ArticleGlycoconjugate journal2006
Carbohydrate ligands of human C-reactive protein: binding of neoglycoproteins containing galactose-6-phosphate and galactose-terminated disaccharide.
Article in Glycoconjugate journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Evaluating the CRP Interactome: Insights into Possible Novel Roles in Cellular Signaling and Tumorigenicity.Current issues in molecular biology · 2025Review
- C-Reactive Protein: Pathophysiology, Diagnosis, False Test Results and a Novel Diagnostic Algorithm for Clinicians.Diseases (Basel, Switzerland) · 2023Review
- Human Lectins, Their Carbohydrate Affinities and Where to Find Them.Biomolecules · 2021Review
- The plasma level of mCRP is linked to cardiovascular disease in antineutrophil cytoplasmic antibody-associated vasculitis.Arthritis research & therapy · 2020Article
- Structure-Function Relationships of C-Reactive Protein in Bacterial Infection.Frontiers in immunology · 2019Review
- C-reactive protein enhances activation of coagulation system and inflammatory response through dissociating into monomeric form in antineutrophil cytoplasmic antibody-associated vasculitis.BMC immunology · 2015Article
- An epidemiological analysis of potential associations between C-reactive protein, inflammation, and prostate cancer in the male US population using the 2009-2010 National Health and Nutrition Examination Survey (NHANES) data.Frontiers in chemistry · 2015Article
- The protective function of human C-reactive protein in mouse models of Streptococcus pneumoniae infection.Endocrine, metabolic & immune disorders drug targets · 2008Review
- The connection between C-reactive protein and atherosclerosis.Annals of medicine · 2008Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Binding of carbohydrate ligand by human C-reactive protein (CRP), in both native form and structurally deviated form (neoCRP or mCRP), was investigated using galactose-6-phosphate (Gal6P)- and Galbeta3GalNAc-containing bovine serum albumin (BSA) derivatives. To this end, we synthesized glycosides of Gal6P and Galbeta3GalNAc that can potentially generate a terminal aldehyde group. omega-Aldehydo glycosides were then conjugated to BSA via reductive amination. Using these neoglycoproteins, we showed that: (1) Gal6P-BSA and Galbeta3GalNAc-BSA bound to both forms of CRP, the former with or without calcium and the latter only in the absence of calcium; (2) phosphate-containing ligands can be bound with or without calcium, but the binding is much stronger in the presence of calcium than in the absence, underscoring the importance of direct coordination of phosphate to two calcium ions observed in the X-ray structure of phosphorylcholine (PC)-CRP complex; (3) cross-inhibition studies further corroborated the hypothesis that binding sites of PC and sugar are contiguous; (4) while PC-BSA bound to the native CRP over a wide pH range of 4.5 to 9, all the carbohydrate ligands and protamine-BSA (poly-cation-based ligand) exhibited optimal binding at around pH 6 to 6.5; and (5) ligand-binding conformation of mCRP appears to be more fragile than that of the native CRP in the acidic media (pH < 6).
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