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Structural basis of malaria RIFIN binding by LILRB1-containing antibodies.
Nature
April 2021
Institute for Research in Biomedicine, Università della Svizzera italiana, Bellinzona, Switzerland.
Some Plasmodium falciparum repetitive interspersed families of polypeptides (RIFINs)-variant surface antigens that are expressed on infected erythrocytes-bind to the inhibitory receptor LAIR1, and insertion of DNA that encodes LAIR1 into immunoglobulin genes generates RIFIN-specific antibodies. Here we address the general relevance of this finding by searching for antibodies that incorporate LILRB1, another inhibitory receptor that binds to β2 microglobulin and RIFINs through their apical domains. By screening plasma from a cohort of donors from Mali, we identified individuals with LILRB1-containing antibodies.
View Article and Find Full Text PDFStructure of a human IgA1 Fab fragment at 1.55 Å resolution: potential effect of the constant domains on antigen-affinity modulation.
Acta Crystallogr D Biol Crystallogr
March 2013
Unit of Recombinant Proteins, Institut Pasteur de Montevideo, 11400 Montevideo, Uruguay.
Despite being the most abundant class of immunoglobulins in humans and playing central roles in the adaptive immune response, high-resolution structural data are still lacking for the antigen-binding region of human isotype A antibodies (IgAs). The crystal structures of a human Fab fragment of IgA1 in three different crystal forms are now reported. The three-dimensional organization is similar to those of other Fab classes, but FabA1 seems to be more rigid, being constrained by a hydrophobic core in the interface between the variable and constant domains of the heavy chain (VH-CH1) as well as by a disulfide bridge that connects the light and heavy chains, influencing the relative heavy/light-chain orientation.
View Article and Find Full Text PDFHeat-induced structural changes in the Fab fragment of IgG recognized by molecular dynamics stimulation--implications for signal transduction in antibodies.
Folia Biol (Krakow)
September 1995
Department of Medical Informatics, Collegium Medicum, Jagiellonian University, Kraków, Poland.
Molecular dynamics simulation was used to identify the conformational alterations in the Fab fragment (Kol), driven by heating at 300, 320, and 340 K. Comparison of heat-modified VH,CH1 and VL,CL domain structures with the corresponding crystal conformations revealed specific differences, most definitely expressed in the CH1 domain. These are dislocations of predominantly peripheral peptide loops exposed to the V-C interdomain interface, comprising in particular the 175-185 amino acids of the heavy chain, as well as the 112-123 amino acids of the interdomain hinge fragment.
View Article and Find Full Text PDFImmune complexes composed of rabbit IgG and Fab fragments of antibody specific for the VH framework allotypes were analyzed by molecular immunoelectron microscopy. In this manner, the number of allotypic epitopes ( allotopes ) and their approximate topological location could be determined. A monoclonal anti-allotype Fab was used to show that relatively fine details of allotope location and orientation are demonstrable with this technique.
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