Oligomerization of the Macrophage Mannose Receptor Enhances gp120-mediated Binding of HIV-1
C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose, and N-acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin on dend...
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Published in | The Journal of biological chemistry Vol. 284; no. 17; pp. 11027 - 11038 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
24.04.2009
American Society for Biochemistry and Molecular Biology |
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Abstract | C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose, and N-acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin on dendritic cells, and mannose receptor (MR) on dendritic cells and macrophages bind the human immunodeficiency virus (HIV) envelope protein gp120 principally via high mannose oligosaccharides. These C-type lectin receptors can also oligomerize to facilitate enhanced ligand binding. This study examined the effect of oligomerization of MR on its ability to bind to mannan, monomeric gp120, native trimeric gp140, and HIV type 1 BaL. Mass spectrometry analysis of cross-linked MR showed homodimerization on the surface of primary monocyte-derived dendritic cells and macrophages. Both monomeric and dimeric MR were precipitated by mannan, but only the dimeric form was co-immunoprecipitated by gp120. These results were confirmed independently by flow cytometry analysis of soluble monomeric and trimeric HIV envelope and a cellular HIV virion capture assay. As expected, mannan bound to the carbohydrate recognition domains of MR dimers mostly in a calcium-dependent fashion. Unexpectedly, gp120-mediated binding of HIV to dimers on MR-transfected Rat-6 cells and macrophages was not calcium-dependent, was only partially blocked by mannan, and was also partially inhibited by N-acetylgalactosamine 4-sulfate. Thus gp120-mediated HIV binding occurs via the calcium-dependent, non-calcium-dependent carbohydrate recognition domains and the cysteine-rich domain at the C terminus of MR dimers, presenting a much broader target for potential inhibitors of gp120-MR binding. |
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AbstractList | C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial
pathogens via mannose, fucose, and N -acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin
on dendritic cells, and mannose receptor (MR) on dendritic cells and macrophages bind the human immunodeficiency virus (HIV)
envelope protein gp120 principally via high mannose oligosaccharides. These C-type lectin receptors can also oligomerize to
facilitate enhanced ligand binding. This study examined the effect of oligomerization of MR on its ability to bind to mannan,
monomeric gp120, native trimeric gp140, and HIV type 1 BaL. Mass spectrometry analysis of cross-linked MR showed homodimerization
on the surface of primary monocyte-derived dendritic cells and macrophages. Both monomeric and dimeric MR were precipitated
by mannan, but only the dimeric form was co-immunoprecipitated by gp120. These results were confirmed independently by flow
cytometry analysis of soluble monomeric and trimeric HIV envelope and a cellular HIV virion capture assay. As expected, mannan
bound to the carbohydrate recognition domains of MR dimers mostly in a calcium-dependent fashion. Unexpectedly, gp120-mediated
binding of HIV to dimers on MR-transfected Rat-6 cells and macrophages was not calcium-dependent, was only partially blocked
by mannan, and was also partially inhibited by N -acetylgalactosamine 4-sulfate. Thus gp120-mediated HIV binding occurs via the calcium-dependent, non-calcium-dependent carbohydrate
recognition domains and the cysteine-rich domain at the C terminus of MR dimers, presenting a much broader target for potential
inhibitors of gp120-MR binding. C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose, and N-acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin on dendritic cells, and mannose receptor (MR) on dendritic cells and macrophages bind the human immunodeficiency virus (HIV) envelope protein gp120 principally via high mannose oligosaccharides. These C-type lectin receptors can also oligomerize to facilitate enhanced ligand binding. This study examined the effect of oligomerization of MR on its ability to bind to mannan, monomeric gp120, native trimeric gp140, and HIV type 1 BaL. Mass spectrometry analysis of cross-linked MR showed homodimerization on the surface of primary monocyte-derived dendritic cells and macrophages. Both monomeric and dimeric MR were precipitated by mannan, but only the dimeric form was