Competitive Selection from Single Domain Antibody Libraries Allows Isolation of High-Affinity Antihapten Antibodies That Are Not Favored in the llama Immune Response
Single-domain antibodies (sdAbs) found in camelids lack a light chain, and their antigen-binding site sits completely in the heavy-chain variable domain (VHH). Their simplicity, thermostability, and ease in expression have made VHHs highly attractive. Although this has been successfully exploited fo...
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Published in | Analytical chemistry (Washington) Vol. 83; no. 18; pp. 7213 - 7220 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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United States
American Chemical Society
15.09.2011
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Abstract | Single-domain antibodies (sdAbs) found in camelids lack a light chain, and their antigen-binding site sits completely in the heavy-chain variable domain (VHH). Their simplicity, thermostability, and ease in expression have made VHHs highly attractive. Although this has been successfully exploited for macromolecular antigens, their application to the detection of small molecules is still limited to a very few reports, mostly describing low-affinity VHHs. Using triclocarban (TCC) as a model hapten, we found that conventional antibodies, IgG1 fraction, reacted with free TCC with a higher relative affinity (IC50 51.0 ng/mL) than did the sdAbs (IgG2 and IgG3, 497 and 370 ng/mL, respectively). A VHH library was prepared, and by elution of phage with limiting concentrations of TCC and competitive selection of binders, we were able to isolate high-affinity clones, K D 0.98–1.37 nM (SPR), which allowed development of a competitive assay for TCC with an IC50 = 3.5 ng/mL (11 nM). This represents a 100-fold improvement with regard to the performance of the sdAb serum fraction, and it is 100-fold better than the IC50 attained with other antihapten VHHs reported thus far. Despite the modest overall antihapten sdAbs response in llamas, a small subpopulation of high-affinity VHHs is generated that can be isolated by careful design of the selection process. |
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AbstractList | Single-domain antibodies (sdAbs) found in camelids lack a light chain, and their antigen-binding site sits completely in the heavy-chain variable domain (VHH). Their simplicity, thermostability, and ease in expression have made VHHs highly attractive. Although this has been successfully exploited for macromolecular antigens, their application to the detection of small molecules is still limited to a very few reports, mostly describing low-affinity VHHs. Using triclocarban (TCC) as a model hapten, we found that conventional antibodies, IgG1 fraction, reacted with free TCC with a higher relative affinity (IC... 51.0 ng/mL) than did the sdAbs (IgG2 and IgG3, 497 and 370 ng/mL, respectively). A VHH library was prepared, and by elution of phage with limiting concentrations of TCC and competitive selection of binders, we were able to isolate high-affinity clones, K... 0.98-1.37 nM (SPR), which allowed development of a competitive assay for TCC with an IC... = 3.5 ng/mL (11 nM). This represents a 100-fold improvement with regard to the performance of the sdAb serum fraction, and it is 100-fold better than the IC... attained with other antihapten VHHs reported thus far. Despite the modest overall antihapten sdAbs response in llamas, a small subpopulation of high-affinity VHHs is generated that can be isolated by careful design of the selection process. (ProQuest: ... denotes formulae/symbols omitted.) Single-domain antibodies (sdAbs) found in camelids lack a light chain, and their antigen-binding site sits completely in the heavy-chain variable domain (VHH). Their simplicity, thermostability, and ease in expression have made VHHs highly attractive. Although this has been successfully exploited for macromolecular antigens, their application to the detection of small molecules is still limited to a very few reports, mostly describing low-affinity VHHs. Using triclocarban (TCC) as a model hapten, we found that conventional antibodies, IgG1 fraction, reacted with free TCC with a higher relative affinity (IC(50) 51.0 ng/mL) than did the sdAbs (IgG2 and IgG3, 497 and 370 ng/mL, respectively). A VHH library was prepared, and by elution of phage with limiting concentrations of TCC and competitive selection of binders, we were able to isolate high-affinity clones, K(D) 0.98-1.37 nM (SPR), which allowed development of a competitive assay for TCC with an IC(50) = 3.5 ng/mL (11 nM). This represents a 100-fold improvement with regard to the performance of the sdAb serum fraction, and it is 100-fold better than the IC(50) attained with other antihapten VHHs reported thus far. Despite the modest overall antihapten sdAbs response in llamas, a small subpopulation of high-affinity VHHs is generated that can be isolated by careful design of the selection process. Single-domain antibodies (sdAbs) found in camelids lack a light chain, and their antigen-binding site sits completely in the heavy-chain variable domain (VHH). Their simplicity, thermostability, and ease in expression have made VHHs highly attractive. Although this has been successfully exploited for macromolecular antigens, their application to the detection of small molecules is still limited to a very few reports, mostly describing low-affinity VHHs. Using triclocarban (TCC) as a model hapten, we found that conventional antibodies, IgG1 fraction, reacted with free TCC