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DC Field | Value | Language |
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dc.contributor.author | Kishore, U | - |
dc.contributor.author | Dodagatta-Marri, E | - |
dc.contributor.author | Mitchell, DA | - |
dc.contributor.author | Pandit, H | - |
dc.contributor.author | Sonowane, A | - |
dc.contributor.author | Murigaiah, V | - |
dc.contributor.author | Idicula-Thomas, S | - |
dc.contributor.author | Nal, B | - |
dc.contributor.author | Al-Mozaini, M | - |
dc.contributor.author | Kaur, A | - |
dc.contributor.author | Madan, T | - |
dc.date.accessioned | 2017-07-11T12:52:51Z | - |
dc.date.available | 2017-07-11T12:52:51Z | - |
dc.date.issued | 2017 | - |
dc.identifier.citation | Frontiers in Immunology | en_US |
dc.identifier.issn | 1664-3224 | - |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/14894 | - |
dc.description.abstract | Surfactant protein SP-D is a soluble C-type lectin, belonging to the collectin (collagencontaining calcium-dependent lectin) family, which acts as an innate immune pattern recognition molecule in the lungs and other mucosal surfaces. Immune regulation and surfactant homeostasis are salient functions of SP-D. SP-D can bind to a range of viral, bacterial and fungal pathogens and trigger clearance mechanisms. SP-D binds to gp120, the envelope protein expressed on HIV-1, through its C-type lectin or carbohydrate recognition domain (CRD). This is of importance since SP-D is secreted by human mucosal epithelial cells and is present in the female reproductive tract including vagina. Another C-type lectin, Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin (DCSIGN), present on the surface of the dendritic cells, also binds to HIV-1 gp120 and facilitates viral transfer to the lymphoid tissues. Dendritic cells are also present at the site of HIV-1 entry, embedded in vaginal or rectal mucosa. In the present study, we report a direct proteinprotein interaction between recombinant forms of SP-D (rfhSP-D) and DC-SIGN via their Ctype lectin domains. Both SP-D and DC-SIGN competed for binding to immobilized HIV-1 gp120. Pre-incubation of Human Embryonic Kidney (HEK) cells expressing surface DCSIGN with rfhSP-D significantly inhibited the HIV-1 transfer to activated PBMCs. In silico analysis revealed that SP-D and gp120 may occupy same sites on DC-SIGN, which may explain the reduced transfer of HIV-1. In summary, we demonstrate, for the first time, that DC-SIGN is a novel binding partner of SP-D, and this interaction can modulate HIV-1 capture and transfer to CD4+ T cells. In addition, the present study also reveals a distinct mechanism of host defense by SP-D against HIV-1. | en_US |
dc.language.iso | en | en_US |
dc.title | Protein-protein interaction between surfactant protein D and DC-SIGN via C-type lectin domain can suppress HIV-1 transfer | en_US |
dc.type | Article | en_US |
dc.identifier.doi | http://dx.doi.org/10.3389/fimmu.2017.00834 | - |
dc.relation.isPartOf | Frontiers in Immunology | - |
pubs.publication-status | Accepted | - |
Appears in Collections: | Dept of Health Sciences Research Papers |
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Fulltext.pdf | 5.04 MB | Adobe PDF | View/Open |
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