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. 2022 Jan 19;98:106233. doi: 10.1016/j.ijsu.2022.106233

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Fig. 1 — A. Four peptide chains, two identical heavy chains, and two light chains make up the entire 150 kDa IgG antibody (Conventional IgG antibodies). The antigen-binding sites are produced by the two variable domains (VL and VH), while the stem of the antibody molecule is generated by the constant Fc-region.

B. Sera of camelids contain a unique functional heavy (H)-chain antibody (HCAbs) in addition to conventional antibodies. The VHH or nanobody (15 kDa), a single-domain antibody generated from HCAb, is the smallest available antibody fragment with functional antigen binding. HCAb is devoid of light chains and is capable of antigen recognition solely by one single domain, the variable heavy domain (VHH).

Fab; fragment antigen binding, CL; light chain constant region, CH; heavy chain constant region, VL; light chain variable region. VH; heavy chain variable region, VHH; variable heavy domain, HCAbs; heavy (H)-chain antibody.

Fig. 1 — A. Four peptide chains, two identical heavy chains, and two light chains make up the entire 150 kDa IgG antibody (Conventional IgG antibodies). The antigen-binding sites are produced by the two variable domains (VL and VH), while the stem of the antibody molecule is generated by the constant Fc-region.

B. Sera of camelids contain a unique functional heavy (H)-chain antibody (HCAbs) in addition to conventional antibodies. The VHH or nanobody (15 kDa), a single-domain antibody generated from HCAb, is the smallest available antibody fragment with functional antigen binding. HCAb is devoid of light chains and is capable of antigen recognition solely by one single domain, the variable heavy domain (VHH).

Fab; fragment antigen binding, CL; light chain constant region, CH; heavy chain constant region, VL; light chain variable region. VH; heavy chain variable region, VHH; variable heavy domain, HCAbs; heavy (H)-chain antibody.