---
title: "Heparan sulfate clusters act as primary docking sites for SARS-CoV-2 attachment and entry"
id: "pubmed-42559812"
canonical_url: "https://medichelpline.com/clinical-feed/pubmed-42559812"
content_type: "clinical_feed_article"
specialty: "Critical Care"
source_name: "PubMed / NCBI"
source_url: "https://pubmed.ncbi.nlm.nih.gov/42559812/"
doi: "10.7554/eLife.108925"
published_at: "2026-08-06T00:00:00.000Z"
evidence_level: "Journal Article"
license: "CC-BY-NC-4.0 / Informational Use"
---
# Heparan sulfate clusters act as primary docking sites for SARS-CoV-2 attachment and entry
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/pubmed-42559812
- **Specialty:** [Critical Care](https://medichelpline.com/clinical-feed/critical-care.md)
- **Primary Source:** PubMed / NCBI
- **Source URL:** [Original Journal Publication](https://pubmed.ncbi.nlm.nih.gov/42559812/)
- **DOI:** [10.7554/eLife.108925](https://doi.org/10.7554%2FeLife.108925)
- **Published At:** 2026-08-06T00:00:00.000Z
- **Evidence Rating:** Journal Article
## Executive GIST (TL;DR)
- Advanced single-molecule nanoscopy (MINFLUX) resolved individual SARS-CoV-2 virions and cell-surface receptors to investigate virus attachment and entry. - The study found that **heparan sulfate (HS)**, not **ACE2**, mediates initial SARS-CoV-2 cell-surface attachment and subsequent endocytosis; ACE2 functions downstream to enable viral genome expression. - SARS-CoV-2 binds to discrete, tall **HS-rich clusters** composed of approximately 6–137 HS molecules that extend about 60–410 nm above the plasma membrane. - These HS clusters occur at a density of roughly one cluster per 6 μm² and serve as docking sites for viral attachment rather than single-molecule HS interactions. - Blocking HS binding with the clinically used HS-binding agent **pixantrone** strongly inhibited attachment and infection by an authentic SARS-CoV-2 Omicron JN.1 subvariant in human airway cells. - The authors propose a revised entry paradigm: HS clusters mediate attachment and endocytosis, while ACE2 acts downstream to permit viral genome expression. - The findings suggest therapeutic potential in targeting HS–virus interactions and indicate that this paradigm may extend beyond SARS-CoV-2 because many other viruses bind HS as an attachment regulator. - The work used high-resolution optical techniques to reveal structural and spatial features of HS that conventional approaches could not resolve. - Conflict of interest: two authors are employed by Abberior Instruments America LLC, which commercializes the MINFLUX microscope; other authors declared no competing interests. - Details on specific experimental protocols, sample sizes, or quantitative assay methods were not reported in the PubMed abstract and would require consulting the full article for full methodological specifics.
## Clinical Analysis & Structured Key Points
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Nanoscopy reveals heparan sulfate clusters as docking sites for SARS-CoV-2 attachment and entry [Sue Han](https://pubmed.ncbi.nlm.nih.gov/?term=Han+S&cauthor_id=42559812)[#](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-equal-contrib-explanation "Contributed equally")[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Xin Wang](https://pubmed.ncbi.nlm.nih.gov/?term=Wang+X&cauthor_id=42559812)[#](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-equal-contrib-explanation "Contributed equally")[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Tiansheng Li](https://pubmed.ncbi.nlm.nih.gov/?term=Li+T&cauthor_id=42559812)[#](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-equal-contrib-explanation "Contributed equally")[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-2 "Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States."), [Ammar Mohseni](https://pubmed.ncbi.nlm.nih.gov/?term=Mohseni+A&cauthor_id=42559812)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Ivan Kosik](https://pubmed.ncbi.nlm.nih.gov/?term=Kosik+I&cauthor_id=42559812)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-2 "Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States."), [Chung Yu Chan](https://pubmed.ncbi.nlm.nih.gov/?term=Chan+CY&cauthor_id=42559812)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Alberto Domingo López-Muñoz](https://pubmed.ncbi.nlm.nih.gov/?term=L%C3%B3pez-Mu%C3%B1oz+AD&cauthor_id=42559812)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-2 "Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States."), [Jessica Matthias](https://pubmed.ncbi.nlm.nih.gov/?term=Matthias+J&cauthor_id=42559812)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-3 "Abberior Instruments America LLC, Bethesda, United States."), [Reid