co-immunoprecipitated by gp120. These results were confirmed independently by flow cytometry analysis of soluble monomeric and trimeric HIV envelope and a cellular HIV virion capture assay. As expected, mannan bound to the carbohydrate recognition domains of MR dimers mostly in a calcium-dependent fashion. Unexpectedly, gp120-mediated binding of HIV to dimers on MR-transfected Rat-6 cells and macrophages was not calcium-dependent, was only partially blocked by mannan, and was also partially inhibited by N-acetylgalactosamine 4-sulfate. Thus gp120-mediated HIV binding occurs via the calcium-dependent, non-calcium-dependent carbohydrate recognition domains and the cysteine-rich domain at the C terminus of MR dimers, presenting a much broader target for potential inhibitors of gp120-MR binding. C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose, and N -acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin on dendritic cells, and mannose receptor (MR) on dendritic cells and macrophages bind the human immunodeficiency virus (HIV) envelope protein gp120 principally via high mannose oligosaccharides. These C-type lectin receptors can also oligomerize to facilitate enhanced ligand binding. This study examined the effect of oligomerization of MR on its ability to bind to mannan, monomeric gp120, native trimeric gp140, and HIV type 1 BaL. Mass spectrometry analysis of cross-linked MR showed homodimerization on the surface of primary monocyte-derived dendritic cells and macrophages. Both monomeric and dimeric MR were precipitated by mannan, but only the dimeric form was co-immunoprecipitated by gp120. These results were confirmed independently by flow cytometry analysis of soluble monomeric and trimeric HIV envelope and a cellular HIV virion capture assay. As expected, mannan bound to the carbohydrate recognition domains of MR dimers mostly in a calcium-dependent fashion. Unexpectedly, gp120-mediated binding of HIV to dimers on MR-transfected Rat-6 cells and macrophages was not calcium-dependent, was only partially blocked by mannan, and was also partially inhibited by N -acetylgalactosamine 4-sulfate. Thus gp120-mediated HIV binding occurs via the calcium-dependent, non-calcium-dependent carbohydrate recognition domains and the cysteine-rich domain at the C terminus of MR dimers, presenting a much broader target for potential inhibitors of gp120-MR binding. C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose, and N-acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin on dendritic cells, and mannose receptor (MR) on dendritic cells and macrophages bind the human immunodeficiency virus (HIV) envelope protein gp120 principally via high mannose oligosaccharides. These C-type lectin receptors can also oligomerize to facilitate enhanced ligand binding. This study examined the effect of oligomerization of MR on its ability to bind to mannan, monomeric gp120, native trimeric gp140, and HIV type 1 BaL. Mass spectrometry analysis of cross-linked MR showed homodimerization on the surface of primary monocyte-derived dendritic cells and macrophages. Both monomeric and dimeric MR were precipitated by mannan, but only the dimeric form was co-immunoprecipitated by gp120. These results were confirmed independently by flow cytometry analysis of soluble monomeric and trimeric HIV envelope and a cellular HIV virion capture assay. As expected, mannan bound to the carbohydrate recognition domains of MR dimers mostly in a calcium-dependent fashion. Unexpectedly, gp120-mediated binding of HIV to dimers on MR-transfected Rat-6 cells and macrophages was not calcium-dependent, was only partially blocked by mannan, and was also partially inhibited by N-acetylgalactosamine 4-sulfate. Thus gp120-mediated HIV binding occurs via the calcium-dependent, non-calcium-dependent carbohydrate recognition domains and the cysteine-rich domain at the C terminus of MR dimers, presenting a much broader target for potential inhibitors of gp120-MR binding.C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose, and N-acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin on dendritic cells, and mannose receptor (MR) on dendritic cells and macrophages bind the human immunodeficiency virus (HIV) envelope protein gp120 principally via high mannose oligosaccharides. These C-type lectin receptors can also oligomerize to facilitate enhanced ligand binding. This study examined the effect of oligomerization of MR on its ability to bind to mannan, monomeric gp120, native trimeric gp140, and HIV type 1 BaL. Mass spectrometry analysis of cross-linked MR showed homodimerization on the surface of primary