The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies
Open accessAbstract
Clefts on protein surfaces are avoided by antigen-combining sites of conventional antibodies, in contrast to heavy-chain antibodies (HCAbs) of camelids that seem to be attracted by enzymes’ substrate pockets. The explanation for this pronounced preference of HCAbs was investigated. Eight single domain antigen-binding fragments of HCAbs (VHH) with nanomolar affinities for lysozyme were isolated from three immunized dromedaries. Six of eight VHHs compete with small lysozyme inhibitors. This ratio of active site binders is also found within the VHH pool derived from polyclonal HCAbs purified from the serum of the immunized dromedary. The crystal structures of six VHHs in complex with lysozyme and their interaction surfaces were compared to those of conventional antibodies with the same antigen. The interface sizes of VHH and conventional antibodies to lysozyme are very similar as well as the number and chemical nature of the contacts. The main difference comes from the compact prolate shape of VHH that presents a large convex paratope, predominantly formed by the H3 loop and interacting, although with different structures, into the concave lysozyme substrate-binding pocket. Therefore, a single domain antigen-combining site has a clear structural advantage over a conventional dimeric format for targeting clefts on antigenic surfaces.
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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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“Occasionally, VHHs with affinity constants (KD) as low as 100 pM are isolated (Saerens et al. 2004; De Genst et al. 2006; Harmsen et al. 2006), which equals the affinity ceiling proposed for natural antibodies (Sundberg and Mariuzza 2002).”
BackgroundInfluentialUltrasensitive and Highly Specific Lateral Flow Assays for Point-of-Care Diagnosis
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David vs. Goliath: The Structure, Function, and Clinical Prospects of Antibody Fragments
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Metadata
- Authors
- De Genst, E., Silence, K., Decanniere, K., Conrath, K., Loris, R., Kinne, J., Muyldermans, S., & Wyns, L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-03-13
- Volume
- 103
- Issue
- 12
- Pages
- 4586-4591
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2037042031
- Cited by
- 676
- References
- 49
- FWCI
- 14.11
- Type
- journal article
- Language
- en
- Open access
- green
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