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Abstract
Heavy chain only antibodies (HCAbs) repre- sent a rare type of antibody that is devoid of light chains and the CH1 domain that have been reported in cartilaginous fish and camelids. By analyzing transcript data and genome sequences, we conducted a comprehen- sive analysis of Bactrian camel immunoglobulin heavy chain genes. Based on the transcript data, one μ gene, five γ genes, one α gene and one e gene were found. Additionally, the variable region of HCAbs (VHH) and the conventional antibodies (VH) sequences associated with the γ3, γ1a/b and μ genes were amplified. Based on these genome sequences, seven DH, six JH, μ, γ2a, γ2c, α, and e genes and a portion of a γ3 gene were observed. Different Kozak sequences within different VH families were found in our analysis, and the variability index differed between the VHH3 and VH3 families. Phyloge- netic analysis of the constant regions of the camelid immunoglobulin genes indicates that these genes appeared before the evolutionary divergence of Bactrian camels and dromedaries.
Highlights
Innate immunity is the first line of defense against pathogenic microorganisms
Due to a relatively long and protruding H3 loop and the absence of light chains, Heavy chain only antibodies (HCAbs) can interact with concave antigen binding surfaces and might be better adapted to target epitopes that are normally inaccessible for conventional antibodies[12]
The variable region library of IgM was investigated using 5′ RACE of spleen RNA that was isolated from one Bactrian camel
Summary
Innate immunity is the first line of defense against pathogenic microorganisms. when pathogens break this early defense, the adaptive humoral immune system produces specific antibodies (Abs) from terminally differentiated B lymphocytes, which bind to specific targets or antigens derived from the pathogen to defend against further infection. CH1, which typically forms covalent bonds with CL domains in conventional Abs (cAbs), is present in the genome of the heavy chain isotype for the HCAbs but is absent after mRNA splicing. This finding might be due to the presence of a point mutation at the conserved GT in the splice signal at the 3′ end of the CH1 exon to AT[11]. Due to a relatively long and protruding H3 loop and the absence of light chains, HCAbs can interact with concave antigen binding surfaces and might be better adapted to target epitopes that are normally inaccessible for conventional antibodies[12]. We provide a more thorough analysis of Bactrian camel IgH genes based on our own sequence data and on previous studies
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