monocyte-derived dendritic cells and macrophages. Both monomeric and dimeric MR were precipitated by mannan, but only the dimeric form was co-immunoprecipitated by gp120. These results were confirmed independently by flow cytometry analysis of soluble monomeric and trimeric HIV envelope and a cellular HIV virion capture assay. As expected, mannan bound to the carbohydrate recognition domains of MR dimers mostly in a calcium-dependent fashion. Unexpectedly, gp120-mediated binding of HIV to dimers on MR-transfected Rat-6 cells and macrophages was not calcium-dependent, was only partially blocked by mannan, and was also partially inhibited by N-acetylgalactosamine 4-sulfate. Thus gp120-mediated HIV binding occurs via the calcium-dependent, non-calcium-dependent carbohydrate recognition domains and the cysteine-rich domain at the C terminus of MR dimers, presenting a much broader target for potential inhibitors of gp120-MR binding. |
Author | Harman, Andrew N. Bernhard, Oliver K. Turville, Stuart G. Lai, Joey Wilkinson, John Cunningham, Anthony L. |
AuthorAffiliation | Centre for Virus Research, Westmead Millennium Institute, Westmead Hospital, Westmead, Sydney, New South Wales 2145 and the § Joint Proteomics Laboratory, Ludwig Institute for Cancer Research, Parkville, Melbourne, Victoria 3050, Australia |
AuthorAffiliation_xml | – name: Centre for Virus Research, Westmead Millennium Institute, Westmead Hospital, Westmead, Sydney, New South Wales 2145 and the § Joint Proteomics Laboratory, Ludwig Institute for Cancer Research, Parkville, Melbourne, Victoria 3050, Australia |
Author_xml | – sequence: 1 givenname: Joey surname: Lai fullname: Lai, Joey organization: Centre for Virus Research, Westmead Millennium Institute, Westmead Hospital, Westmead, Sydney, New South Wales 2145 – sequence: 2 givenname: Oliver K. surname: Bernhard fullname: Bernhard, Oliver K. organization: Joint Proteomics Laboratory, Ludwig Institute for Cancer Research, Parkville, Melbourne, Victoria 3050, Australia – sequence: 3 givenname: Stuart G. surname: Turville fullname: Turville, Stuart G. organization: Centre for Virus Research, Westmead Millennium Institute, Westmead Hospital, Westmead, Sydney, New South Wales 2145 – sequence: 4 givenname: Andrew N. surname: Harman fullname: Harman, Andrew N. organization: Centre for Virus Research, Westmead Millennium Institute, Westmead Hospital, Westmead, Sydney, New South Wales 2145 – sequence: 5 givenname: John surname: Wilkinson fullname: Wilkinson, John organization: Centre for Virus Research, Westmead Millennium Institute, Westmead Hospital, Westmead, Sydney, New South Wales 2145 – sequence: 6 givenname: Anthony L. surname: Cunningham fullname: Cunningham, Anthony L. email: tony_cunningham@wmi.usyd.edu.au organization: Centre for Virus Research, Westmead Millennium Institute, Westmead Hospital, Westmead, Sydney, New South Wales 2145 |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19224860$$D View this record in MEDLINE/PubMed |
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Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 To whom correspondence should be addressed. Tel.: 612-9845-9005; Fax: 612-9845-9100; E-mail: tony_cunningham@wmi.usyd.edu.au. |
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Snippet | C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose,... C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose,... C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose,... |
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SubjectTerms | Acetylgalactosamine - metabolism Animals Calcium Calcium - metabolism Carbohydrates Cell adhesion molecules Cross-Linking Reagents - chemistry Cysteine - metabolism Dendritic cells Dimerization Envelope protein Flow Cytometry fucose Glycoprotein gp120 HIV Envelope Protein gp120 - metabolism HIV-1 - metabolism Human immunodeficiency virus 1 Humans Langerhans cells Langerhans Cells - metabolism Langerhans Cells - virology Lectins Lectins, C-Type - chemistry Lectins, C-Type - metabolism Macrophages Macrophages - metabolism Macrophages - virology mannan Mannose Mannose Receptor Mannose receptors Mannose-Binding Lectins - chemistry Mannose-Binding Lectins - metabolism Mass spectroscopy Monocytes N-Acetylgalactosamine N-Acetylglucosamine Oligomerization oligosaccharides Oligosaccharides - metabolism Pathogens Protein Structure and Folding Rats Receptors, Cell Surface - chemistry Receptors, Cell Surface - metabolism Virions |
Title | Oligomerization of the Macrophage Mannose Receptor Enhances gp120-mediated Binding of HIV-1 |
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