---
title: "ACE2 Clustering Activates PIEZO1–Sphingomyelinase Pathway Driving SARS‑CoV‑2 Spike Cell‑Cell Fusion"
id: "biorxiv-7-multivalent-ace2-engagement-activates-piezo1-sphingomyelinase-signaling-in-sars"
canonical_url: "https://medichelpline.com/clinical-feed/biorxiv-7-multivalent-ace2-engagement-activates-piezo1-sphingomyelinase-signaling-in-sars"
content_type: "clinical_feed_article"
specialty: "Infectious Disease"
source_name: "bioRxiv (Biomedical Preprints)"
source_url: "https://www.biorxiv.org/content/10.64898/2026.10.22.761047v1?rss=1"
published_at: "2026-10-23T12:00:00.000Z"
evidence_level: "Verified Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# ACE2 Clustering Activates PIEZO1–Sphingomyelinase Pathway Driving SARS‑CoV‑2 Spike Cell‑Cell Fusion
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/biorxiv-7-multivalent-ace2-engagement-activates-piezo1-sphingomyelinase-signaling-in-sars
- **Specialty:** [Infectious Disease](https://medichelpline.com/clinical-feed/infectious-disease.md)
- **Primary Source:** bioRxiv (Biomedical Preprints)
- **Source URL:** [Original Journal Publication](https://www.biorxiv.org/content/10.64898/2026.10.22.761047v1?rss=1)
- **Published At:** 2026-10-23T12:00:00.000Z
- **Evidence Rating:** Verified Feed
## Executive GIST (TL;DR)
- Investigators reported that SARS‑CoV‑2 **Spike** drives not only viral envelope fusion but also syncytium formation, a process linked to viral spread and lung pathology. - The study team examined Spike-triggered signaling in ACE2-expressing A549 cells and focused on activation of acid sphingomyelinase (**ASM**) as a mediator of fusion. - Using ASM-deficient and complemented cells, the cohort showed that restoring ASM activity and adding exogenous **ceramide** promoted Spike-mediated cell-cell fusion. - Data indicated pharmacological perturbations and a split-NeonGreen fusion assay were used to quantify fusion; the source did not report detailed dosing or exact inhibitor identities in the abstract. - Authors noted a proposed pathway: multivalent **ACE2** engagement by Spike clusters ACE2, which activates the mechanosensitive ion channel **PIEZO1**, leading to lysosomal exocytosis and secretion of ASM. - Secreted ASM, together with intracellular neutral sphingomyelinase, generates ceramide that enhances syncytium formation, likely via activation of protein phosphatases PP1 and PP2A. - The study team observed that PP1/PP2A activity may facilitate actin cortex detachment and reduce actomyosin tension through dephosphorylation of ERM proteins, promoting membrane fusion. - Authors suggested these membrane lipid changes and membrane–cytoskeleton interactions regulate Spike-mediated fusion and could apply to other viral or cellular fusion systems. - The abstract did not report numerical effect sizes, experimental counts, or specific methodological parameters beyond the cell line (ACE2-expressing A549), so those details remain unreported in this source.
