Ask about this productRelated genes to: FCGRT Blocking Peptide
- Gene:
- FCGRT NIH gene
- Name:
- Fc fragment of IgG receptor and transporter
- Previous symbol:
- -
- Synonyms:
- FCRN, alpha-chain
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 1995-08-23
- Date modifiied:
- 2016-10-05
Related products to: FCGRT Blocking Peptide
Related articles to: FCGRT Blocking Peptide
- Broadly neutralising antibodies (bNAbs) represent a promising long-acting modality for HIV prevention. However, substantial interindividual pharmacokinetic variability poses a threat to real-world efficacy. This review investigates the impact of systemic inflammation, driven by the high prevalence of sexually transmitted infections (STIs), co-endemic pathogens, and metabolic activation, on bNAb persistence, particularly within the vulnerable demographic of women in sub-Saharan Africa. We aim to bridge the gap between neonatal fragment crystallisable receptor (FcRn) biology and clinical pharmacokinetic observations to identify why certain individuals clear bNAbs faster than others. - Source: PubMed
Publication date: 2026/07/10
Khumalo AndilePillay SanjaliMohan JivankaMahomed SharanaArchary Derseree - Elucidating the quaternary structures of protein complexes under physiological conditions remains a central challenge for structural biology. Here, we introduce an integrative analytical pipeline that combines size exclusion chromatography (SEC), Taylor dispersion analysis (TDA), native mass spectrometry (nMS), and artificial intelligence to resolve macromolecular architectures under near-native solution conditions. The workflow begins with the SEC-based separation of heterogeneous mixtures, followed by online TDA in a PEEK capillary to probe hydrodynamic behavior via laminar-flow-induced dispersion. By deconvolving pre- and postdispersion chromatograms, a system transfer function is derived and subjected to Gaussian fitting to yield precise measurements of hydrodynamic radii. These experimentally derived radii are subsequently applied as biophysical constraints in an AlphaFold 3-based structural selection process. We validated this method using a six-protein model mixture, demonstrating its ability to simultaneously determine the hydrodynamic radii of individual components within complex mixtures. The methodology was further applied to three protein complexes (FCGRT-B2M, streptavidin, and concanavalin A), allowing for the precise measurement of their oligomeric hydrodynamic radii and the determination of their quaternary structures. By bridging high-resolution analytical chemistry with AI-driven structural prediction, this strategy offers a robust experimentally grounded framework for characterizing macromolecular assemblies. - Source: PubMed
Publication date: 2026/06/18
Zhang WenjingMa RonghuiJiang TingXu Wei - - Source: PubMed
Publication date: 2026/06/08
Ala Abdul SametLo BerniceOzen AhmetIslek AliTumgor Gokhan - Understanding the geographical differentiation of black tea is essential for exploring the influence of territory on its chemical composition. In this study, black tea (powder) samples from key tea-producing regions, including Siliguri, Assam, and Idukki (Kerala) in India, Sylhet in Bangladesh, and Kandy in Sri Lanka, were analyzed using ultra-high-performance liquid chromatography coupled with high-resolution mass spectrometry. The tea extracts were analysed in full MS/ddMS mode with heated electrospray ionization, using a non-targeted metabolomics approach. A broad range of compounds (209) including polyphenols, amino acids, organic acids and their derivatives were identified based on accurate mass measurements with mass error (±5 ppm) and retention time matching (±0.2 min). Various metabolite profiles were observed across different regional samples, with certain marker compounds identified as potential indicators of geographical origin. Principal component analysis (PCA) further confirmed clear clustering and differentiation of tea samples based on the origin, highlighting the role of regional environmental factors such as climate, soil composition, and altitude. Molecular docking and dynamics were carried out to examine the interaction of theanine and the neonatal Fc receptor (FcRn), a key regulator of IgG recycling and immune homeostasis, encoded by the FCGRT gene. Results showed that theanine forms a stable complex with the neonatal Fc receptor (FcRn) and maintained consistent hydrogen bonding, particularly with key residue Ile685, and preserved FcRn's secondary structure. Binding energy analysis (MM-PBSA) showed favourable interactions dominated by van der Waals forces, with theanine exhibiting a slightly higher binding affinity (-18.72 kcal mol) than RVT-1401 (-17.82 kcal mol), a therapeutic monoclonal antibody known to inhibit FcRn function. The findings have significant implications for the tea industry in quality control, authentication, traceability, and health benefits, which offer new insights into how territory shapes the chemical and potentially sensory attributes of black tea. - Source: PubMed
Publication date: 2026/05/21
Budakoti Subodh KumarAnwar KhalidKumar Nagendla NarendraBhat M L AnirudhOulkar DasharathSharma Pratibha - The neonatal fc receptor (FcRn) is indispensable in sustaining IgG homeostasis. Recently, the potential role of FcRn in infectious diseases has attracted more attention. However, the function of FcRn in tuberculosis is unclear. The present study aimed to investigate the role of FcRn in regulating BCG infection-induced autophagy in vitro and vivo. FCGRT knockout mice and FcRn knockdown cells were constructed by CRISPR/Cas9 and small interfering RNA. The related indicators of autophagy were detected by transmission electron microscopy, flow cytometry, and western blot. The proteins interacting with FcRn were screened by immunoprecipitation (IP) and mass spectrometry (MS). The results showed more lung injury and less autophagy marker expression in the KO-FcRn mice lungs than wild type (WT) mice after BCG infection (p < 0.01). Meanwhile, si-FcRn restrained BCG-induced macrophage autophagy by activating the PI3K/AKT/m-TOR pathway. Furthermore, FcRn was confirmed to interact with the Y-box binding protein 1 (YBX1) and promote its nuclear translocation. Hence, the current study proved that FcRn protects against BCG-induced lung injury by triggering YBX1-mediated autophagy and suppressing the PI3K /AKT/mTOR signaling pathway. These findings present a novel understanding of the immune role of FcRn in treating and preventing tuberculosis. - Source: PubMed
Publication date: 2026/02/02
Xu YananGong ZhaoqianYu JialinZhang JiameiDeng GuangcunWu Xiaoling