“Cleavable” hapten–biotin conjugates: Preparation and use for the generation of anti-steroid single-domain antibody fragments
Antibody engineering technology has the potential to provide artificial antibodies with higher performance than conventional antibodies. Filamentous phage particles are often used to express a vast diversity of mutated antibody fragments from which clones displaying improved fragments can be isolate...
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Published in | Analytical biochemistry Vol. 387; no. 2; pp. 257 - 266 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier Inc
15.04.2009
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Abstract | Antibody engineering technology has the potential to provide artificial antibodies with higher performance than conventional antibodies. Filamentous phage particles are often used to express a vast diversity of mutated antibody fragments from which clones displaying improved fragments can be isolated. We recently showed that hapten–biotin conjugates, combined via a linker involving a reductively cleavable disulfide bond, are useful for isolating phage clones displaying high-affinity anti-hapten antibody fragments. Here we prepare cleavable hapten–biotin conjugates and use them to isolate anti-hapten antibody fragments with relatively low affinities. Three diagnostically important steroids (estradiol-17β [E
2], cortisol, and 17α-hydroxyprogesterone) were each coupled with a biotin derivative containing a disulfide bond. These conjugates could be bound simultaneously by their relevant anti-steroid antibody and NeutrAvidin, and their linkers were easily cleaved by dithiothreitol (DTT) treatment. The E
2–biotin conjugate was used to generate anti-E
2 single-domain antibody fragments (sdAbs). Random point mutations were introduced by error-prone PCR into the gene fragment encoding the V
H domain of a mouse anti-E
2 antibody, and these products were expressed as phagemid particles that were reacted with the E
2–biotin conjugates that had already been immobilized on a solid-phase via NeutrAvidin. Thorough washing off of nonspecific phages and subsequent DTT treatment provided a phagemid clone that displayed a mutated sdAb with improved binding properties. |
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AbstractList | Antibody engineering technology has the potential to provide artificial antibodies with higher performance than conventional antibodies. Filamentous phage particles are often used to express a vast diversity of mutated antibody fragments from which clones displaying improved fragments can be isolated. We recently showed that hapten-biotin conjugates, combined via a linker involving a reductively cleavable disulfide bond, are useful for isolating phage clones displaying high-affinity anti-hapten antibody fragments. Here we prepare cleavable hapten-biotin conjugates and use them to isolate anti-hapten antibody fragments with relatively low affinities. Three diagnostically important steroids (estradiol-17beta [E(2)], cortisol, and 17alpha-hydroxyprogesterone) were each coupled with a biotin derivative containing a disulfide bond. These conjugates could be bound simultaneously by their relevant anti-steroid antibody and NeutrAvidin, and their linkers were easily cleaved by dithiothreitol (DTT) treatment. The E(2)-biotin conjugate was used to generate anti-E(2) single-domain antibody fragments (sdAbs). Random point mutations were introduced by error-prone PCR into the gene fragment encoding the V(H) domain of a mouse anti-E(2) antibody, and these products were expressed as phagemid particles that were reacted with the E(2)-biotin conjugates that had already been immobilized on a solid-phase via NeutrAvidin. Thorough washing off of nonspecific phages and subsequent DTT treatment provided a phagemid clone that displayed a mutated sdAb with improved binding properties. Antibody engineering technology has the potential to provide artificial antibodies with higher performance than conventional antibodies. Filamentous phage particles are often used to express a vast diversity of mutated antibody fragments from which clones displaying improved fragments can be isolated. We recently showed that hapten–biotin conjugates, combined via a linker involving a reductively cleavable disulfide bond, are useful for isolating phage clones displaying high-affinity anti-hapten antibody fragments. Here we prepare cleavable hapten–biotin conjugates and use them to isolate anti-hapten antibody fragments with relatively low affinities. Three diagnostically important steroids (estradiol-17β [E 2], cortisol, and 17α-hydroxyprogesterone) were each coupled with a biotin derivative containing a disulfide bond. These conjugates could be bound simultaneously by their relevant anti-steroid antibody and NeutrAvidin, and their linkers were easily cleaved by dithiothreitol (DTT) treatment. The E 2–biotin conjugate was used to generate anti-E 2 single-domain antibody fragments (sdAbs). Random point mutations were introduced by error-prone PCR into the gene fragment encoding the V H domain of a mouse anti-E 2 antibody, and these products were expressed as phagemid particles that were reacted with the E 2–biotin conjugates that had already been immobilized on a solid-phase via NeutrAvidin. Thorough washing off of nonspecific phages and subsequent DTT treatment provided a phagemid clone that displayed a mutated sdAb with improved binding properties. |
Author | Nakano, Masanori Kato, Yoshinori Karibe, Tsuyoshi Goto, Junichi Nishio, Tadashi Kobayashi, Norihiro Kanda, Tatsuaki Oyama, Hiroyuki Banzono, Erika |
Author_xml | – sequence: 1 givenname: Norihiro surname: Kobayashi fullname: Kobayashi, Norihiro email: no-kobay@kobepharma-u.ac.jp organization: Kobe Pharmaceutical University, Higashinada-ku, Kobe 658-8558, Japan – sequence: 2 givenname: Hiroyuki surname: Oyama fullname: Oyama, Hiroyuki organization: Kobe Pharmaceutical University, Higashinada-ku, Kobe 658-8558, Japan – sequence: 3 givenname: Masanori surname: Nakano fullname: Nakano, Masanori organization: Kobe Pharmaceutical University, Higashinada-ku, Kobe 658-8558, Japan – sequence: 4 givenname: Tatsuaki surname: Kanda fullname: Kanda, Tatsuaki organization: Kobe Pharmaceutical University, Higashinada-ku, Kobe 658-8558, Japan – sequence: 5 givenname: Erika surname: Banzono fullname: Banzono, Erika organization: Kobe Pharmaceutical University, Higashinada-ku, Kobe 658-8558, Japan – sequence: 6 givenname: Yoshinori surname: Kato fullname: Kato, Yoshinori organization: Kobe Pharmaceutical University, Higashinada-ku, Kobe 658-8558, Japan – sequence: 7 givenname: Tsuyoshi surname: Karibe fullname: Karibe, Tsuyoshi organization: Graduate School of Pharmaceutical Sciences, Tohoku University, Aoba-ku, Sendai 980-8578, Japan – sequence: 8 givenname: Tadashi surname: Nishio fullname: Nishio, Tadashi organization: Graduate School of Pharmaceutical Sciences, Tohoku University, Aoba-ku, Sendai 980-8578, Japan – sequence: 9 givenname: Junichi surname: Goto fullname: Goto, Junichi organization: Department of Pharmaceutical Sciences, Tohoku University Hospital, Aoba-ku, Sendai 980-8574, Japan |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19454256$$D View this record in MEDLINE/PubMed |
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Keywords | Estradiol-17β Steroid–biotin conjugate Phage display Antibody engineering Single-domain antibody fragment Hapten |
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SubjectTerms | 17-alpha-Hydroxyprogesterone - immunology Amino Acid Sequence Antibody engineering Base Sequence Biotin Estradiol - immunology Estradiol-17β Hapten Haptens - immunology Hydrocortisone - immunology Immunoglobulin Fragments - biosynthesis Molecular Sequence Data Phage display Protein Engineering Single-domain antibody fragment Steroid–biotin conjugate |
Title | “Cleavable” hapten–biotin conjugates: Preparation and use for the generation of anti-steroid single-domain antibody fragments |
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