ArticleGlycobiology2018
Streptococcal Siglec-like adhesins recognize different subsets of human plasma glycoproteins: implications for infective endocarditis.
Article in Glycobiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- The microenvironment dictates glyco-immune surveillance via HSF1-mediated metabolism.Science advances · 2026Article
- HIV-1 interactions with sialic acid-binding bacterial lectins promote virus infectivityFrontiers in cellular and infection microbiology · 2026Article
- Lectin Microarray-based Glycomics and Machine Learning Identify Shared Osteoarthritis Biomarkers in Humans, Dogs, and Horses.bioRxiv : the preprint server for biology · 2025Article
- Age-related remodeling of the sialoglycans dampens murine CD8Science advances · 2025Article
- Integrated in vivo functional screens and multiomics analyses identify α-2,3-sialylation as essential for melanoma maintenance.Science advances · 2025Article
- Understanding the Glycosylation Pathways Involved in the Biosynthesis of the Sulfated Glycan Ligands for Siglecs.ACS chemical biology · 2025Article
- Collagen Mineralization Decreases NK Cell-Mediated Cytotoxicity of Breast Cancer Cells via Increased Glycocalyx Thickness.Advanced materials (Deerfield Beach, Fla.) · 2024Article
- HIV-1 interaction with aniScience · 2024Article
- Molecular Insights into O-Linked Sialoglycans Recognition by the Siglec-Like SLBR-N (SLBRACS central science · 2024Article
- COLLAGEN MINERALIZATION DECREASES NK CELL-MEDIATED CYTOTOXICITY OF BREAST CANCER CELLS VIA INCREASED GLYCOCALYX THICKNESS.bioRxiv : the preprint server for biology · 2024Article
- The microenvironment dictates glycocalyx construction and immune surveillance.Research square · 2023Article
- Recombinant mucin biotechnology and engineering.Advanced drug delivery reviews · 2023Review
- Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.Nature communications · 2022Article
- How bacteria utilize sialic acid during interactions with the host: snip, snatch, dispatch, match and attach.Microbiology (Reading, England) · 2022Review
- O-linked α2,3 sialylation defines stem cell populations in breast cancer.Science advances · 2022Article
- Proteoglycan 4 (lubricin) is a highly sialylated glycoprotein associated with cardiac valve damage in animal models of infective endocarditis.Glycobiology · 2021Article
- Molecular recognition of sialoglycans by streptococcal Siglec-like adhesins: toward the shape of specific inhibitors.RSC chemical biology · 2021Article
- Age-Dependent Glycomic Response to the 2009 Pandemic H1N1 Influenza Virus and Its Association with Disease Severity.Journal of proteome research · 2020Article
- Tandem sialoglycan-binding modules in aThe Journal of biological chemistry · 2020Article
- Manganese Depletion Leads to Multisystem Changes in the Transcriptome of the Opportunistic PathogenFrontiers in microbiology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Streptococcus gordonii and Streptococcus sanguinis are typically found among the normal oral microbiota but can also cause infective endocarditis. These organisms express cell surface serine-rich repeat adhesins containing "Siglec-like" binding regions (SLBRs) that mediate attachment to α2-3-linked sialic acids on human glycoproteins. Two known receptors for the Siglec-like adhesins are the salivary mucin MG2/MUC7 and platelet GPIbα, and the interaction of streptococci with these targets may contribute to oral colonization and endocarditis, respectively. The SLBRs display a surprising diversity of preferences for defined glycans, ranging from highly selective to broader specificity. In this report, we characterize the glycoproteins in human plasma recognized by four SLBRs that prefer different α2-3 sialoglycan structures. We found that the SLBRs recognize a surprisingly small subset of plasma proteins that are extensively O-glycosylated. The preferred plasma protein ligands for a sialyl-T antigen-selective SLBR are proteoglycan 4 (lubricin) and inter-alpha-trypsin inhibitor heavy chain H4. Conversely, the preferred ligand for a 3'sialyllactosamine-selective SLBR is glycocalicin (the extracellular portion of platelet GPIbα). All four SLBRs recognize C1 inhibitor but detect distinctly different glycoforms of this key regulator of the complement and kallikrein protease cascades. The four plasma ligands have potential roles in thrombosis and inflammation, and each has been cited as a biomarker for one or more vascular or other diseases. The combined results suggest that the interaction of Siglec-like adhesins with different subsets of plasma glycoproteins could have a significant impact on the propensity of streptococci to establish endocardial infections.
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