TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.

Human T-cell Immunoglobulin and Mucin-domain containing proteins (TIM1, 3, and 4) specifically bind phosphatidylserine (PS). TIM1 has been proposed to serve as a cellular receptor for hepatitis A virus and Ebola virus and as an entry factor for dengue virus. Here we show that TIM1 promotes infection...

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Autores principales:	Stephanie Jemielity, Jinyize J Wang, Ying Kai Chan, Asim A Ahmed, Wenhui Li, Sheena Monahan, Xia Bu, Michael Farzan, Gordon J Freeman, Dale T Umetsu, Rosemarie H Dekruyff, Hyeryun Choe
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/3e0b25be82fb4447a20dffe357f3ec19
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spelling	oai:doaj.org-article:3e0b25be82fb4447a20dffe357f3ec192021-11-18T06:05:52ZTIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.1553-73661553-737410.1371/journal.ppat.1003232https://doaj.org/article/3e0b25be82fb4447a20dffe357f3ec192013-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23555248/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Human T-cell Immunoglobulin and Mucin-domain containing proteins (TIM1, 3, and 4) specifically bind phosphatidylserine (PS). TIM1 has been proposed to serve as a cellular receptor for hepatitis A virus and Ebola virus and as an entry factor for dengue virus. Here we show that TIM1 promotes infection of retroviruses and virus-like particles (VLPs) pseudotyped with a range of viral entry proteins, in particular those from the filovirus, flavivirus, New World arenavirus and alphavirus families. TIM1 also robustly enhanced the infection of replication-competent viruses from the same families, including dengue, Tacaribe, Sindbis and Ross River viruses. All interactions between TIM1 and pseudoviruses or VLPs were PS-mediated, as demonstrated with liposome blocking and TIM1 mutagenesis experiments. In addition, other PS-binding proteins, such as Axl and TIM4, promoted infection similarly to TIM1. Finally, the blocking of PS receptors on macrophages inhibited the entry of Ebola VLPs, suggesting that PS receptors can contribute to infection in physiologically relevant cells. Notably, infection mediated by the entry proteins of Lassa fever virus, influenza A virus and SARS coronavirus was largely unaffected by TIM1 expression. Taken together our data show that TIM1 and related PS-binding proteins promote infection of diverse families of enveloped viruses, and may therefore be useful targets for broad-spectrum antiviral therapies.Stephanie JemielityJinyize J WangYing Kai ChanAsim A AhmedWenhui LiSheena MonahanXia BuMichael FarzanGordon J FreemanDale T UmetsuRosemarie H DekruyffHyeryun ChoePublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 3, p e1003232 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Stephanie Jemielity Jinyize J Wang Ying Kai Chan Asim A Ahmed Wenhui Li Sheena Monahan Xia Bu Michael Farzan Gordon J Freeman Dale T Umetsu Rosemarie H Dekruyff Hyeryun Choe TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
description	Human T-cell Immunoglobulin and Mucin-domain containing proteins (TIM1, 3, and 4) specifically bind phosphatidylserine (PS). TIM1 has been proposed to serve as a cellular receptor for hepatitis A virus and Ebola virus and as an entry factor for dengue virus. Here we show that TIM1 promotes infection of retroviruses and virus-like particles (VLPs) pseudotyped with a range of viral entry proteins, in particular those from the filovirus, flavivirus, New World arenavirus and alphavirus families. TIM1 also robustly enhanced the infection of replication-competent viruses from the same families, including dengue, Tacaribe, Sindbis and Ross River viruses. All interactions between TIM1 and pseudoviruses or VLPs were PS-mediated, as demonstrated with liposome blocking and TIM1 mutagenesis experiments. In addition, other PS-binding proteins, such as Axl and TIM4, promoted infection similarly to TIM1. Finally, the blocking of PS receptors on macrophages inhibited the entry of Ebola VLPs, suggesting that PS receptors can contribute to infection in physiologically relevant cells. Notably, infection mediated by the entry proteins of Lassa fever virus, influenza A virus and SARS coronavirus was largely unaffected by TIM1 expression. Taken together our data show that TIM1 and related PS-binding proteins promote infection of diverse families of enveloped viruses, and may therefore be useful targets for broad-spectrum antiviral therapies.
format	article
author	Stephanie Jemielity Jinyize J Wang Ying Kai Chan Asim A Ahmed Wenhui Li Sheena Monahan Xia Bu Michael Farzan Gordon J Freeman Dale T Umetsu Rosemarie H Dekruyff Hyeryun Choe
author_facet	Stephanie Jemielity Jinyize J Wang Ying Kai Chan Asim A Ahmed Wenhui Li Sheena Monahan Xia Bu Michael Farzan Gordon J Freeman Dale T Umetsu Rosemarie H Dekruyff Hyeryun Choe
author_sort	Stephanie Jemielity
title	TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
title_short	TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
title_full	TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
title_fullStr	TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
title_full_unstemmed	TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
title_sort	tim-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/3e0b25be82fb4447a20dffe357f3ec19
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TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.

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