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Bglbrick strategy for the construction of single domain antibody fusions

Single domain antibodies, recombinantly expressed variable domains derived from camelid heavy chain antibodies, are often expressed as multimers for detection and therapeutic applications. Constructs in which several single domain antibodies are genetically fused serially, as well as those in which...

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Detalles Bibliográficos
Autores principales: Goldman, Ellen R., Broussard, Aeris, Anderson, George P., Liu, Jinny L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5753753/
https://www.ncbi.nlm.nih.gov/pubmed/29322100
http://dx.doi.org/10.1016/j.heliyon.2017.e00474
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author Goldman, Ellen R.
Broussard, Aeris
Anderson, George P.
Liu, Jinny L.
author_facet Goldman, Ellen R.
Broussard, Aeris
Anderson, George P.
Liu, Jinny L.
author_sort Goldman, Ellen R.
collection PubMed
description Single domain antibodies, recombinantly expressed variable domains derived from camelid heavy chain antibodies, are often expressed as multimers for detection and therapeutic applications. Constructs in which several single domain antibodies are genetically fused serially, as well as those in which single domain antibodies are genetically linked with domains that naturally form multimers, yield improvement in apparent binding affinity due to avidity. Here, using a single domain antibody that binds envelope protein from the Dengue virus, we demonstrated the construction of single domain antibody dimers using the Bglbrick cloning strategy. Constructing single domain antibodies and multimerization domains as Bglbrick parts enables the easy mixing and matching of parts. The dimeric constructs provided enhanced fluorescent signal in assays for detection of Dengue virus like particles over the monomeric single domain antibody.
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spelling pubmed-57537532018-01-10 Bglbrick strategy for the construction of single domain antibody fusions Goldman, Ellen R. Broussard, Aeris Anderson, George P. Liu, Jinny L. Heliyon Article Single domain antibodies, recombinantly expressed variable domains derived from camelid heavy chain antibodies, are often expressed as multimers for detection and therapeutic applications. Constructs in which several single domain antibodies are genetically fused serially, as well as those in which single domain antibodies are genetically linked with domains that naturally form multimers, yield improvement in apparent binding affinity due to avidity. Here, using a single domain antibody that binds envelope protein from the Dengue virus, we demonstrated the construction of single domain antibody dimers using the Bglbrick cloning strategy. Constructing single domain antibodies and multimerization domains as Bglbrick parts enables the easy mixing and matching of parts. The dimeric constructs provided enhanced fluorescent signal in assays for detection of Dengue virus like particles over the monomeric single domain antibody. Elsevier 2018-01-11 /pmc/articles/PMC5753753/ /pubmed/29322100 http://dx.doi.org/10.1016/j.heliyon.2017.e00474 Text en © 2017 Published by Elsevier Ltd. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Goldman, Ellen R.
Broussard, Aeris
Anderson, George P.
Liu, Jinny L.
Bglbrick strategy for the construction of single domain antibody fusions
title Bglbrick strategy for the construction of single domain antibody fusions
title_full Bglbrick strategy for the construction of single domain antibody fusions
title_fullStr Bglbrick strategy for the construction of single domain antibody fusions
title_full_unstemmed Bglbrick strategy for the construction of single domain antibody fusions
title_short Bglbrick strategy for the construction of single domain antibody fusions
title_sort bglbrick strategy for the construction of single domain antibody fusions
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5753753/
https://www.ncbi.nlm.nih.gov/pubmed/29322100
http://dx.doi.org/10.1016/j.heliyon.2017.e00474
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