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Lactoferricin enables adenovirus infection of human skeletal muscle cells

Danskog, Katarina ; Mistry, Nitesh ; Årdahl, Carin ; Durbeej-Hjalt, Madeleine LU ; Forsell, Mattias N.E. ; Lenman, Annasara and Arnberg, Niklas (2025) In NPJ Viruses 3(1).
Abstract

Although adenoviruses (AdVs) possess advantageous features as vectors, several challenges remain. These include a high prevalence of neutralizing antibodies against certain AdV types and the inability to efficiently transduce CAR-deficient cells and tissues. We showed previously that lactoferricin (Lfcin) enhances CAR-independent HAdV-C5 infection of epithelial and T-cells. Here, we assessed the ability of Lfcin to enable HAdV-C5 infection and transduction of human skeletal muscle cells. Lfcin increases HAdV-C5 infection and transduction of muscle myoblasts and myotubes by 10- to 30-fold. Enhanced infection correlates with increased cell binding, which differs mechanistically from that of coagulation factor X-mediated binding, as it... (More)

Although adenoviruses (AdVs) possess advantageous features as vectors, several challenges remain. These include a high prevalence of neutralizing antibodies against certain AdV types and the inability to efficiently transduce CAR-deficient cells and tissues. We showed previously that lactoferricin (Lfcin) enhances CAR-independent HAdV-C5 infection of epithelial and T-cells. Here, we assessed the ability of Lfcin to enable HAdV-C5 infection and transduction of human skeletal muscle cells. Lfcin increases HAdV-C5 infection and transduction of muscle myoblasts and myotubes by 10- to 30-fold. Enhanced infection correlates with increased cell binding, which differs mechanistically from that of coagulation factor X-mediated binding, as it remains unaffected by the removal of heparan sulfate. Additionally, Lfcin reduces the neutralizing effects of serum against HAdV-C5, suggesting it may shield key epitopes. By enabling viral binding to muscle cells and mitigating serum neutralization, Lfcin offers a novel strategy to improve the efficiency and durability of HAdV-C5-based gene delivery systems.

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Contribution to journal
publication status
published
subject
in
NPJ Viruses
volume
3
issue
1
article number
62
publisher
Springer Nature
external identifiers
  • scopus:105022271801
  • pmid:40826223
ISSN
2948-1767
DOI
10.1038/s44298-025-00144-7
language
English
LU publication?
yes
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Publisher Copyright: © The Author(s) 2025.
id
228d28bc-cf37-4890-a30f-c30c57aceafb
date added to LUP
2026-01-16 14:28:02
date last changed
2026-01-17 03:00:08
@article{228d28bc-cf37-4890-a30f-c30c57aceafb,
  abstract     = {{<p>Although adenoviruses (AdVs) possess advantageous features as vectors, several challenges remain. These include a high prevalence of neutralizing antibodies against certain AdV types and the inability to efficiently transduce CAR-deficient cells and tissues. We showed previously that lactoferricin (Lfcin) enhances CAR-independent HAdV-C5 infection of epithelial and T-cells. Here, we assessed the ability of Lfcin to enable HAdV-C5 infection and transduction of human skeletal muscle cells. Lfcin increases HAdV-C5 infection and transduction of muscle myoblasts and myotubes by 10- to 30-fold. Enhanced infection correlates with increased cell binding, which differs mechanistically from that of coagulation factor X-mediated binding, as it remains unaffected by the removal of heparan sulfate. Additionally, Lfcin reduces the neutralizing effects of serum against HAdV-C5, suggesting it may shield key epitopes. By enabling viral binding to muscle cells and mitigating serum neutralization, Lfcin offers a novel strategy to improve the efficiency and durability of HAdV-C5-based gene delivery systems.</p>}},
  author       = {{Danskog, Katarina and Mistry, Nitesh and Årdahl, Carin and Durbeej-Hjalt, Madeleine and Forsell, Mattias N.E. and Lenman, Annasara and Arnberg, Niklas}},
  issn         = {{2948-1767}},
  language     = {{eng}},
  number       = {{1}},
  publisher    = {{Springer Nature}},
  series       = {{NPJ Viruses}},
  title        = {{Lactoferricin enables adenovirus infection of human skeletal muscle cells}},
  url          = {{http://dx.doi.org/10.1038/s44298-025-00144-7}},
  doi          = {{10.1038/s44298-025-00144-7}},
  volume       = {{3}},
  year         = {{2025}},
}