Background: The objective of the study was to evaluate the diagnostic accuracy of recently developed antiglycan serological tests in clinical practice for the diagnosis of Crohn's disease.
Methods: This study was a cohort analysis of both clinical and biochemical parameters of patients with diagnosed inflammatory bowel disease compared with those in a control population. Antiglycan antibodies were determined using commercially available enzyme immunoassays. The setting was the outpatient unit of the gastroenterology department of a large, tertiary-care referral academic hospital. Participants were 214 consecutive patients, enrolled over a 5-month period, including 116 with Crohn's disease and 53 with ulcerative colitis, as well as 45 with other gastrointestinal diseases and 51 healthy controls.
Results: Anti-Saccharomyces cerevisiae antibodies showed the best performance (54% sensitivity and 88%-95% specificity for Crohn's disease). Among patients with negative anti-Saccharomyces antibodies, 19 (34%) had high titers of at least another tested antiglycan antibody. Anti-Saccharomyces and anti-laminaribioside antibodies were associated with disease involving the small bowel and with penetrating or stricturing phenotype. Anti-laminaribioside was significantly higher in patients with a familial history of inflammatory bowel disease.
Conclusions: The new proposed serological markers are significantly associated with Crohn's disease, with low sensitivity but good specificity. About one third of anti-Saccharomyces-negative patients may be positive for at least 1 of those markers. Antiglycan antibodies appear to be associated with characteristic localization and phenotype of the disease.
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http://dx.doi.org/10.1002/ibd.20368 | DOI Listing |
Antibodies (Basel)
December 2024
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Science, 117991 Moscow, Russia.
Naturally occurring human antibodies against glycans recognize and quickly eliminate infectious bacteria, viruses and aberrantly glycosylated neoplastic malignant cells, and they often initiate processes that involve the complement system. Using a printed glycan array (PGA) containing 605 glycoligands (oligo- and polysaccharides, glycopeptides), we examined which of the glycan-binding antibodies are able to activate the complement system. Using this PGA, the specificities of antibodies of the IgM and IgG classes were determined in the blood serum of healthy donors (suggested as mostly natural), and, then, using the same array, it was determined which types of the bound immunoglobulins were also showing C3 deposition.
View Article and Find Full Text PDFAnal Chem
January 2025
School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450001, China.
Fibroblast activation protein (FAP) is an important antigen in the tumor microenvironment, which plays a crucial role in promoting extracellular matrix remodeling and tumor cell metastasis. A circulating form of soluble FAP has also been identified in the serum, becoming a biomarker for pan-cancer diagnosis and prognosis. However, the current peptide substrate-based enzymatic activity detection or antibody-dependent detection methods have been hindered by insufficient selectivity and complex operations, so it is valuable to develop effective nucleic acid aptamers as FAP affinity ligands.
View Article and Find Full Text PDFbioRxiv
October 2024
Department of Microbiology, University of Alabama at Birmingham Heersink School of Medicine, Birmingham AL 35294, USA.
The human antibody repertoire is broadly reactive with carbohydrate antigens represented in the universe of all living things, including both the host/self- as well as the commensal microflora-derived glycomes. Here we have used BCR receptor cloning and expression together with single-cell transcriptomics to analyze the B cell repertoire to the ubiquitous N-acetyl-D-glucosamine (GlcNAc) epitope in human cohorts and dissect the immune phylogeny of this predominant class of antibodies. We find that circulating anti-GlcNAc B cells exhibiting canonical BMem phenotypes emerge rapidly after birth and couple this observation with evidence for germinal center-dependent affinity maturation of carbohydrate-specific B cell receptors during early childhood.
View Article and Find Full Text PDFTetrahedron
September 2024
Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA.
We developed a method for making immune responses to bacterial glycans T cell-dependent, which involves attachment of short, synthetic glycans to a virus-like nanoparticle (VLP). This strategy enhances immune responses to glycans by facilitating cognate T cell help of B cells, leading to antibody class switching and affinity maturation yielding high-affinity, anti-glycan antibodies. This method requires synthesis of bacterial glycans as propargyl glycosides for covalent attachment to VLPs, and the resulting short linker between the VLP and glycan is important for optimal T cell receptor recognition.
View Article and Find Full Text PDFFront Immunol
August 2024
Department of Pathology, Sidney Kimmel Medical College at Thomas Jefferson University, Philadelphia, PA, United States.
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