Endoplasmic Reticulum Chaperones in Viral Infection: Therapeutic Perspectives.
Fiche publication
Date publication
octobre 2021
Journal
Microbiology and molecular biology reviews : MMBR
Auteurs
Membres identifiés du Cancéropôle Est :
Dr DUBREZ Laurence, Dr GARRIDO Carmen, Dr DEMIDOV Oleg, Pr KOHLI Evelyne
Tous les auteurs :
Kohli E, Causse S, Baverel V, Dubrez L, Borges-Bonan N, Demidov O, Garrido C
Lien Pubmed
Résumé
Viruses are intracellular parasites that subvert the functions of their host cells to accomplish their infection cycle. The endoplasmic reticulum (ER)-residing chaperone proteins are central for the achievement of different steps of the viral cycle, from entry and replication to assembly and exit. The most abundant ER chaperones are GRP78 (78-kDa glucose-regulated protein), GRP94 (94-kDa glucose-regulated protein), the carbohydrate or lectin-like chaperones calnexin (CNX) and calreticulin (CRT), the protein disulfide isomerases (PDIs), and the DNAJ chaperones. This review will focus on the pleiotropic roles of ER chaperones during viral infection. We will cover their essential role in the folding and quality control of viral proteins, notably viral glycoproteins which play a major role in host cell infection. We will also describe how viruses co-opt ER chaperones at various steps of their infectious cycle but also in order to evade immune responses and avoid apoptosis. Finally, we will discuss the different molecules targeting these chaperones and the perspectives in the development of broad-spectrum antiviral drugs.
Mots clés
DNAJ, ER chaperone, GRP78, GRP94, calnexin, calreticulin, protein disulfide isomerase, viral infection
Référence
Microbiol Mol Biol Rev. 2021 Oct 13;:e0003521