Altered IgG N-Glycosylation at Onset of Type 1 Diabetes in Children Is Predominantly Driven by Changes in the Fab N-Glycans [PDF]
BiomedicinesBackground: N-glycosylation is a post-translational modification involving the attachment of oligosaccharides to proteins and is known to influence immunoglobulin G (IgG) effector functions and even antigen binding.
Branimir Plavša +3 more
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Biochemical and structural characterization of the human gut microbiome metallopeptidase IgAse provides insight into its unique specificity for the Fab' region of IgA1 and IgA2. [PDF]
PLoS PathogensHuman immunoglobulin A (IgA), comprising the isotypes IgA1 and IgA2, protects ~400 m2 of mucosal surfaces against microbial infections but can also lead to aberrant IgA deposits that cause disease. Certain bacteria have evolved peptidases that cleave the
Juan Sebastián Ramírez-Larrota +4 more
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Allosteric inhibition of IgE–FcεRI interactions by simultaneous targeting of IgE F(ab’)2 epitopes [PDF]
Communications BiologyImmunoglobulin E (IgE) plays pivotal roles in allergic diseases through interaction with a high-affinity receptor (FcεRI). We established that Fab fragments of anti-IgE antibodies (HMK-12 Fab) rapidly dissociate preformed IgE-FcεRI complexes in a ...
Takao Hirano +6 more
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Effect of IgG fragments in IVIG(pH4)on phagocytosis of sensitized erythrocytes by macrophage
Zhongguo shuxue zazhi, 2022 Objective To research the effect of the Fc, Fab and F(ab′)2 fragments of immunoglobulin G, the main components of Human Immunoglobulin(pH4) for Intravenous Injection(IVIG), on the phagocytic function of macrophages derived from THP-1 cells. Methods First
Liyuan ZHU +6 more
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The Fab region of IgG impairs the internalization pathway of FcRn upon Fc engagement
Nature Communications, 2022 Disrupting the association between the Immunoglobulin G constant fragment (Fc) and the neonatal Fc receptor (FcRn) by engineered antibodies is a promising strategy to reduce autoantibody levels in autoimmune diseases.
Maximilian Brinkhaus +13 more
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Scientific Reports, 2023 With increased accessibility and tissue penetration, smaller antibody formats such as antibody fragments (Fab) and single chain variable fragments (scFv) show potential as effective and low-cost choices to full-length antibodies.
Aatir A. Tungekar, Lloyd W. Ruddock
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Direct IgG epitope mapping on bacterial AB toxins by cryo-EM
STAR Protocols, 2021 Summary: This cryo-EM protocol was used to determine the B cell epitope map on the CdtB subunit of typhoid toxin, an A2B5 toxin secreted by Salmonella Typhi during infection.
Tri Nguyen, Jeongmin Song
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EJNMMI Research, 2023 Background Following resection and standard adjuvant radio- and chemotherapy, approved maintenance therapies for glioblastoma are lacking. Intracavitary radioimmunotherapy (iRIT) with 177Lu-labeled 6A10-Fab fragments targeting tumor-associated carbonic ...
Wolfgang Roll +10 more
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Structure of an immunoglobulin Fab fragment specific for triple-stranded DNA. [PDF]
Journal of Biological Chemistry, 1994 Triple-stranded DNA of the form poly(Pyr).poly-(Pur).poly(Pyr) (where Pyr represents a pyrimidine, and Pur represents a purine) has become the subject of intense research because of its potential use in the control of gene expression and in the development of sequence-specific reagents for cleaving DNA.
Mol, Clifford D. +4 more
openaire +3 more sources
A Fab-Selective Immunoglobulin-Binding Domain from Streptococcal Protein G with Improved Half-Life Extension Properties. [PDF]
PLoS ONE, 2015 Half-life extension strategies have gained increasing interest to improve the pharmacokinetic and pharmacodynamic properties of protein therapeutics. Recently, we established an immunoglobulin-binding domain (IgBD) from streptococcal protein G (SpGC3) as
Felix Unverdorben +3 more
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