@article{14255,
  abstract     = {Toscana virus is a major cause of arboviral disease in humans in the Mediterranean basin during summer. However, early virus-host cell interactions and entry mechanisms remain poorly characterized. Investigating iPSC-derived human neurons and cell lines, we found that virus binding to the cell surface was specific, and 50% of bound virions were endocytosed within 10 min. Virions entered Rab5a+ early endosomes and, subsequently, Rab7a+ and LAMP-1+ late endosomal compartments. Penetration required intact late endosomes and occurred within 30 min following internalization. Virus entry relied on vacuolar acidification, with an optimal pH for viral membrane fusion at pH 5.5. The pH threshold increased to 5.8 with longer pre-exposure of virions to the slightly acidic pH in early endosomes. Strikingly, the particles remained infectious after entering late endosomes with a pH below the fusion threshold. Overall, our study establishes Toscana virus as a late-penetrating virus and reveals an atypical use of vacuolar acidity by this virus to enter host cells.},
  author       = {Koch, Jana and Xin, Qilin and Obr, Martin and Schäfer, Alicia and Rolfs, Nina and Anagho, Holda A. and Kudulyte, Aiste and Woltereck, Lea and Kummer, Susann and Campos, Joaquin and Uckeley, Zina M. and Bell-Sakyi, Lesley and Kräusslich, Hans Georg and Schur, Florian Km and Acuna, Claudio and Lozach, Pierre Yves},
  issn         = {1553-7374},
  journal      = {PLoS Pathogens},
  number       = {8},
  publisher    = {Public Library of Science},
  title        = {{The phenuivirus Toscana virus makes an atypical use of vacuolar acidity to enter host cells}},
  doi          = {10.1371/journal.ppat.1011562},
  volume       = {19},
  year         = {2023},
}

@article{9046,
  author       = {Römhild, Roderich and Andersson, Dan I.},
  issn         = {1553-7374},
  journal      = {PLoS Pathogens},
  number       = {1},
  publisher    = {Public Library of Science},
  title        = {{Mechanisms and therapeutic potential of collateral sensitivity to antibiotics}},
  doi          = {10.1371/journal.ppat.1009172},
  volume       = {17},
  year         = {2021},
}

@article{540,
  abstract     = {RNA-dependent RNA polymerases (RdRps) play a key role in the life cycle of RNA viruses and impact their immunobiology. The arenavirus lymphocytic choriomeningitis virus (LCMV) strain Clone 13 provides a benchmark model for studying chronic infection. A major genetic determinant for its ability to persist maps to a single amino acid exchange in the viral L protein, which exhibits RdRp activity, yet its functional consequences remain elusive. To unravel the L protein interactions with the host proteome, we engineered infectious L protein-tagged LCMV virions by reverse genetics. A subsequent mass-spectrometric analysis of L protein pulldowns from infected human cells revealed a comprehensive network of interacting host proteins. The obtained LCMV L protein interactome was bioinformatically integrated with known host protein interactors of RdRps from other RNA viruses, emphasizing interconnected modules of human proteins. Functional characterization of selected interactors highlighted proviral (DDX3X) as well as antiviral (NKRF, TRIM21) host factors. To corroborate these findings, we infected Trim21-/-mice with LCMV and found impaired virus control in chronic infection. These results provide insights into the complex interactions of the arenavirus LCMV and other viral RdRps with the host proteome and contribute to a better molecular understanding of how chronic viruses interact with their host.},
  author       = {Khamina, Kseniya and Lercher, Alexander and Caldera, Michael and Schliehe, Christopher and Vilagos, Bojan and Sahin, Mehmet and Kosack, Lindsay and Bhattacharya, Anannya and Májek, Peter and Stukalov, Alexey and Sacco, Roberto and James, Leo and Pinschewer, Daniel and Bennett, Keiryn and Menche, Jörg and Bergthaler, Andreas},
  issn         = {1553-7366},
  journal      = {PLoS Pathogens},
  number       = {12},
  publisher    = {Public Library of Science},
  title        = {{Characterization of host proteins interacting with the lymphocytic choriomeningitis virus L protein}},
  doi          = {10.1371/journal.ppat.1006758},
  volume       = {13},
  year         = {2017},
}