9/1/2023 0 Comments Prodeus igg![]() ![]() This broad coverage is facilitated by a low-affinity antigen-binding site. It is produced rapidly to provide immediate and broad defense against infections. IgM is the primordial member and the first to respond to foreign insults to the body. Igs are indeed one of the most exhaustively studied bio-molecules and have over a century revealed an endless trove of invaluable molecular secrets. Nature designed the antibody molecule including a whole family of these immunoglobulins (Igs) with great intricacy and intrigue. These findings call for a re-look at the clinical potential of IgM antibodies particularly in specific areas of cancer therapy, tissue pathology and vaccine design, where IgG antibodies have failed due to target inaccessibility. We further speculate that polyreactive IgMs, which enigmatically bind to more than one type of antigen, use the same modus operandi. We hypothesize that whereas the intact and rigid antigen-binding site of IgG hinders the antibody from docking with antigens that are obstructed, in IgM, the two component polypeptides of the antigen-binding site can dissociate from each other and navigate individually through obstacles like the ancestral single-polypeptide antibodies found in sharks and camelids, both components eventually re-grouping around the antigen. We reason that, contrary to current belief, IgM does not bind in a lock-and-key manner like IgG. Accordingly, oligomerization of GTP (30-mer) destroyed the binding of the IgG antibodies but enhanced that of the IgMs in inhibition ELISA. ![]() ![]() The IgG antibodies could bind, however, if GTP was presented more spaciously on larger particles or as a univalent hapten. The results were replicated in cell-free direct binding assays using small latex microspheres decorated densely with GTP. Serendipitously, however, we found a paradox: While murine IgM antibodies specific for guanosine triphosphate (GTP) were able to recognize native guanylyl antigens found in primate or rat muscle tissues by immunofluorescence assays (which mimicked the auto-antibodies from autoimmune patients to skeletal or smooth muscle), the murine and human IgG counterparts failed. IgM is the primordial member and the neglected sibling of the later-evolved and more proficient IgG in regard to their therapeutic and diagnostic use. 1Clinical Immunology Unit, The Chinese University of Hong Kong, Hong Kong, ChinaĪntibodies are well-known protein mediators of immunity.Eric Chun Yiu Law 1†‡ Danny Tze Ming Leung 1†‡ Frankie Chi Hang Tam 1,2 ‡ Kitty Kit Ting Cheung 1 † Naomi Hua Yin Cheng 1 † Pak Leong Lim 1,2 * ![]()
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