Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.

Herpes simplex virus type-1 expresses a heterodimeric Fc receptor, gE-gI, on the surfaces of virions and infected cells that binds the Fc region of host immunoglobulin G and is implicated in the cell-to-cell spread of virus. gE-gI binds immunoglobulin G at the basic pH of the cell surface and releas...

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Autores principales:	Elizabeth R Sprague, Chu Wang, David Baker, Pamela J Bjorkman
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2006
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/28f7ba86feca4ea9b79232413f4a1c09
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spelling	oai:doaj.org-article:28f7ba86feca4ea9b79232413f4a1c092021-11-25T05:33:09ZCrystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.1544-91731545-788510.1371/journal.pbio.0040148https://doaj.org/article/28f7ba86feca4ea9b79232413f4a1c092006-06-01T00:00:00Zhttps://doi.org/10.1371/journal.pbio.0040148https://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Herpes simplex virus type-1 expresses a heterodimeric Fc receptor, gE-gI, on the surfaces of virions and infected cells that binds the Fc region of host immunoglobulin G and is implicated in the cell-to-cell spread of virus. gE-gI binds immunoglobulin G at the basic pH of the cell surface and releases it at the acidic pH of lysosomes, consistent with a role in facilitating the degradation of antiviral antibodies. Here we identify the C-terminal domain of the gE ectodomain (CgE) as the minimal Fc-binding domain and present a 1.78-angstroms CgE structure. A 5-angstroms gE-gI/Fc crystal structure, which was independently verified by a theoretical prediction method, reveals that CgE binds Fc at the C(H)2-C(H)3 interface, the binding site for several mammalian and bacterial Fc-binding proteins. The structure identifies interface histidines that may confer pH-dependent binding and regions of CgE implicated in cell-to-cell spread of virus. The ternary organization of the gE-gI/Fc complex is compatible with antibody bipolar bridging, which can interfere with the antiviral immune response.Elizabeth R SpragueChu WangDavid BakerPamela J BjorkmanPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 4, Iss 6, p e148 (2006)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Elizabeth R Sprague Chu Wang David Baker Pamela J Bjorkman Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.
description	Herpes simplex virus type-1 expresses a heterodimeric Fc receptor, gE-gI, on the surfaces of virions and infected cells that binds the Fc region of host immunoglobulin G and is implicated in the cell-to-cell spread of virus. gE-gI binds immunoglobulin G at the basic pH of the cell surface and releases it at the acidic pH of lysosomes, consistent with a role in facilitating the degradation of antiviral antibodies. Here we identify the C-terminal domain of the gE ectodomain (CgE) as the minimal Fc-binding domain and present a 1.78-angstroms CgE structure. A 5-angstroms gE-gI/Fc crystal structure, which was independently verified by a theoretical prediction method, reveals that CgE binds Fc at the C(H)2-C(H)3 interface, the binding site for several mammalian and bacterial Fc-binding proteins. The structure identifies interface histidines that may confer pH-dependent binding and regions of CgE implicated in cell-to-cell spread of virus. The ternary organization of the gE-gI/Fc complex is compatible with antibody bipolar bridging, which can interfere with the antiviral immune response.
format	article
author	Elizabeth R Sprague Chu Wang David Baker Pamela J Bjorkman
author_facet	Elizabeth R Sprague Chu Wang David Baker Pamela J Bjorkman
author_sort	Elizabeth R Sprague
title	Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.
title_short	Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.
title_full	Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.
title_fullStr	Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.
title_full_unstemmed	Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.
title_sort	crystal structure of the hsv-1 fc receptor bound to fc reveals a mechanism for antibody bipolar bridging.
publisher	Public Library of Science (PLoS)
publishDate	2006
url	https://doaj.org/article/28f7ba86feca4ea9b79232413f4a1c09
work_keys_str_mv	AT elizabethrsprague crystalstructureofthehsv1fcreceptorboundtofcrevealsamechanismforantibodybipolarbridging AT chuwang crystalstructureofthehsv1fcreceptorboundtofcrevealsamechanismforantibodybipolarbridging AT davidbaker crystalstructureofthehsv1fcreceptorboundtofcrevealsamechanismforantibodybipolarbridging AT pamelajbjorkman crystalstructureofthehsv1fcreceptorboundtofcrevealsamechanismforantibodybipolarbridging
_version_	1718414626294595584

Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging.

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