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Evolution of SARS-CoV-2 spike trimers towards optimized heparan sulfate cross-linking and inter-chain mobility.
Sci Rep
December 2024
Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Waldeyerstrasse 15, D-48149, Münster, Germany.
The heparan sulfate (HS)-rich extracellular matrix (ECM) serves as an initial interaction site for the homotrimeric spike (S) protein of SARS-CoV-2 to facilitate subsequent docking to angiotensin-converting enzyme 2 (ACE2) receptors and cellular infection. More recent variants, notably Omicron, have evolved by swapping several amino acids to positively charged residues to enhance the interaction of the S-protein trimer with the negatively charged HS. However, these enhanced interactions may reduce Omicron's ability to move through the HS-rich ECM to effectively find ACE2 receptors and infect cells, raising the question of how to mechanistically explain HS-associated viral movement.
View Article and Find Full Text PDFThe diagnostic and prognostic value of heparin-binding protein in cerebrospinal fluid for patients with intracranial infections.
Eur J Med Res
December 2024
Department of Clinical Laboratory, The First Affiliated Hospital, Jiangxi Medical College, Nanchang University, 17 Yongwai Zhengjie, Nanchang, 330006, Jiangxi, China.
Background: This study aims to evaluate the diagnostic and prognostic value of heparin-binding protein (HBP) in cerebrospinal fluid (CSF) for patients with intracranial infections.
Methods: This study included 211 subjects, of whom 138 were diagnosed with intracranial infections, 20 were patients with non-infectious inflammatory encephalopathies, and 53 controls who were eventually excluded from intracranial infections and inflammatory encephalopathies. The levels of HBP and procalcitonin (PCT) in CSF were detected in the subjects, and the diagnostic value of CSF HBP and PCT for intracranial infections was assessed using the receiver operating characteristic (ROC) curves.
Single-cell RNA sequencing identifies endothelial-derived HBEGF as promoting pancreatic beta cell proliferation in mice via the EGFR-Kmt5a-H4K20me pathway.
Diabetologia
December 2024
Department of Cardiology, Jinan Central Hospital Affiliated to Shandong First Medical University, Jinan, China.
Aims/hypothesis: Pancreatic beta cell mass is dynamically regulated in response to increased physiological and pathological demands. Understanding the mechanisms that control physiological beta cell proliferation could provide valuable insights into novel therapeutic approaches to diabetes. Here, we aimed to analyse the intracellular and extracellular signalling pathways involved in regulating the physiological proliferation of beta cells using single-cell RNA-seq (scRNA-seq) and in vitro functional assays.
View Article and Find Full Text PDFElucidating the Mechanism of Recognition and Binding of Heparin to Amyloid Fibrils of Serum Amyloid A.
Biochemistry
January 2025
Department of Chemistry, Boston University, Boston, Massachusetts 02215, United States.
Amyloid diseases feature pathologic deposition of normally soluble proteins and peptides as insoluble fibrils in vital organs. Amyloid fibrils co-deposit with various nonfibrillar components including heparan sulfate (HS), a glycosaminoglycan that promotes amyloid formation in vitro for many unrelated proteins. HS-amyloid interactions have been proposed as a therapeutic target for inflammation-linked amyloidosis wherein N-terminal fragments of serum amyloid A (SAA) protein deposit in the kidney and liver.
View Article and Find Full Text PDFInteraction between the Polyelectrolytes Unfractionated Heparin and Universal Heparin Reversal Agents.
J Phys Chem B
December 2024
Institut für Chemie und Biochemie, Freie Universität Berlin, Berlin 14195, Germany.
The interaction of unfractionated heparin (UFH) with universal heparin reversal agent 7 (UHRA-7) is investigated. UHRA-7 is composed of a hyperbranched polyglycerol core onto which an array of methylated tris(2-aminoethylamine) (Me-TREN) charged groups is grafted, which in turn are shielded with a layer of small chain poly(ethylene glycol) methyl ether (mPEG) chains. This system has previously been shown to be biocompatible and to be effective at neutralizing heparin.
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