Surfactant Protein D modulates HIV infection of both T-cells and dendritic cells.
Surfactant Protein D (SP-D) is an oligomerized C-type lectin molecule with immunomodulatory properties and involvement in lung surfactant homeostasis in the respiratory tract. SP-D binds to the enveloped viruses, influenza A virus and respiratory syncytial virus and inhibits their replication in vit...
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0059047&type=printable |
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| author | Jens Madsen Gaurav D Gaiha Nades Palaniyar Tao Dong Daniel A Mitchell Howard W Clark |
| author_facet | Jens Madsen Gaurav D Gaiha Nades Palaniyar Tao Dong Daniel A Mitchell Howard W Clark |
| author_sort | Jens Madsen |
| collection | DOAJ |
| description | Surfactant Protein D (SP-D) is an oligomerized C-type lectin molecule with immunomodulatory properties and involvement in lung surfactant homeostasis in the respiratory tract. SP-D binds to the enveloped viruses, influenza A virus and respiratory syncytial virus and inhibits their replication in vitro and in vivo. SP-D has been shown to bind to HIV via the HIV envelope protein gp120 and inhibit infectivity in vitro. Here we show that SP-D binds to different strains of HIV (BaL and IIIB) and the binding occurs at both pH 7.4 and 5.0 resembling physiological relevant pH values found in the body and the female urogenital tract, respectively. The binding of SP-D to HIV particles and gp120 was inhibited by the presence of several hexoses with mannose found to be the strongest inhibitor. Competition studies showed that soluble CD4 and CVN did not interfere with the interaction between SP-D and gp120. However, soluble recombinant DC-SIGN was shown to inhibit the binding between SP-D and gp120. SP-D agglutinated HIV and gp120 in a calcium dependent manner. SP-D inhibited the infectivity of HIV strains at both pH values of 7.4 and 5.0 in a concentration dependent manner. The inhibition of the infectivity was abolished by the presence of mannose. SP-D enhanced the binding of HIV to immature monocyte derived dendritic cells (iMDDCs) and was also found to enhance HIV capture and transfer to the T-cell like line PM1. These results suggest that SP-D can bind to and inhibit direct infection of T-cells by HIV but also enhance the transfer of infectious HIV particles from DCs to T-cells in vivo. |
| format | Article |
| id | doaj-art-dae37d2140ee4f09b35d4f18d9fa0f05 |
| institution | OA Journals |
| issn | 1932-6203 |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-dae37d2140ee4f09b35d4f18d9fa0f052025-08-20T02:30:38ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0183e5904710.1371/journal.pone.0059047Surfactant Protein D modulates HIV infection of both T-cells and dendritic cells.Jens MadsenGaurav D GaihaNades PalaniyarTao DongDaniel A MitchellHoward W ClarkSurfactant Protein D (SP-D) is an oligomerized C-type lectin molecule with immunomodulatory properties and involvement in lung surfactant homeostasis in the respiratory tract. SP-D binds to the enveloped viruses, influenza A virus and respiratory syncytial virus and inhibits their replication in vitro and in vivo. SP-D has been shown to bind to HIV via the HIV envelope protein gp120 and inhibit infectivity in vitro. Here we show that SP-D binds to different strains of HIV (BaL and IIIB) and the binding occurs at both pH 7.4 and 5.0 resembling physiological relevant pH values found in the body and the female urogenital tract, respectively. The binding of SP-D to HIV particles and gp120 was inhibited by the presence of several hexoses with mannose found to be the strongest inhibitor. Competition studies showed that soluble CD4 and CVN did not interfere with the interaction between SP-D and gp120. However, soluble recombinant DC-SIGN was shown to inhibit the binding between SP-D and gp120. SP-D agglutinated HIV and gp120 in a calcium dependent manner. SP-D inhibited the infectivity of HIV strains at both pH values of 7.4 and 5.0 in a concentration dependent manner. The inhibition of the infectivity was abolished by the presence of mannose. SP-D enhanced the binding of HIV to immature monocyte derived dendritic cells (iMDDCs) and was also found to enhance HIV capture and transfer to the T-cell like line PM1. These results suggest that SP-D can bind to and inhibit direct infection of T-cells by HIV but also enhance the transfer of infectious HIV particles from DCs to T-cells in vivo.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0059047&type=printable |
| spellingShingle | Jens Madsen Gaurav D Gaiha Nades Palaniyar Tao Dong Daniel A Mitchell Howard W Clark Surfactant Protein D modulates HIV infection of both T-cells and dendritic cells. PLoS ONE |
| title | Surfactant Protein D modulates HIV infection of both T-cells and dendritic cells. |
| title_full | Surfactant Protein D modulates HIV infection of both T-cells and dendritic cells. |
| title_fullStr | Surfactant Protein D modulates HIV infection of both T-cells and dendritic cells. |
| title_full_unstemmed | Surfactant Protein D modulates HIV infection of both T-cells and dendritic cells. |
| title_short | Surfactant Protein D modulates HIV infection of both T-cells and dendritic cells. |
| title_sort | surfactant protein d modulates hiv infection of both t cells and dendritic cells |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0059047&type=printable |
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