Abstract
The homophilic potential emerges as an important biological principle to boost the potency of immunoglobulins. Since homophilic antibodies in human and mouse sera exist prior environmental exposure, they are part of the natural antibody repertoire. Nevertheless, hemophilic properties are also identified in induced antibody repertoire. The use of homophilicity of antibodies in the adaptive immunity signifies an archetypic antibody structure. The unique feature of homophilicity in the antibody repertoire also highlights an important mechanism to boost the antibody potency to protect against infection and atherosclerosis as well to treat cancer patients.
Highlights
HK surveyed the literature and wrote the article
The unique feature of homophilicity in the antibody repertoire highlights an important mechanism to boost the antibody potency to protect against infection and atherosclerosis as well to treat cancer patients
Since the T15 homophilic peptide dissociate the homophilic Ig complex, thereby reducing the polyvalency and binding potency, one can conclude that in sera, auto-anti-HLA antibodies are bound to corresponding HLA and are not detected
Summary
Oudin and Jerne are the founders of the idiotype concept [23, 24]. They “discovered” that one antibody could recognize another antibody as an individual and unique member of the immune system. The idiotype antibody individuality is separated from the antigen-binding site, determined by unique sequence variability. Both regions are linked by a unique variability and have a functional relation. Ab2β has been used as an antigen to induce a specific immune response [28] Another shared idiotype has been discovered in HIV-infected primates [29]. The domain responsible for antibody self-binding (homophilicity) has been described as a region in VH of T15, extending from CDR2 to Fr3 [35, 37] Because of their preimmune presence in normal sera, homophilic antibodies are segment of the natural antibody repertoire [33, 37]
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.