HIV-1 Envelope Glycoproteins Proteolytic Cleavage Protects Infected Cells from ADCC Mediated by Plasma from Infected Individuals
The HIV-1 envelope glycoprotein (Env) is synthesized in the endoplasmic reticulum as a trimeric gp160 precursor, which requires proteolytic cleavage by a cellular furin protease to mediate virus-cell fusion. Env is conformationally flexible but controls its transition from the unbound “closed” confo...
Main Authors: | Jérémie Prévost, Halima Medjahed, Dani Vézina, Hung-Ching Chen, Beatrice H. Hahn, Amos B. Smith, Andrés Finzi |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2021-11-01
|
Series: | Viruses |
Subjects: | |
Online Access: | https://www.mdpi.com/1999-4915/13/11/2236 |
Similar Items
-
Temsavir Modulates HIV-1 Envelope Conformation by Decreasing Its Proteolytic Cleavage
by: Marianne Boutin, et al.
Published: (2023-05-01) -
Temsavir Treatment of HIV-1-Infected Cells Decreases Envelope Glycoprotein Recognition by Broadly Neutralizing Antibodies
by: Marianne Boutin, et al.
Published: (2022-06-01) -
Host antiviral factors hijack furin to block SARS-CoV-2, ebola virus, and HIV-1 glycoproteins cleavage
by: Changqing Yu, et al.
Published: (2023-12-01) -
Genome-wide bioinformatics analysis of human protease capacity for proteolytic cleavage of the SARS-CoV-2 spike glycoprotein
by: Evgenii V. Matveev, et al.
Published: (2024-02-01) -
Positively Selected Sites at HCMV gB Furin Processing Region and Their Effects in Cleavage Efficiency
by: Lucas M. Stangherlin, et al.
Published: (2017-05-01)