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Correspondence to Author: Kelvin H. Senry, Gareg Hussackman , Janiel Gettermans, Coly M. Brooks. 

Human Health Therapeutics Research Centre, National Research Council Canada, Ottawa, ON, Canada.

Abstract:

The basic characteristics of sdAbs were covered in one original study. In order to comprehend the perhaps different mechanisms of sdAbs’ recognition of antigens, Gordon et al. analyzed the structures of 345 sdAb:antigen complexes with 892 conventional antibody:antigen complexes in the largest study of this kind to date. The analysis’s findings are consistent with previous research in that sdAbs’ paratopes are smaller than those of conventional antibodies; however, there were no discernible variations in the size (measured in residues), amino acid composition, or accessibility of the epitopes that sdAbs target. This seeming paradox can be explained by the fact that a longer complementarity-determining region 3 (CDR3) loop contributes more interactions per residue within smaller sdAb paratopes. One original study looked into a novel method for finding camelid sdAb. Matsuda et al. created a predictive algorithm to find antigen-specific sdAbs without in vitro screening by using longitudinal sequencing and phylogenetic analysis of the peripheral sdAb repertoire, despite the fact that many groups have incorporated highthroughput sequencing of antibody repertoires into already-existing discovery pipelines that assess the antigen reactivity of individual clones in vitro. The accumulation of somatic hypermutations and high turnover rates within clonal families during the affinity maturation process serve as the foundation for discovering antigenspecific sdAbs. However, initial analysis of antigen-specific sdAbs recovered with this approach revealed inconsistent binding results across tests.

Citation:

Dr.Kelvin H. Senry, Single-Domain Antibodies—Biology, Engineering And Emerging Applications. Journal of Antibodies 2025.