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Elena M Zaitseva 1 NIH; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Elena%2BM%2BZaitseva%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Zaitseva%20EM&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AElena%2BM%2BZaitseva%2B) Eugene N Zaitsev 1 NIH; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Eugene%2BN%2BZaitsev%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Zaitsev%20EN&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AEugene%2BN%2BZaitsev%2B) Kamran Melikov 2 Eunice Kennedy Shriver National Institute of Child Health and Human Development * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Kamran%2BMelikov%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Melikov%20K&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AKamran%2BMelikov%2B) * [ORCID record for Kamran Melikov](http://orcid.org/0009-0009-6523-4346 "Open in new tab") Leonid V Chernomordik 1 NIH; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Leonid%2BV%2BChernomordik%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Chernomordik%20LV&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3ALeonid%2BV%2BChernomordik%2B) * [ORCID record for Leonid V Chernomordik](http://orcid.org/0000-0001-7131-9244 "Open in new tab") * For correspondence: chernoml@mail.nih.gov * [Abstract](https://www.biorxiv.org/content/10.64898/2026.10.22.761047v1)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_art/node:5898072/1) * [Info/History](https://www.biorxiv.org/content/10.64898/2026.10.22.761047v1.article-info)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_info/node:5898072/1) * [Metrics](https://www.biorxiv.org/content/10.64898/2026.10.22.761047v1.article-metrics)[](https://www.biorxiv.org/panels_ajax_tab/article_tab_metrics/node:5898072/1) * [ Preview PDF](https://www.biorxiv.org/content/10.64898/2026.10.22.761047v1.full.pdf+html)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_pdf/node:5898072/1) ![Loading](https://www.biorxiv.org/sites/all/modules/contrib/panels_ajax_tab/images/loading.gif) ## Abstract SARS CoV 2 Spike not only fuses the viral envelope with host membranes to deliver viral RNA but also drives syncytium formation, a process that may contribute to viral spread and pulmonary pathology. Although the conformational transitions in Spike triggered by ACE2 engagement are well characterized, the host cell signaling events initiated by Spike-ACE2 interactions remain less understood. Here, we examine how Spike activates acid sphingomyelinase (ASM) in ACE2 expressing A549 cells and how this activity promotes cell-cell fusion. Using ASM-deficient and complemented cells, exogenous ceramide, pharmacological perturbations, and a split-NeonGreen fusion assay, we support a fusion-promoting pathway in which Spike-induced ACE2 clustering activates the mechanosensitive ion channel PIEZO1, triggering lysosomal exocytosis. Secreted ASM, together with intracellular neutral sphingomyelinase, generates ceramide that enhances syncytium formation, likely through activation of protein phosphatases PP1 and PP2A. Our results suggest that these phosphatases promote fusion by facilitating actin cortex detachment and reducing actomyosin tension through dephosphorylation of ERM proteins. Our findings highlight dynamic changes in membrane lipid composition and membrane-cytoskeleton interactions as regulators of fusion and signaling in SARS-CoV-2 infection and, potentially, other viral and cellular systems. ### Competing Interest Statement The authors have declared no competing interest. ## Funder Information Declared Intramural Program, NICHD, NIH, ZIA HD001501 Copyright The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. This article is a US Government work. It is not subject to copyright under 17 USC 105 and is also made available for use under a CC0 license. bioRxiv and medRxiv thank the following for their generous financial support: > The Chan Zuckerberg Initiative, Cold Spring Harbor Laboratory, the Sergey Brin Family Foundation, California Institute of Technology, Centre National de la Recherche Scientifique, Fred Hutchinson Cancer Center, Imperial College London, Massachusetts Institute of Technology, Stanford University, The University of Edinburgh, University of Washington, and Vrije Universiteit Amsterdam. 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[ Download PDF](https://www.biorxiv.org/content/10.64898/2026.10.22.761047v1.full.pdf) Print/Save Options [Download PDF](https://www.biorxiv.org/content/biorxiv/early/2026/10/23/2026.10.22.761047.full.pdf)Full Text & In-line FiguresXML [More Info](https://www.biorxiv.org/about/FAQ#PrintOptions "More Information on Print/Save Options") [ Email](https://www.biorxiv.org/ "Email this Article") [ Share](https://www.biorxiv.org/) MULTIVALENT ACE2 ENGAGEMENT ACTIVATES PIEZO1-SPHINGOMYELINASE SIGNALING IN SARS-COV-2 SPIKE-MEDIATED CELL-CELL FUSION Elena M Zaitseva, Eugene N Zaitsev, Kamran Melikov, Leonid V Chernomordik bioRxiv 2026.10.22.761047; doi: https://doi.org/10.64898/2026.10.22.761047 This article is a preprint and has not been certified by peer review [[what does this mean?](https://www.biorxiv.org/about/FAQ#unrefereed)]. 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