4.5 Article

The Examination of Viral Characteristics of HIV-1 CRF07_BC and Its Potential Interaction with Extracellular Galectin-3

Journal

PATHOGENS
Volume 9, Issue 6, Pages -

Publisher

MDPI
DOI: 10.3390/pathogens9060425

Keywords

Galectin-3; HIV-1; CRF07_BC; envelope; gp120; CD4

Categories

Funding

  1. Ministry of Science and Technology, R.O.C. [MOST 108-2918-I-037-001, 108-2320-B-037-035-MY3, MOST 107-2923-B-005-005-MY3]
  2. Kaohsiung Medical University Research Center Grant [KMU-TC108B03]
  3. Taiwan Centers for Disease Control (CDC) [MOHW109-CDC-C-114-000105, MOHW108-CDC-C-114-000105]

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HIV-1 CRF07_BC is a B' and C subtype recombinant emerging virus and many of its viral characteristics remain unclear. Galectin-3 (Gal3) is a beta-galactose binding lectin that has been reported as a pattern recognition receptor (PRR) and is known to mediate adhesion between cells and microbes. This study aims to examine the viral characteristics of HIV-1 CRF07_BC virus and the role of extracellular galectin-3 in HIV-1 CRF07_BC infection. A total of 28 HIV-1+ injecting drug users (IDUs) were recruited and 24 (85.7%) were identified as HIV-1 CRF07_BC. Results indicate that significant higher serum galectin-3 was measured in CRF07_BC infected patients and CRF07_BC infection triggered significant galectin-3 expression (p< 0.01). Viral characteristics demonstrate that CRF07_BC virions display a higher level of envelope gp120 spikes. The virus infectivity assay demonstrated that co-treatment with galectin-3 significantly promoted CRF07_BC attachment and internalization (p< 0.01). A co-immunoprecipitation assay showed that pulldown galectin-3 co-precipitated both CD4 and gp120 proteins. Results from an enzyme-linked immunosorbent assay (ELISA) indicate that the galectin-3 promoting effect occurs through enhancement of the interaction between gp120 and CD4. This study suggests that CRF07_BC was predominant in HIV-1+ IDUs and CRF07_BC utilized extracellular galectin-3 to enhance its infectivity via stabilization of the gp120-CD4 interaction.

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