Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

Ag recognition and Ab production in B cells are major components of the humoral immune response. In the current study, we found that the core fucosylation catalyzed by α1,6-fucosyltransferase (Fut8) was required for the Ag recognition of BCR and the subsequent signal transduction. Moreover, compared with the 3-83 B cells, the coalescing of lipid rafts and Ag-BCR endocytosis were substantially reduced in Fut8-knockdown (3-83-KD) cells with p31 stimulation and then completely restored by reintroduction of the Fut8 gene to the 3-83-KD cells. Indeed, Fut8-null (Fut8(-/-)) mice evoked a low immune response following OVA immunization. Also, the frequency of IgG-producing cells was significantly reduced in the Fut8(-/-) spleen following OVA immunization. Our results clearly suggest an unexpected mode of BCR function, in which the core fucosylation of IgG-BCR mediates Ag recognition and, concomitantly, cell signal transduction via BCR and Ab production.

Download full-text PDF

Source
http://dx.doi.org/10.4049/jimmunol.1402678DOI Listing

Publication Analysis

Top Keywords

core fucosylation
12
immune response
8
signal transduction
8
3-83-kd cells
8
ova immunization
8
cells
5
fucosylation igg
4
igg cell
4
cell receptor
4
receptor required
4

Similar Publications

Gut mucin fucosylation dictates the entry of botulinum toxin complexes.

bioRxiv

August 2025

Department of Bacteriology, Graduate School of Medical Sciences, Kanazawa University, Ishikawa 920-8640, Japan.

Botulinum toxins (BoNTs) are the most potent known bacterial toxins. The BoNT complex from B-Okra (large progenitor toxin complex (L-PTC)/B, hyper-oral-toxic) exerts at least 80-fold higher oral toxicity in mice compared with that from serotype A1 (L-PTC/A, non-hyper-oral-toxic). Here, we showed that L-PTC/B was predominantly absorbed through enterocytes, whereas L-PTC/A targeted intestinal microfold cells.

View Article and Find Full Text PDF

Bisected and core-fucosylated N-glycans represent a distinct class of complex biomolecules that are implicated in diverse biological and pathological processes. The structural complexity and synthetic challenges of these glycans hinder comprehensive understanding of their biological functions due to limited access to well-defined samples. Despite advances in the complex N-glycan synthesis, the efficient preparation of bisected and core-fucosylated asymmetric N-glycans with various branches and terminal epitopes remains an unmet challenge.

View Article and Find Full Text PDF

Background: It is well established that the cancerous transformation of cells is accompanied by profound alterations in glycosylation. In this study, we demonstrate the diagnostic potential of N-glycan profiling in tissue specimens from patients, primarily representing the two major types of lung cancer: non-small cell and small cell lung cancer.

Methods: Lung tissues and biopsies obtained from surgery and bronchoscopy underwent sample processing and enzymatic digestion.

View Article and Find Full Text PDF

Core-fucosylated glycoproteins as biomarkers for diagnosing pancreatic ductal adenocarcinoma.

Int J Biol Macromol

September 2025

State Key Laboratory of Medical Proteomics, National Center for Protein Sciences (Beijing), Academy of Military Medical Sciences, Beijing 102206, China. Electronic address:

Pancreatic ductal adenocarcinoma (PDAC) is highly malignant, with a five-year survival rate of only 12 %. Exact diagnosis and intervention are critical for improving patient prognosis. Core fucosylation (CF) of proteins plays a vital role in the progression of various cancers, including PDAC.

View Article and Find Full Text PDF