| Respiratory Syncytial Virus G Glycoprotein Interacts with DC-SIGN and L-SIGN to Activate ERK1 and ERK2. | |
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MedLine Citation:
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PMID: 22090124 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Respiratory syncytial virus (RSV) interaction with epithelial and dendritic cells (DC) is known to require divalent cations suggesting involvement of C-type lectins. RSV infection and maturation of primary human DCs are reduced in a dose-dependent manner by EDTA. Therefore, we asked whether RSV infection involves DC-SIGN (CD209) or its isoform L-SIGN (CD299, DC-SIGN/R). Using surface plasmon resonance analysis, we demonstrated that the attachment G glycoprotein of RSV binds both DC- and L-SIGN. However, neutralization of DC- and L-SIGN on primary human DCs did not inhibit RSV infection, demonstrating interactions between RSV G and DC- or L-SIGN are not required for productive infection. Thus, neither DC- nor L-SIGN represents a functional receptor for RSV. However, inhibition of these interactions increased DC activation as evidenced by significantly higher levels of IFN-α, MIP-1α, and MIP-1β in pDCs exposed to RSV after neutralization of DC-and L-SIGN. To understand the molecular interactions involved, intracellular signaling events triggered by purified RSV G glycoprotein were examined in DC- and L-SIGN transfected 3T3 cells. RSV G interaction with DC- or L-SIGN was shown to stimulate ERK1 and ERK2 phosphorylation with statistically significant increases relative to mock-infected cells. Neutralization of DC- and L-SIGN reduced ERK1/2 phosphorylation. With increased DC activation following DC- and L-SIGN neutralization and RSV exposure, these data demonstrate that the signaling events mediated by RSV G interactions with DC/L-SIGN are immunomodulatory and diminish DC activation which may limit induction of RSV-specific immunity. |
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Authors:
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Teresa R Johnson; Jason S McLellan; Barney S Graham |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-11-16 |
Journal Detail:
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Title: Journal of virology Volume: - ISSN: 1098-5514 ISO Abbreviation: - Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-17 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0113724 Medline TA: J Virol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Viral Pathogenesis Laboratory. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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