Entry Efficiency, Protease Dependence, and Antibody-Mediated Neutralization of SARS-CoV-2 Sublineages KP.3.1.1 and XEC

Our findings demonstrate that JN.1, KP.3.1.1, and XEC, like their predecessor BA.2.86, rely on TMPRSS2 for lung cell entry and remain sensitive to certain neutralizing monoclonal antibodies. However, these variants differ in their ability to utilize ACE2 species orthologs for cell entry.

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Publication Details

Journal
Vaccines
Published
2025-04-03
DOI
https://doi.org/10.3390/vaccines13040385
Citations
3
Primary Topic
SARS-CoV-2 and COVID-19 Research
Type
article
Field-Weighted Citation Impact
4.19

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article

Entry Efficiency, Protease Dependence, and Antibody-Mediated Neutralization of SARS-CoV-2 Sublineages KP.3.1.1 and XEC

Stefan Pöhlmann, Inga Nehlmeier, Markus Hoffmann, Amy Kempf et al.
3 citations
Vaccines
SARS-CoV-2 and COVID-19 Research
4.19
article

Entry Efficiency, Protease Dependence, and Antibody-Mediated Neutralization of SARS-CoV-2 Sublineages KP.3.1.1 and XEC

Stefan Pöhlmann, Inga Nehlmeier, Markus Hoffmann, Amy Kempf, Sebastian Schulz, Hans‐Martin Jäck, Prerna Arora
article en
3 citations

Abstract

Our findings demonstrate that JN.1, KP.3.1.1, and XEC, like their predecessor BA.2.86, rely on TMPRSS2 for lung cell entry and remain sensitive to certain neutralizing monoclonal antibodies. However, these variants differ in their ability to utilize ACE2 species orthologs for cell entry.

VaccinesVol. 13(4)
Friedrich-Alexander-Universität Erlangen-Nürnberg (DE), German Primate Center (DE), University of Göttingen (DE)
Bayerische Forschungsstiftung
Good health and well-being
Openalex Percentile: Top 7%
SARS-CoV-2 and COVID-19 Research
4.19
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Entry Efficiency, Protease Dependence, and Antibody-Mediated Neutralization of SARS-CoV-2 Sublineages KP.3.1.1 and XEC — Stefan Pöhlmann, Inga Nehlmeier, et al. · Vaccines (2025) | TGRS Research Map | TGRS