Please use this identifier to cite or link to this item: http://buratest.brunel.ac.uk/handle/2438/10332
Title: Surfactant protein D inhibits HIV-1 infection of target cells via interference with gp120-CD4 interaction and modulates pro-inflammatory cytokine production
Authors: Pandit, H
Gopal, S
Sonawani, A
Yadav, AK
Qaseem, AS
Warke, H
Patil, A
Gajbhiye, R
Kulkarni, V
Al-Mozaini, MA
Idicula-Thomas, S
Kishore, U
Madan, T
Keywords: Surfactant Protein SP-D;Innate immunity;Viral replication
Issue Date: 2014
Publisher: Public Library of Science
Citation: PLoS ONE, 9 (7): e102395, (July 2014)
Abstract: Surfactant Protein SP-D, a member of the collectin family, is a pattern recognition protein, secreted by mucosal epithelial cells and has an important role in innate immunity against various pathogens. In this study, we confirm that native human SP-D and a recombinant fragment of human SP-D (rhSP-D) bind to gp120 of HIV-1 and significantly inhibit viral replication in vitro in a calcium and dose-dependent manner. We show, for the first time, that SP-D and rhSP-D act as potent inhibitors of HIV-1 entry in to target cells and block the interaction between CD4 and gp120 in a dose-dependent manner. The rhSP-D-mediated inhibition of viral replication was examined using three clinical isolates of HIV-1 and three target cells: Jurkat T cells, U937 monocytic cells and PBMCs. HIV-1 induced cytokine storm in the three target cells was significantly suppressed by rhSP-D. Phosphorylation of key kinases p38, Erk1/2 and AKT, which contribute to HIV-1 induced immune activation, was significantly reduced in vitro in the presence of rhSP-D. Notably, anti-HIV-1 activity of rhSP-D was retained in the presence of biological fluids such as cervico-vaginal lavage and seminal plasma. Our study illustrates the multi-faceted role of human SPD against HIV-1 and potential of rhSP-D for immunotherapy to inhibit viral entry and immune activation in acute HIV infection. © 2014 Pandit et al.
Description: © 2014 Pandit et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
URI: http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0102395
http://bura.brunel.ac.uk/handle/2438/10332
DOI: http://dx.doi.org/10.1371/journal.pone.0102395
ISSN: 1932-6203
Appears in Collections:Dept of Life Sciences Research Papers

Files in This Item:
File Description SizeFormat 
Fulltext.pdf3.14 MBAdobe PDFView/Open


Items in BURA are protected by copyright, with all rights reserved, unless otherwise indicated.