with a higher relative affinity (IC50 51.0 ng/mL) than did the sdAbs (IgG2 and IgG3, 497 and 370 ng/mL, respectively). A VHH library was prepared, and by elution of phage with limiting concentrations of TCC and competitive selection of binders, we were able to isolate high-affinity clones, K D 0.98–1.37 nM (SPR), which allowed development of a competitive assay for TCC with an IC50 = 3.5 ng/mL (11 nM). This represents a 100-fold improvement with regard to the performance of the sdAb serum fraction, and it is 100-fold better than the IC50 attained with other antihapten VHHs reported thus far. Despite the modest overall antihapten sdAbs response in llamas, a small subpopulation of high-affinity VHHs is generated that can be isolated by careful design of the selection process. Single-domain antibodies (sdAbs) found in camelids, lack a light chain and their antigen-binding site sits completely in the heavy-chain variable domain (VHH). Their simplicity, thermostability, and ease in expression have made VHHs highly attractive. While this has been successfully exploited for macromolecular antigens, their application to the detection of small molecules is still limited to a very few reports, mostly describing low affinity VHHs. Using triclocarban (TCC) as a model hapten, we found that conventional antibodies, IgG1 fraction, reacted with free TCC with a higher relative affinity (IC 50 51.0 ng/mL) than did the sdAbs (IgG2 and IgG3, 497 and 370 ng/mL, respectively). A VHH library was prepared, and by elution of phage with limiting concentrations of TCC and competitive selection of binders, we were able to isolate high-affinity clones, K D 0.98–1.37 nM (SPR) which allowed development of a competitive assay for TCC with an IC 50 = 3.5 ng/mL (11 nM). This represents a 100-fold improvement with regard to the performance of the sdAb serum fraction, and it is 100-fold better than the IC 50 attained with other anti-hapten VHHs reported thus far. Despite the modest overall anti-hapten sdAbs response in llamas, a small subpopulation of high affinity VHHs are generated that can be isolated by carefully design of the selection process. |
Author | Rossotti, Martin Carleiza, Carmen Hammock, Bruce D Pritsch, Otto Last, Jerold A Carrión, Federico Ahn, Ki Chang Tabares-da Rosa, Sofia González-Sapienza, Gualberto |
AuthorAffiliation | Pulmonary/Critical Care Medicine, School of Medicine Institut Pasteur de Montevideo University of California, Davis Department of Entomology and Cancer Research Center Universidad de la República Intendencia Municipal de Montevideo |
AuthorAffiliation_xml | – name: Pulmonary/Critical Care Medicine, School of Medicine – name: Intendencia Municipal de Montevideo – name: Department of Entomology and Cancer Research Center – name: – name: University of California, Davis – name: Universidad de la República – name: Institut Pasteur de Montevideo – name: 4 Departamento de Inmunobiología, Facultad de Medicina, UDELAR – name: 2 Zoo Parque Lecocq, Intendencia Municipal de Montevideo – name: 5 Department of Entomology and Cancer Research Center, University of California, Davis, CA, USA – name: 3 Institut Pasteur de Montevideo, Uruguay – name: 1 Cátedra de Inmunología, Facultad de Química, Instituto de Higiene, UDELAR, Montevideo, Uruguay – name: 6 Pulmonary/Critical Care Medicine, School of Medicine, University of California, Davis, CA, USA |
Author_xml | – sequence: 1 givenname: Sofia surname: Tabares-da Rosa fullname: Tabares-da Rosa, Sofia – sequence: 2 givenname: Martin surname: Rossotti fullname: Rossotti, Martin – sequence: 3 givenname: Carmen surname: Carleiza fullname: Carleiza, Carmen – sequence: 4 givenname: Federico surname: Carrión fullname: Carrión, Federico – sequence: 5 givenname: Otto surname: Pritsch fullname: Pritsch, Otto – sequence: 6 givenname: Ki Chang surname: Ahn fullname: Ahn, Ki Chang – sequence: 7 givenname: Jerold A surname: Last fullname: Last, Jerold A – sequence: 8 givenname: Bruce D surname: Hammock fullname: Hammock, Bruce D – sequence: 9 givenname: Gualberto surname: González-Sapienza fullname: González-Sapienza, Gualberto email: ggonzal@fq.edu.uy |
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Snippet | Single-domain antibodies (sdAbs) found in camelids lack a light chain, and their antigen-binding site sits completely in the heavy-chain variable domain (VHH).... Single-domain antibodies (sdAbs) found in camelids, lack a light chain and their antigen-binding site sits completely in the heavy-chain variable domain (VHH).... |
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SubjectTerms | Analytical chemistry Animals Antibodies Antibodies - immunology Antibodies - isolation & purification Antigens Binding Sites Biochemistry, Molecular Biology Camelids, New World Camelids, New World - immunology Carbanilides Carbanilides - immunology Cloning Haptens Haptens - immunology Life Sciences Male Molecules Peptide Library Recombinant Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Single-Chain Antibodies Single-Chain Antibodies - chemistry Single-Chain Antibodies - genetics Single-Chain Antibodies - metabolism Surface Plasmon Resonance |
Title | Competitive Selection from Single Domain Antibody Libraries Allows Isolation of High-Affinity Antihapten Antibodies That Are Not Favored in the llama Immune Response |
URI | http://dx.doi.org/10.1021/ac201824z https://www.ncbi.nlm.nih.gov/pubmed/21827167 https://www.proquest.com/docview/894852474/abstract/ https://riip.hal.science/pasteur-00686306 https://pubmed.ncbi.nlm.nih.gov/PMC3193053 |
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