Suddaby](https://pubmed.ncbi.nlm.nih.gov/?term=Suddaby+R&cauthor_id=42559812)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Zhixiong Wang](https://pubmed.ncbi.nlm.nih.gov/?term=Wang+Z&cauthor_id=42559812)[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-4 "Intramural Research Program, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, United States."), [Albert J Jin](https://pubmed.ncbi.nlm.nih.gov/?term=Jin+AJ&cauthor_id=42559812)[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-4 "Intramural Research Program, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, United States."), [Christian A Wurm](https://pubmed.ncbi.nlm.nih.gov/?term=Wurm+CA&cauthor_id=42559812)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-3 "Abberior Instruments America LLC, Bethesda, United States."), [Jonathan W Yewdell](https://pubmed.ncbi.nlm.nih.gov/?term=Yewdell+JW&cauthor_id=42559812)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-2 "Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States."), [Ling-Gang Wu](https://pubmed.ncbi.nlm.nih.gov/?term=Wu+LG&cauthor_id=42559812)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#full-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States.") Affiliations Expand ### Affiliations * 1 National Institute of Neurological Disorders and Stroke, Bethesda, United States. * 2 Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States. * 3 Abberior Instruments America LLC, Bethesda, United States. * 4 Intramural Research Program, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, United States. # Contributed equally. * PMID: **42559812** * DOI: [ 10.7554/eLife.108925 ](https://doi.org/10.7554/elife.108925) Item in Clipboard # Nanoscopy reveals heparan sulfate clusters as docking sites for SARS-CoV-2 attachment and entry Sue Han et al. Elife. 2026. Show details Display options Display options Format Abstract PubMed PMID Elife Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Elife%22%5Bjour%5D&sort=date&sort_order=desc) * [ Search in NLM Catalog ](https://www.ncbi.nlm.nih.gov/nlmcatalog?term=%22Elife%22%5BTitle+Abbreviation%5D) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42559812/) . 2026 Aug 6:14:RP108925. doi: 10.7554/eLife.108925. ### Authors [Sue Han](https://pubmed.ncbi.nlm.nih.gov/?term=Han+S&cauthor_id=42559812)[#](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-equal-contrib-explanation "Contributed equally")[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Xin Wang](https://pubmed.ncbi.nlm.nih.gov/?term=Wang+X&cauthor_id=42559812)[#](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-equal-contrib-explanation "Contributed equally")[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Tiansheng Li](https://pubmed.ncbi.nlm.nih.gov/?term=Li+T&cauthor_id=42559812)[#](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-equal-contrib-explanation "Contributed equally")[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-2 "Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States."), [Ammar Mohseni](https://pubmed.ncbi.nlm.nih.gov/?term=Mohseni+A&cauthor_id=42559812)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Ivan Kosik](https://pubmed.ncbi.nlm.nih.gov/?term=Kosik+I&cauthor_id=42559812)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-2 "Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States."), [Chung Yu Chan](https://pubmed.ncbi.nlm.nih.gov/?term=Chan+CY&cauthor_id=42559812)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Alberto Domingo López-Muñoz](https://pubmed.ncbi.nlm.nih.gov/?term=L%C3%B3pez-Mu%C3%B1oz+AD&cauthor_id=42559812)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-2 "Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States."), [Jessica Matthias](https://pubmed.ncbi.nlm.nih.gov/?term=Matthias+J&cauthor_id=42559812)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-3 "Abberior Instruments America LLC, Bethesda, United States."), [Reid Suddaby](https://pubmed.ncbi.nlm.nih.gov/?term=Suddaby+R&cauthor_id=42559812)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States."), [Zhixiong Wang](https://pubmed.ncbi.nlm.nih.gov/?term=Wang+Z&cauthor_id=42559812)[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-4 "Intramural Research Program, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, United States."), [Albert J Jin](https://pubmed.ncbi.nlm.nih.gov/?term=Jin+AJ&cauthor_id=42559812)[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-4 "Intramural Research Program, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, United States."), [Christian A Wurm](https://pubmed.ncbi.nlm.nih.gov/?term=Wurm+CA&cauthor_id=42559812)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-3 "Abberior Instruments