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Apjok, G.* ; Sári, T.* ; Méhi, O.* ; Asbóth, A.* ; Barna, L.* ; Sala, D.* ; Gróf, I.* ; Vásárhelyi, B.M.* ; Juhász, S.* ; Pál, C.* ; Horvath, P. ; Migh, E.* ; Schneider, G.* ; Hill, C.* ; Deli, M.* ; Shkoporov, A.* ; Kintses, B.*

Prevalent gut phages encode modular adhesins mediating epithelial binding and endoplasmic reticulum trafficking.

Nat. Commun. 17:6191 (2026)
Publ. Version/Full Text Research data DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
Bacteriophages are crucial components of the human microbiome and hold promise as therapeutic agents. Yet, their physical interactions with mammalian cells remain poorly understood. Here, we developed a high-throughput platform to identify phages that adhere to epithelial layers and the proteins that mediate this interaction. The identified phages encode immunoglobulin (Ig)-like domain-containing proteins that, when displayed on a non-adherent phage, confer epithelial binding and internalization in vitro, and increased phage retention in the mouse gut in vivo. Phages encoding these adhesins are among the most abundant and prevalent human gut phages, including crAss-like phages and myoviruses closely related to the recently proposed Flandersviridae family. Domain sequence variation alters epithelial interaction profiles, and internalized phages traffic to the endoplasmic reticulum through the Golgi apparatus, suggesting access to non-degradative internalization pathways. These findings reveal widespread phage-human interactions in the human viral community, with potential impacts on health and implications for next-generation phage therapeutics.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Invasive Escherichia-coli; Outer Capsid Protein; Bacteriophages; Host; Recognition; Bacteria; Therapy; Domains; Pathway; Models
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Journal Nature Communications
Quellenangaben Volume: 17, Issue: 1, Pages: , Article Number: 6191 Supplement: ,
Publisher Springer
Publishing Place London
Reviewing status Peer reviewed
Institute(s) Institute of AI for Health (AIH)
Grants and t
This work was supported by the National Research, Development and Innovation Fund ADVANCED 149516 grant, the 2024-1.2.2-ERA_NET-2024-00004 grant, the National Laboratory of Biotechnology grant 2022-2.1.1-NL-2022-00008, the HUN-REN TKCS-2024/66 grant
Wellcome Trust (Wellcome)
European Molecular Biology Organization (EMBO)