In the 1990s, scientists reported the existence of peculiar antibody subsets found in camelids and cartilaginous fish that are devoid of light chains. The discovery of these so-called “heavy-chain only antibodies” (HCAbs) in camelids and certain sharks represented a revolution in antibody research. In both HCAb variants, a single domain (termed VHH and VNAR for camelid and shark HCAbs, respectively) mediates antigen recognition and thus represents the functional equivalent of a Fab fragment from conventional antibodies. Interestingly, the context of the full-length HCAb is not required for the VHHs/VNARs to properly fold, maintain structural stability, and function as antigen-binding units. Hence, VHHs/VNARs can be produced as single entities and are termed “single-domain antibodies” (sdAbs) because they retain the complete antigen-binding potential of their full-length counterpart. As such, camelid and shark sdAbs are the smallest known functional antibody fragments (4 nm long and 2.5 nm wide). They possess robust folding properties, increased solubility, and unique paratope features usually not found in conventional antibodies. The unique characteristics of camelid and shark sdAbs enable important discoveries in infectious disease biology and allow their deployment in the development of novel diagnostics and therapeutics.
The goal of this Research Topic is to highlight innovative applications of camelid and shark sdAbs for basic and translational research in the field of infectious diseases and for the development of new therapeutic and diagnostic modalities.
The following topics on the development and use of sdAbs (VHHs and VNARs) in infectious disease research are welcome:
1. Exploration of fundamental pathogen biology using sdAb approaches
2. sdAb-fuelled drug discovery and rational vaccine design
3. sdAb-enabled pathogen diagnostic and test-of-cure applications
4. sdAb-based therapy developments (pathogen-directed approaches, host-directed approaches, toxin neutralization, and transmission-blocking strategies)
In the 1990s, scientists reported the existence of peculiar antibody subsets found in camelids and cartilaginous fish that are devoid of light chains. The discovery of these so-called “heavy-chain only antibodies” (HCAbs) in camelids and certain sharks represented a revolution in antibody research. In both HCAb variants, a single domain (termed VHH and VNAR for camelid and shark HCAbs, respectively) mediates antigen recognition and thus represents the functional equivalent of a Fab fragment from conventional antibodies. Interestingly, the context of the full-length HCAb is not required for the VHHs/VNARs to properly fold, maintain structural stability, and function as antigen-binding units. Hence, VHHs/VNARs can be produced as single entities and are termed “single-domain antibodies” (sdAbs) because they retain the complete antigen-binding potential of their full-length counterpart. As such, camelid and shark sdAbs are the smallest known functional antibody fragments (4 nm long and 2.5 nm wide). They possess robust folding properties, increased solubility, and unique paratope features usually not found in conventional antibodies. The unique characteristics of camelid and shark sdAbs enable important discoveries in infectious disease biology and allow their deployment in the development of novel diagnostics and therapeutics.
The goal of this Research Topic is to highlight innovative applications of camelid and shark sdAbs for basic and translational research in the field of infectious diseases and for the development of new therapeutic and diagnostic modalities.
The following topics on the development and use of sdAbs (VHHs and VNARs) in infectious disease research are welcome:
1. Exploration of fundamental pathogen biology using sdAb approaches
2. sdAb-fuelled drug discovery and rational vaccine design
3. sdAb-enabled pathogen diagnostic and test-of-cure applications
4. sdAb-based therapy developments (pathogen-directed approaches, host-directed approaches, toxin neutralization, and transmission-blocking strategies)