America LLC, Bethesda, United States."), [Jonathan W Yewdell](https://pubmed.ncbi.nlm.nih.gov/?term=Yewdell+JW&cauthor_id=42559812)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-2 "Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States."), [Ling-Gang Wu](https://pubmed.ncbi.nlm.nih.gov/?term=Wu+LG&cauthor_id=42559812)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42559812/#short-view-affiliation-1 "National Institute of Neurological Disorders and Stroke, Bethesda, United States.") ### Affiliations * 1 National Institute of Neurological Disorders and Stroke, Bethesda, United States. * 2 Cellular Biology Section, Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States. * 3 Abberior Instruments America LLC, Bethesda, United States. * 4 Intramural Research Program, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, United States. # Contributed equally. * PMID: **42559812** * DOI: [ 10.7554/eLife.108925 ](https://doi.org/10.7554/elife.108925) Item in Clipboard Cite Display options Display options Format Abstract PubMed PMID ## Abstract Virus entry is thought to involve binding a unique receptor for cell attachment and cytosolic entry. For SARS-CoV-2 underlying the COVID-19 pandemic, angiotensin-converting enzyme 2 (ACE2) is widely considered the receptor for cell-surface attachment and subsequent cell entry. Using advanced light microscopy to resolve individual virions and receptors, we found instead that heparan sulfate (HS), not ACE2, mediates SARS-CoV-2 cell-surface attachment, and subsequent endocytosis. ACE2 functions only downstream of HS to enable viral genome expression. Instead of binding single HS molecules that electrostatically interact with viral surface proteins weakly, SARS-CoV-2 binds clusters of ~6-137 HS molecules projecting 60-410 nm above the plasma membrane. These tall, HS-rich clusters, present at about one per 6 μm², act as docking sites for viral attachment. Blocking HS binding with the clinically used HS-binding agent pixantrone strongly inhibited an authentic pathogen, the SARS-CoV-2 Omicron JN.1 subvariant, from attaching to and infecting human airway cells. This work establishes a revised entry paradigm in which HS clusters mediate SARS-CoV-2 attachment and endocytosis, with ACE2 acting downstream, thereby identifying HS interactions as a key anti-COVID-19 strategy. This paradigm and its therapeutic implications may apply broadly beyond COVID-19 because, analogous to SARS-CoV-2, HS binds many other viruses but is only considered an attachment regulator. **Keywords:** MINFLUX nanoscopy; SARS-CoV-2; attachment receptor; heparan sulfate; infectious disease; microbiology; virus endocytosis; virus receptor; viruses. [PubMed Disclaimer](https://pubmed.ncbi.nlm.nih.gov/disclaimer/) ## Conflict of interest statement SH, XW, TL, AM, IK, CC, AL, RS, ZW, AJ, JY, LW No competing interests declared, JM Jessica Matthias works for Abberior Instruments America LLC, Bethesda, MD, United States, which commercializes the MINFLUX microscope, CW Christian A. Wurm works for Abberior Instruments America LLC, Bethesda, MD, United States, which commercializes the MINFLUX microscope ## Similar articles * [ SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2. ](https://pubmed.ncbi.nlm.nih.gov/32970989/) Clausen TM, Sandoval DR, Spliid CB, Pihl J, Perrett HR, Painter CD, Narayanan A, Majowicz SA, Kwong EM, McVicar RN, Thacker BE, Glass CA, Yang Z, Torres JL, Golden GJ, Bartels PL, Porell RN, Garretson AF, Laubach L, Feldman J, Yin X, Pu Y, Hauser BM, Caradonna TM, Kellman BP, Martino C, Gordts PLSM, Chanda SK, Schmidt AG, Godula K, Leibel SL, Jose J, Corbett KD, Ward AB, Carlin AF, Esko JD.Clausen TM, et al.Cell. 2020 Nov 12;183(4):1043-1057.e15. doi: 10.1016/j.cell.2020.09.033. Epub 2020 Sep 14.Cell. 2020.PMID: 32970989Free PMC article. * [ Identification of SARS-CoV-2 Cell Entry Inhibitors by Drug Repurposing Using _in silico_ Structure-Based Virtual Screening Approach. ](https://pubmed.ncbi.nlm.nih.gov/32754161/) Choudhary S, Malik YS, Tomar S.Choudhary S, et al.Front Immunol. 2020 Jul 10;11:1664. doi: 10.3389/fimmu.2020.01664. eCollection 2020.Front Immunol. 2020.PMID: 32754161Free PMC article. * [ Disrupting SARS-CoV-2 Spike-ACE2 Interactions via Glycosaminoglycans in a Pseudoviral Study of Heparan Sulfate and Enoxaparin. ](https://pubmed.ncbi.nlm.nih.gov/40723804/) Fuochi V, Furnari S, Drago F, Furneri PM.Fuochi V, et al.Biomolecules. 2025 Jun 26;15(7):931. doi: 10.3390/biom15070931.Biomolecules. 2025.PMID: 40723804Free PMC article. * [ Targeting the viral-entry facilitators of SARS-CoV-2 as a therapeutic strategy in COVID-19. ](https://pubmed.ncbi.
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