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• W4220842478 endingPage "2090" @default.
• W4220842478 startingPage "2090" @default.
• W4220842478 abstract "Immunoglobulin G (IgG) adopts a modular multidomain structure that mediates antigen recognition and effector functions, such as complement-dependent cytotoxicity. IgG molecules are self-assembled into a hexameric ring on antigen-containing membranes, recruiting the complement component C1q. In order to provide deeper insights into the initial step of the complement pathway, we report a high-speed atomic force microscopy study for the quantitative visualization of the interaction between mouse IgG and the C1 complex composed of C1q, C1r, and C1s. The results showed that the C1q in the C1 complex is restricted regarding internal motion, and that it has a stronger binding affinity for on-membrane IgG2b assemblages than C1q alone, presumably because of the lower conformational entropy loss upon binding. Furthermore, we visualized a 1:1 stoichiometric interaction between C1/C1q and an IgG2a variant that lacks the entire CH1 domain in the absence of an antigen. In addition to the canonical C1q-binding site on Fc, their interactions are mediated through a secondary site on the CL domain that is cryptic in the presence of the CH1 domain. Our findings offer clues for novel-modality therapeutic antibodies." @default.
• W4220842478 created "2022-04-03" @default.
• W4220842478 creator A5006059987 @default.
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• W4220842478 date "2022-02-14" @default.
• W4220842478 modified "2023-10-14" @default.
• W4220842478 title "Quantitative Visualization of the Interaction between Complement Component C1 and Immunoglobulin G: The Effect of CH1 Domain Deletion" @default.
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• W4220842478 doi "https://doi.org/10.3390/ijms23042090" @default.
• W4220842478 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35216207" @default.
• W4220842478 hasPublicationYear "2022" @default.
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