond for single domain antibody fragments. J Biol Chem. 2012;287(3):1970-1979.
64. Saerens D, Stijlemans B, Baral TN, et al. Parallel selection of multiple anti-infectome Nanobodies without access to purified antigens. J Immunol Methods. 2008;329(1-2):138-150.
65. Abbady AQ, Al-Mariri A, Zarkawi M, Al-Assad A, Muyldermans S. Evaluation of a nanobody phage display library constructed from a Brucella-immunised camel. Vet Immunol Immunopathol. 2011;142(1-2):49-56.
66. Goldman ER, Anderson GP, Liu JL, et al. Facile generation of heat-stable antiviral and antitoxin single domain antibodies from a semisynthetic llama library. Anal Chem. 2006;78(24):8245-8255.
67. Monegal A, Ami D, Martinelli C, et al. Immunological applications of single-domain llama recombinant antibodies isolated from a naïve library. Protein Eng Des Sel. 2009;22(4):273-280.
68. Gerngross TU. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat Biotechnol. 2004;22(11): 1409-1414.
69. Thomassen YE, Meijer W, Sierkstra L, Verrips CT. Large-scale production of VHH antibody fragments by Saccharomyces cerevisiae. Enzyme Microb Technol. 2002;3(3):273-278.
70. Sethuraman N, Stadheim TA. Challenges in therapeutic glycoprotein production. Curr Opin Biotechnol. 2006;17(4):341-346.
71. Ryckaert S, Pardon E, Steyaert J, Callewaert N. Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris. J Biotechnol. 2010;145(2):93-98.
72. Hagihara Y, Mine S, Uegaki K. Stabilization of an immunoglobulin fold domain by an engineered disulfide bond at the buried hydrophobic region. J Biol Chem. 2007;282(50):36489-36495.
73. Saerens D, Conrath K, Govaert J, Muyldermans S. Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains. J Mol Biol. 2008;377(2):478-488.
74. Harmsen MM, van Solt CB, van Zijderveld-van Bemmel AM, Niewold TA, van Zijderveld FG. Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapy. Appl Microbiol Biotechnol. 2006;72(3):544-551.
75. Pant N, Hultberg A, Zhao Y, et al. Lactobacilli expressing variable domain of llama heavy-chain antibody fragments (lactobodies) confer protection against rotavirus-induced diarrhea. J Infect Dis. 2006;194(11):1580-1588.
76. Hmila I, Abdallah RBA, Saerens D, et al. VHH, bivalent domains and chimeric Heavy chain-only antibodies with high neutralizing efficacy for scorpion toxin AahI'. Mol Immunol. 2008;45(14):3847-3856.
77. Hussack G, Arbabi-Ghahroudi M, van Faassen H, et al. Neutralization of Clostridium difficile toxin A with single-domain antibodies targeting the cell receptor binding domain. J Biol Chem. 2011;286(11):8961-8976.
78. Hulstein JJ, de Groot PG, Silence K, Veyradier A, Fijnheer R, Lenting PJ. A novel nanobody that detects the gain-of-function phenotype of von Willebrand factor in ADAMTS13 deficiency and von Willebrand disease type 2B. Blood. 2005;106(9):3035-3042.
79. Vaneycken I, Govaert J, Vincke C, et al. In vitro analysis and in vivo tumor targeting of a humanized, grafted nanobody in mice using pinhole SPECT/micro-CT. J Nucl Med. 2010;51(7):1099-1106.
80. Abulrob A, Sprong H, Van Bergen en Henegouwen P, Stanimirovic D. The blood-brain barrier transmigrating single domain antibody: mechanisms of transport and antigenic epitopes in human brain endothelial cells. J Neurochem. 2005;95(4):1201-1214.
81. Marquardt A, Muyldermans S, Przybylski M. A synthetic camel anti-lysozyme peptide antibody (peptibody) with flexible loop structure identified by high-resolution affinity mass spectrometry. Chemistry. 2006;12(7):1915-1923.
82. Backmann N, Zahnd C, Huber F, et al. A label-free immunosensor array using single-chain antibody fragments. Proc Natl Acad Sci U S A. 2005;102(41):14587-14592.
83. Steinhauer C, Wingren C, Hager AC, Borrebaeck CA. Single framework recombinant antibody fragments designed for protein chip applications. BioTechniques. 2002;Suppl:38-45.
84. Saerens D, Frederix F, Reekmans G, et al. Engineering camel single-domain antibodies and immobilization chemistry for human prostate-specific antigen sensing. Anal Chem. 2005;77(23):7547-7555.