Back to Search Start Over

Identification of Host PDZ-Based Interactions with the SARS-CoV-2 E Protein in Human Monocytes.

Authors :
Ávila-Flores, Antonia
Sánchez-Cabezón, Juan José
Ochoa-Echeverría, Ane
Checa, Ana I.
Rosas-García, Jorge
Téllez-Araiza, Mariana
Casado, Sara
Liébana, Rosa
Santos-Mendoza, Teresa
Mérida, Isabel
Source :
International Journal of Molecular Sciences. Aug2023, Vol. 24 Issue 16, p12793. 24p.
Publication Year :
2023

Abstract

Proteins containing PDZ (post-synaptic density, PSD-95/disc large, Dlg/zonula occludens, ZO-1) domains assemble signaling complexes that orchestrate cell responses. Viral pathogens target host PDZ proteins by coding proteins containing a PDZ-binding motif (PBM). The presence of a PBM in the SARS-CoV-2 E protein contributes to the virus's pathogenicity. SARS-CoV-2 infects epithelia, but also cells from the innate immune response, including monocytes and alveolar macrophages. This process is critical for alterations of the immune response that are related to the deaths caused by SARS-CoV-2. Identification of E-protein targets in immune cells might offer clues to understanding how SARS-CoV-2 alters the immune response. We analyzed the interactome of the SARS-CoV-2 E protein in human monocytes. The E protein was expressed fused to a GFP tag at the amino terminal in THP-1 monocytes, and associated proteins were identified using a proteomic approach. The E-protein interactome provided 372 partners; only 8 of these harbored PDZ domains, including the cell polarity protein ZO-2, the chemoattractant IL-16, and syntenin. We addressed the expression and localization of the identified PDZ proteins along the differentiation of primary and THP-1 monocytes towards macrophages and dendritic cells. Our data highlight the importance of identifying the functions of PDZ proteins in the maintenance of immune fitness and the viral alteration of inflammatory response. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
16616596
Volume :
24
Issue :
16
Database :
Academic Search Index
Journal :
International Journal of Molecular Sciences
Publication Type :
Academic Journal
Accession number :
170745984
Full Text :
https://doi.org/10.3390/ijms241612793