Background: Despite treatment with effective antimalarial drugs, the mortality rate is still high in severe cases of the disease, highlighting the need to find adjunct therapies that can inhibit the adhesion of Plasmodium falciparum-infected erythrocytes (Pf-iEs).
Objectives: In this context, we evaluated a new heparan sulfate (HS) from Nodipecten nodosus for antimalarial activity and inhibition of P. falciparum cytoadhesion and rosetting.
Methods: Parasite inhibition was measured by SYBR green using a cytometer. HS was assessed in rosetting and cytoadhesion assays under static and flow conditions using Chinese hamster ovary (CHO) and human lymphatic endothelial cell (HLEC) cells expressing intercellular adhesion molecule-1 (ICAM1) and chondroitin sulfate A (CSA), respectively.
Findings: This HS inhibited merozoite invasion similar to heparin. Moreover, mollusk HS decreased cytoadherence of P. falciparum to CSA and ICAM-1 on the surface of endothelial cells under static and flow conditions. In addition, this glycan efficiently disrupted rosettes.
Conclusions: These findings support a potential use for mollusk HS as adjunct therapy for severe malaria.
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http://dx.doi.org/10.1590/0074-02760190088 | DOI Listing |
Hypertension
January 2025
Division of Obstetrics and Gynecology, Institute of Clinical Sciences Lund, Lund University, Sweden. (C.E., F.P., L.E., S.R.H.).
Background: Preeclampsia is a hypertensive pregnancy disorder marked by endothelial damage. Healthy endothelium is covered by a protective glycocalyx layer, which, when degraded, releases detectable products into the blood. Sphingosine-1-phosphate (S1P) is a cardiovascular biomarker involved in glycocalyx preservation, linked to placentation and preeclampsia development.
View Article and Find Full Text PDFMacromol Biosci
January 2025
Heinrich- Heine- University Düsseldorf, Faculty of Mathematics and Natural Sciences, Institute of Organic Chemistry and Macromolecular Chemistry, 40204, Düsseldorf, Germany.
Glycosaminoglycans (GAGs) play a pivotal role in pathogen attachment and entry into host cells, where the interaction with GAGs is critical for a diverse range of bacteria and viruses. This study focuses on elucidating the specific interactions between sulfated GAGs and the adhesin OmcB (Outer membrane complex protein B) of Chlamydia species, examining how structural characteristics of GAGs, such as sulfation degree and molecular weight, influence their binding affinity and thereby affect bacterial infectivity. A surface-based binding assay is established to determine the binding constants of OmcB with various GAGs.
View Article and Find Full Text PDFChemistry
January 2025
Indian Institute of Science Education and Research Bhopal, Department of Biological Sciences, INDIA.
Voltage-gated ion channels (VGICs) are allosterically modulated by glycosaminoglycan proteoglycans and sialic acid glycans. However, the structural diversity and heterogeneity of these biomolecules pose significant challenges to precisely delineate their underlying structure-activity relationships. Herein, we demonstrate how heparan sulfate (HS) and sialic acid synthetic glycans appended on amphiphilic glycopeptide backbone influence cell membrane persistence and modulate the gating of the Kv2.
View Article and Find Full Text PDFJ Trop Med
January 2025
National Institute of Parasitic Diseases, Chinese Center for Disease Control and Prevention (Chinese Center for Tropical Diseases Research), Laboratory of Parasite and Vector Biology, Ministry of Public Health, WHO Collaborating Centre for Tropical Diseases, National Center for International Research on Tropical Diseases, Ministry of Science and Technology, Shanghai 200025, China.
Glycosaminoglycan (GAG) molecules on the surface of red blood cells play an important regulatory role in the invasion of merozoites of apicomplexan protozoa. Heparan sulfate, a type of GAG molecule, has been identified as an important receptor facilitating the invasion of red blood cells by these parasites. Proteins in the parasite that exhibit strong affinity for heparin may play a pivotal role in this invasion process.
View Article and Find Full Text PDFAnalyst
January 2025
Key Laboratory of Phytochemistry and Natural Medicines, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, P. R. China.
Although the glycosylation of viral proteins plays a critical role in the process of viral invasion into host cells, studies on the glycosylation of monkeypox virus (MPXV) structural proteins have not yet been reported. To investigate the importance of MPXV protein glycosylation, poly Ser-Arg (poly SR) materials capable of simultaneously enriching both -glycopeptides and -glycopeptides were synthesized by surface-initiated reversible addition-fragmentation chain transfer (SI-RAFT) polymerization. The poly SR materials were evaluated using the digest mixture of standard proteins containing bovine fetuin and bovine serum albumin, and the digest of complex biological samples including bovine sperm tail lysate, mouse sperm tail lysate, mouse brain lysate, and human serum.
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