Ask about this productRelated genes to: IRTA2 antibody
- Gene:
- FCRL5 NIH gene
- Name:
- Fc receptor like 5
- Previous symbol:
- -
- Synonyms:
- FCRH5, IRTA2, BXMAS1, CD307e
- Chromosome:
- 1q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-03-22
- Date modifiied:
- 2016-10-05
Related products to: IRTA2 antibody
Related articles to: IRTA2 antibody
- The heterogeneity of memory B cells in response to repetitive cognate antigen challenges remains to be fully elucidated. Here, we identified a transcriptionally distinct cluster of T-bet B cells, among SARS-CoV-2 RBD-specific B cells in PBMCs from healthy individuals vaccinated with the BNT162b2 SARS-CoV-2 mRNA vaccine. Our findings indicate that T-bet B cells can be defined by a combination of CD11c and FcRL5 receptors, and are distinguished by distinct gene regulatory networks associated with effector functions. Notably, these T-bet B cells were affinity-matured and exhibited rapid differentiation into antibody-secreting cells (ASCs) producing neutralizing antibodies comparable to classical memory B cells, underscoring their role in early recall responses. Taken together, these findings illuminate the potent effector memory roles of T-bet B cells in adaptive immunity following vaccinations. - Source: PubMed
Publication date: 2026/01/27
Lee JeongsooSon SeunghwanChung YouseungCho Sung-DongKwon Ji-SooBae SeongmanSeok JoonChoi BaekgyuJung InkyungOh Ji EunShin Eui-CheolKim Sung-HanPark Su-Hyung - Fc receptor-like (FCRL) proteins constitute a receptor family that displays overlapping yet distinct features compared to classical Fc receptors. In a healthy immune system, FCRL proteins play a role in promoting and regulating the immune response through their immunoreceptor tyrosine-based motifs. FCRL proteins are expressed mainly by B cells, suggesting a primary role in B-cell responses. For several autoimmune diseases, studies have shown that particularly FCRL4, which binds to dimeric IgA, and FCRL5, which binds to IgG, may have a role in disease pathology and prognosis. These proteins and their transcripts are often enriched in blood and/or affected tissue of patients with a systemic or organ-specific autoimmune disease like rheumatoid arthritis, Sjögren's disease, systemic lupus erythematous, Graves' disease or myasthenia gravis. The expression of FCRL4 and FCRL5 appears to be disease- and context-specific, and influenced by the tissue microenvironment. Yet, the functions of FCRL proteins are still incompletely understood, and more mechanistic studies are necessary to unravel the contribution of FCRL4 and FCRL5 to pathogenic B-cell responses occurring in autoimmune diseases. - Source: PubMed
Publication date: 2026/01/28
Haroun ChristinaKroese Frans G MVerstappen Gwenny M - Designing proteins that bind with high affinity to hydrophilic protein target sites remains a challenging problem. Here we show that RFdiffusion can be conditioned to generate protein scaffolds that form geometrically matched extended β-sheets with target protein edge β-strands in which polar groups on the target are complemented with hydrogen bonding groups on the design. We use this approach to design binders against edge-strand target sites on KIT, PDGFRɑ, ALK-2, ALK-3, FCRL5, NRP1, and α-CTX, and obtain higher (pM to mid nM) affinities and success rates than unconditioned RFdiffusion. Despite sharing β-strand interactions, designs have high specificity, reflecting the precise customization of interacting β-strand geometry and additional designed binder-target interactions. A binder-KIT co-crystal structure is nearly identical to the design model, confirming the accuracy of the design approach. The ability to robustly generate binders to the hydrophilic interaction surfaces of exposed β-strands considerably increases the range of computational binder design. - Source: PubMed
Publication date: 2026/01/10
Sappington IsaacToul MartinLee David SRobinson Stephanie AGoreshnik InnaMcCurdy ClaraChan Tung ChingBuchholz NicHuang BuweiVafeados DionneGarcia-Sanchez MarianaRoullier NicoleGlögl MatthiasKim Christopher JWatson Joseph LTorres Susana VázquezVerschueren Koen H GVerstraete KennethHinck Cynthia SBenard-Valle MelisaCoventry BrianSims Jeremiah NelsonAhn GreenWang XinruHinck Andrew PJenkins Timothy PRuohola-Baker HanneleBanik Steven MSavvides Savvas NBaker David - Myasthenia gravis (MG) is an autoimmune disorder characterized by B cell dysfunction. Here, we designed B cell maturation antigen (BCMA)/CD19 chimeric antigen receptor T cell (CAR T cell) therapy for six refractory MGs, demonstrating favorable safety with grade 1 cytokine release syndrome observed. CAR T cell expansion induced profound B cell depletion, a sustained reduction in acetylcholine receptor (AChR) antibody titers, and symptom improvement. Five patients achieved drug-free remission with minimal manifestations by month 6, persisting through the 12-month follow-up despite B cell reconstitution. Reconstituted B cells showed naïve predominance with diminished AChR specificity and functional capacities. Olink proteomics revealed up-regulation of anti-inflammatory factors, along with down-regulation of proinflammatory molecules. Single-cell sequencing revealed that age-associated B cells (ABCs) were up-regulated in a relapsed patient, and differential gene analysis indicated that Fc receptor-like 5 (FCRL5) expression was elevated in ABCs, whereas CAR T cell responders exhibited a down-regulated trend. Notably, similar ABC expansion and FCRL5 up-regulation occurred in rituximab-relapsed patients. Our findings support BCMA/CD19 CAR T cell therapy as feasible, tolerable, and effective in MG, identifying FCRL5 as a previously unidentified target in relapse. - Source: PubMed
Publication date: 2026/01/02
Huang XiaoyuZhang ZhouaoLiu DanLuo TianchengAn XuetingYang MingjinLi ShengliWang GangLi HuizhongCao JiangSun ZengtianDu XueWang ZhouyiGuo XinyanMa TianyuPeng DeyouQi GuoyanZong ShenghuaDing YantingCui GuiyunShi MingZheng JunnianZhang Yong - The Fc receptors play crucial roles in initiating the effector functions of immunoglobulins. FcRL5 is a prominent target in B cell malignancies and has been implicated as a receptor for immunoglobulin G (IgG). However, the molecular mechanism remained unclear. Here, we demonstrate that human FcRL5, but not its mouse counterpart, is a bona fide IgG-Fc (Fcγ) receptor that uniquely requires the presence of two Fcγ molecules in close proximity to form a robust interaction. Cryo-electron microscopy reveals that FcRL5 optimally engages two Fcγ molecules positioned at a 60° angle, with its D1-D2 domains binding to the first Fcγ molecule, while its D3 domain arches over the second Fcγ. This distinctive binding capability enables FcRL5 to specifically recognize IgG immune complexes (ICs), with the binding strength correlating with IgG concentration in the ICs. In addition, we demonstrate that FcRL5 can internalize the IgG polymer and IC. These results shed light on FcRL5 function and reveal a unique Fcγ-FcγR binding mode governed by avidity. - Source: PubMed
Publication date: 2026/01/01
Chen ShihuaLi ShuhanZhang ZhiyingXiao Junyu