Unveiling TMEM106B: SARS-CoV-2's secret entrance to the cell

Alexander Lacrampe; Fenghua Hu

doi:10.1016/j.cell.2023.07.005

Unveiling TMEM106B: SARS-CoV-2's secret entrance to the cell

Cell. 2023 Aug 3;186(16):3329-3331. doi: 10.1016/j.cell.2023.07.005.

Authors

Alexander Lacrampe¹, Fenghua Hu²

Affiliations

¹ Department of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA.
² Department of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA. Electronic address: fh87@cornell.edu.

PMID: 37541193
DOI: 10.1016/j.cell.2023.07.005

Abstract

The lysosomal membrane protein TMEM106B functions as a proviral factor in SARS-CoV-2 infection, though it was not known how. In this issue of Cell, Baggen et al. demonstrate that TMEM106B serves as an ACE2-independent receptor for SARS-CoV-2 entry by promoting the fusion of the viral membrane with the lysosomal membrane.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Angiotensin-Converting Enzyme 2 / metabolism
COVID-19*
Humans
Membrane Proteins / genetics
Membrane Proteins / metabolism
Nerve Tissue Proteins
SARS-CoV-2* / genetics
SARS-CoV-2* / metabolism
Virus Internalization

Substances

Angiotensin-Converting Enzyme 2
TMEM106B protein, human
Membrane Proteins
Nerve Tissue Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding