Differential binding of the HIV-1 envelope to phosphatidylserine receptors

Prior work has shown that the HIV-1 envelope of the human immunodeficiency virus (HIV) interacts directly with T-cell immunoglobulin mucin (TIM) family proteins. Herein, we demonstrate that HIV-1 envelope glycoproteins from varying HIV-1 clades bind differentially to TIM proteins and functionally si...

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Detalles Bibliográficos
Autores principales: Gu, Linlin, Sims, Brian, Krendelchtchikov, Alexandre, Tabengwa, Edlue, Matthews, Qiana L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Pub. Co 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5593811/
https://www.ncbi.nlm.nih.gov/pubmed/28622976
http://dx.doi.org/10.1016/j.bbamem.2017.06.007
Descripción
Sumario:Prior work has shown that the HIV-1 envelope of the human immunodeficiency virus (HIV) interacts directly with T-cell immunoglobulin mucin (TIM) family proteins. Herein, we demonstrate that HIV-1 envelope glycoproteins from varying HIV-1 clades bind differentially to TIM proteins and functionally similar proteins acting as phosphatidylserine (PtdSer) receptors. Using enzyme-linked immunosorbent assay (ELISA) and surface plasmon resonance (SPR) technology, we show that lysate containing HIV-1 envelope and recombinant HIV-1 envelope glycoproteins bind TIM-4 and advanced glycosylation end product-specific receptor (AGER). The complex binding of HIV-1 UG21 gp140 to TIM-4 or AGER suggests a biphasic interaction with these proteins.

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