HIV-1 Envelope Glycoprotein Cell Surface Localization Is Associated with Antibody-Induced Internalization

To minimize immune responses against infected cells, HIV-1 has evolved different mechanisms to limit the surface expression of its envelope glycoproteins (Env). Recent observations suggest that the binding of certain broadly neutralizing antibodies (bNAbs) targeting the 'closed' conformati...

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Bibliographic Details
Published in:Viruses 2021-09, Vol.13 (10), p.1953
Main Authors: Anand, Sai Priya, Prévost, Jérémie, Descôteaux-Dinelle, Jade, Richard, Jonathan, Nguyen, Dung N, Medjahed, Halima, Chen, Hung-Ching, Smith, 3rd, Amos B, Pazgier, Marzena, Finzi, Andrés
Format: Article
Language:English
Subjects:
Acquired immune deficiency syndrome
AIDS
Antibodies
Antigens
broadly neutralizing antibodies
Broadly Neutralizing Antibodies - immunology
CD4 antigen
CD4 Antigens - metabolism
Cell surface
Cloning
Communication
Conformation
endocytosis
Endocytosis - immunology
Env
env Gene Products, Human Immunodeficiency Virus - immunology
env Gene Products, Human Immunodeficiency Virus - metabolism
Epitopes - immunology
Glycoproteins
HEK293 Cells
HIV
HIV Antibodies - immunology
HIV Envelope Protein gp120 - immunology
HIV Envelope Protein gp120 - metabolism
HIV-1
HIV-1 - immunology
Human immunodeficiency virus
Humans
Immune response
Infections
Internalization
Localization
Lymphocytes
Microscopy
Molecular Conformation
non-neutralizing antibodies
Plasmids
Virus Internalization
Viruses
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Summary:To minimize immune responses against infected cells, HIV-1 has evolved different mechanisms to limit the surface expression of its envelope glycoproteins (Env). Recent observations suggest that the binding of certain broadly neutralizing antibodies (bNAbs) targeting the 'closed' conformation of Env induces its internalization. On the other hand, non-neutralizing antibodies (nNAbs) that preferentially target Env in its 'open' conformation, remain bound to Env on the cell surface for longer periods of time. In this study, we attempt to better understand the underlying mechanisms behind the differential rates of antibody-mediated Env internalization. We demonstrate that 'forcing' open Env using CD4 mimetics allows for nNAb binding and results in similar rates of Env internalization as those observed upon the bNAb binding. Moreover, we can identify distinct populations of Env that are differentially targeted by Abs that mediate faster rates of internalization, suggesting that the mechanism of antibody-induced Env internalization partially depends on the localization of Env on the cell surface.
ISSN:1999-4915
1999-4915
DOI:10.3390/v13101953