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@ARTICLE{Fu:302284,
      author       = {R. Fu and P. Jordan and Z. Engels and J. A. Weihs and J.
                      Mürle and H. Chi and S. Burbano de Lara$^*$ and B. Helm$^*$
                      and M. Klöhn and J. Hu and A. Freistaedter and T. Boettler
                      and M. Binder$^*$ and U. Klingmüller$^*$ and E. Steinmann
                      and P.-Y. Lozach and T. Tubiana and S. M. Lemon and V. L.
                      Dao Thi},
      title        = {{I}ntegrin beta 1 facilitates non-enveloped hepatitis {E}
                      virus cell entry through the recycling endosome.},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DKFZ-2025-01303},
      pages        = {5403},
      year         = {2025},
      abstract     = {Hepatitis E virus (HEV) is a major cause of acute hepatitis
                      and mainly transmitted faecal-orally. HEV particles present
                      in faeces are naked (nHEV), whereas those found in the blood
                      are quasi-enveloped (eHEV) with a cell-derived lipid
                      membrane. Despite its global health impact, the cellular
                      life cycle of HEV remains poorly understood, particularly
                      regarding the mechanisms of viral entry into host cells. To
                      address this knowledge gap, we develop a high content
                      RNA-FISH-based imaging assay that allows for the
                      investigation of the entry pathways of both naked and
                      quasi-enveloped HEV particles. Surprisingly, we find that
                      integrin α3, previously implicated in nHEV cell entry, is
                      not expressed in the cell types that are most permissive for
                      HEV infection. Instead, we identify integrin β1 (ITGB1)
                      pairing with different α-integrins as the key player
                      mediating nHEV cell entry. Our results indicate that the
                      interaction of nHEV with ITGB1 facilitates entry through
                      Rab11-positive recycling endosomes. In contrast, eHEV
                      particles do not interact with ITGB1 and enter cells using a
                      classical endocytic route via Rab5a-positive early
                      endosomes. The entry of both types of HEV particles requires
                      endosomal acidification and proteolytic cleavage by
                      lysosomal cathepsins, which ultimately results in delivery
                      of the HEV genome to the cytoplasm.},
      keywords     = {Endosomes: metabolism / Endosomes: virology / Virus
                      Internalization / Humans / Hepatitis E virus: physiology /
                      Hepatitis E virus: genetics / Integrin beta1: metabolism /
                      Integrin beta1: genetics / Hepatitis E: virology / Hepatitis
                      E: metabolism / rab5 GTP-Binding Proteins: metabolism / rab
                      GTP-Binding Proteins: metabolism / HEK293 Cells /
                      Cathepsins: metabolism / Lysosomes: metabolism / Cell Line /
                      Integrin beta1 (NLM Chemicals) / rab5 GTP-Binding Proteins
                      (NLM Chemicals) / Itgb1 protein, human (NLM Chemicals) /
                      rab11 protein (NLM Chemicals) / rab GTP-Binding Proteins
                      (NLM Chemicals) / Cathepsins (NLM Chemicals)},
      cin          = {B200 / D430},
      ddc          = {500},
      cid          = {I:(DE-He78)B200-20160331 / I:(DE-He78)D430-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40571699},
      doi          = {10.1038/s41467-025-61071-y},
      url          = {https://inrepo02.dkfz.de/record/302284},
}