| Literature DB >> 28622976 |
Linlin Gu1, Brian Sims2, Alexandre Krendelchtchikov3, Edlue Tabengwa4, Qiana L Matthews5.
Abstract
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.Entities:
Keywords: Advanced glycosylation end product-specific receptor; Glycoproteins; Human immunodeficiency virus; Phosphatidylserine; Surface plasmon resonance; T-cell immunoglobulin mucin
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Year: 2017 PMID: 28622976 PMCID: PMC5593811 DOI: 10.1016/j.bbamem.2017.06.007
Source DB: PubMed Journal: Biochim Biophys Acta Biomembr ISSN: 0005-2736 Impact factor: 3.747