title: Distinct antibody species: structural differences creating therapeutic opportunities.
abstract: Antibodies have been a remarkably successful class of molecules for binding a large number of antigens in therapeutic, diagnostic, and research applications. Typical antibodies derived from mouse or human sources use the surface formed by complementarity determining regions (CDRs) on the variable regions of the heavy chain/light chain heterodimer, which typically forms a relatively flat binding surface. Alternative species, particularly camelids and bovines, provide a unique paradigm for antigen recognition through novel domains which form the antigen binding paratope. For camelids, heavy chain antibodies bind antigen with only a single heavy chain variable region, in the absence of light chains. In bovines, ultralong CDR-H3 regions form an independently folding minidomain, which protrudes from the surface of the antibody and is diverse in both its sequence and disulfide patterns. The atypical paratopes of camelids and bovines potentially provide the ability to interact with different epitopes, particularly recessed or concave surfaces, compared to traditional antibodies.
authors.affiliation: Cellular and Molecular Immunology, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium. Electronic address: svmuylde@vub.ac.be.
authors.forename: Serge
authors.initials: S
authors.lastname: Muyldermans
authors.affiliation: Fabrus Inc., Division of Sevion Therapeutics, San Diego, CA 92121, United States; Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, United States. Electronic address: vvsmider@scripps.edu.
authors.forename: Vaughn V
authors.initials: VV
authors.lastname: Smider
mesh_terms: D000818:Animals; D000906:Antibodies / Q000737:chemistry / Q000378:metabolism*; D002161:Camelids, New World; D002417:Cattle; D022801:Complementarity Determining Regions / Q000737:chemistry / Q000378:metabolism*; D003198:Computer Simulation; D005818:Genetic Engineering; D006801:Humans; D016056:Immunodominant Epitopes / Q000737:chemistry / Q000378:metabolism*; D007167:Immunotherapy / Q000379:methods*; D051379:Mice; D011487:Protein Conformation; D012698:Serologic Tests; D013045:Species Specificity
chemical_list: D000906:Antibodies; D022801:Complementarity Determining Regions; D016056:Immunodominant Epitopes