The mannose receptor mediates dengue virus infection of macrophages

Joanna L. Miller; Barend J.M. DeWet; Luisa Martinez-Pomares; Catherine M. Radcliffe; Raymond A. Dwek; Pauline M. Rudd; Siamon Gordon

doi:10.1371/journal.ppat.0040017

The mannose receptor mediates dengue virus infection of macrophages

Joanna L. Miller, Barend J.M. DeWet, Luisa Martinez-Pomares, Catherine M. Radcliffe, Raymond A. Dwek, Pauline M. Rudd, Siamon Gordon^*

^*Corresponding author for this work

Research output: Contribution to journal › Journal Article › peer-review

354 Scopus citations

Abstract

Macrophages (MØ) and mononuclear phagocytes are major targets of infection by dengue virus (DV), a mosquito-borne flavivirus that can cause haemorrhagic fever in humans. To our knowledge, we show for the first time that the MØ mannose receptor (MR) binds to all four serotypes of DV and specifically to the envelope glycoprotein. Glycan analysis, ELISA, and blot overlay assays demonstrate that MR binds via its carbohydrate recognition domains to mosquito and human cell-produced DV antigen. This binding is abrogated by deglycosylation of the DV envelope glycoprotein. Surface expression of recombinant MR on NIH3T3 cells confers DV binding. Furthermore, DV infection of primary human MØ can be blocked by anti-MR antibodies. MR is a prototypic marker of alternatively activated MØ, and pre-treatment of human monocytes or MØ with type 2 cytokines (IL-4 or IL-13) enhances their susceptibility to productive DV infection. Our findings indicate a new functional role for the MR in DV infection.

Original language	English
Journal	PLoS Pathogens
Volume	4
Issue number	2
DOIs	https://doi.org/10.1371/journal.ppat.0040017
State	Published - 02 2008
Externally published	Yes

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title = "The mannose receptor mediates dengue virus infection of macrophages",

abstract = "Macrophages (M{\O}) and mononuclear phagocytes are major targets of infection by dengue virus (DV), a mosquito-borne flavivirus that can cause haemorrhagic fever in humans. To our knowledge, we show for the first time that the M{\O} mannose receptor (MR) binds to all four serotypes of DV and specifically to the envelope glycoprotein. Glycan analysis, ELISA, and blot overlay assays demonstrate that MR binds via its carbohydrate recognition domains to mosquito and human cell-produced DV antigen. This binding is abrogated by deglycosylation of the DV envelope glycoprotein. Surface expression of recombinant MR on NIH3T3 cells confers DV binding. Furthermore, DV infection of primary human M{\O} can be blocked by anti-MR antibodies. MR is a prototypic marker of alternatively activated M{\O}, and pre-treatment of human monocytes or M{\O} with type 2 cytokines (IL-4 or IL-13) enhances their susceptibility to productive DV infection. Our findings indicate a new functional role for the MR in DV infection.",

author = "Miller, {Joanna L.} and DeWet, {Barend J.M.} and Luisa Martinez-Pomares and Radcliffe, {Catherine M.} and Dwek, {Raymond A.} and Rudd, {Pauline M.} and Siamon Gordon",

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AU - Miller, Joanna L.

AU - DeWet, Barend J.M.

AU - Martinez-Pomares, Luisa

AU - Radcliffe, Catherine M.

AU - Dwek, Raymond A.

AU - Rudd, Pauline M.

AU - Gordon, Siamon

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N2 - Macrophages (MØ) and mononuclear phagocytes are major targets of infection by dengue virus (DV), a mosquito-borne flavivirus that can cause haemorrhagic fever in humans. To our knowledge, we show for the first time that the MØ mannose receptor (MR) binds to all four serotypes of DV and specifically to the envelope glycoprotein. Glycan analysis, ELISA, and blot overlay assays demonstrate that MR binds via its carbohydrate recognition domains to mosquito and human cell-produced DV antigen. This binding is abrogated by deglycosylation of the DV envelope glycoprotein. Surface expression of recombinant MR on NIH3T3 cells confers DV binding. Furthermore, DV infection of primary human MØ can be blocked by anti-MR antibodies. MR is a prototypic marker of alternatively activated MØ, and pre-treatment of human monocytes or MØ with type 2 cytokines (IL-4 or IL-13) enhances their susceptibility to productive DV infection. Our findings indicate a new functional role for the MR in DV infection.

AB - Macrophages (MØ) and mononuclear phagocytes are major targets of infection by dengue virus (DV), a mosquito-borne flavivirus that can cause haemorrhagic fever in humans. To our knowledge, we show for the first time that the MØ mannose receptor (MR) binds to all four serotypes of DV and specifically to the envelope glycoprotein. Glycan analysis, ELISA, and blot overlay assays demonstrate that MR binds via its carbohydrate recognition domains to mosquito and human cell-produced DV antigen. This binding is abrogated by deglycosylation of the DV envelope glycoprotein. Surface expression of recombinant MR on NIH3T3 cells confers DV binding. Furthermore, DV infection of primary human MØ can be blocked by anti-MR antibodies. MR is a prototypic marker of alternatively activated MØ, and pre-treatment of human monocytes or MØ with type 2 cytokines (IL-4 or IL-13) enhances their susceptibility to productive DV infection. Our findings indicate a new functional role for the MR in DV infection.

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The mannose receptor mediates dengue virus infection of macrophages

Abstract

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