The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Camel Single-domain Antibodies as Modular Building Units in Bispecific and Bivalent Antibody Constructs
Open accessAbstract
Single-domain antibodies against various antigens are isolated from the unique heavy-chain antibodies of immunized camels and llamas. These minimal sized binders are very robust and bind the antigen with high affinity in a monomeric state. We evaluated the feasibility to produce soluble, functional bispecific and bivalent antibodies in Escherichia coli with camel single-domain antibody fragments as building blocks. Two single-domain antibody fragments were tethered by the structural upper hinge of a natural antibody to generate bispecific molecules. This linker was chosen for its protease resistance in serum and its natural flexibility to reorient the upstream and downstream located domains. The expression levels, ease of purification, and the solubility of the recombinant proteins were comparable with those of the constituent monomers. The individual moieties fully retain the binding capacity and the binding characteristics within the recombinant bispecific constructs. The easy generation steps and the biophysical properties of these bispecific and bivalent constructs based on camel single-domain antibody fragments makes them particularly attractive for use in therapeutic or diagnostic programs.
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Cites
Naturally occurring antibodies devoid of light chains
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Self-citationAssembly of a Functional Immunoglobulin F v Fragment in Escherichia coli
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Selection and identification of single domain antibody fragments from camel heavy‐chain antibodies
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Self-citationCrystal structure of a camel single-domain VH antibody fragment in complex with lysozyme
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Self-citationHybrid hybridomas and their use in immunohistochemistry
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Self-citationComparison of llama VH sequences from conventional and heavy chain antibodies
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Cited by
Nanobodies: natural single-domain antibodies
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Self-citationProperties, production, and applications of camelid single-domain antibody fragments
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“However, antigen binding by the C-terminal VHH in such fusions can be compromised (Conrath et al. 2001b) presumably because of steric hindrance by the N-terminal VHH.”
BackgroundAlternative molecular formats and therapeutic applications for bispecific antibodies
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Nanobodies and nanobody-based human heavy chain antibodies as antitumor therapeutics
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“, a flexible glycine–serine linker, yields a bivalent molecule (30–35 kDa) with higher avidity for the antigen (57, 63).”
BackgroundBispecific antibodies for cancer therapy: The light at the end of the tunnel?
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Metadata
- Authors
- Els Conrath, K., Lauwereys, M., Wyns, L., & Muyldermans, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-03
- Volume
- 276
- Issue
- 10
- Pages
- 7346-7350
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2057278101
- Cited by
- 300
- References
- 26
- FWCI
- 5.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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