Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles

Cell surface receptors for phosphatidylserine contribute to the entry of Ebola virus (EBOV) particles, indicating that the presence of phosphatidylserine in the envelope of EBOV is important for the internalization of EBOV particles. Phosphatidylserine is typically distributed in the inner layer of...

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Published inPLoS pathogens Vol. 14; no. 1; p. e1006848
Main Authors Nanbo, Asuka, Maruyama, Junki, Imai, Masaki, Ujie, Michiko, Fujioka, Yoichiro, Nishide, Shinya, Takada, Ayato, Ohba, Yusuke, Kawaoka, Yoshihiro
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 01.01.2018
Public Library of Science (PLoS)
Subjects
Analysis
Animals
Apoptosis
Biology and life sciences
Budding
Caspase
Cell surface
Cercopithecus aethiops
Ebola virus
Ebolavirus
Ebolavirus - physiology
Endoplasmic reticulum
Epidemics
Epidemiology
Exposure
Funding
Glycoproteins
HEK293 Cells
Hemorrhagic Fever, Ebola - metabolism
Hemorrhagic Fever, Ebola - virology
Host-Pathogen Interactions
Host-virus relationships
Humans
Immunology
Infections
Infectious diseases
Internalization
Intracellular
Life sciences
Matrix protein
Medicine
Medicine and Health Sciences
Membrane vesicles
Membranes
Phosphatidylserine
Phosphatidylserines
Phosphatidylserines - metabolism
Phospholipid Transfer Proteins - physiology
Physiology
Plasma
Progeny
Proteins
R&D
Receptors
Research & development
Research and Analysis Methods
Vero Cells
Vesicles
Viral Core Proteins - metabolism
Virion - metabolism
Virions
Virology
Virus Release
Viruses
VP40 protein
Zoonoses
Japan
Online AccessGet full text

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Abstract Cell surface receptors for phosphatidylserine contribute to the entry of Ebola virus (EBOV) particles, indicating that the presence of phosphatidylserine in the envelope of EBOV is important for the internalization of EBOV particles. Phosphatidylserine is typically distributed in the inner layer of the plasma membrane in normal cells. Progeny virions bud from the plasma membrane of infected cells, suggesting that phosphatidylserine is likely flipped to the outer leaflet of the plasma membrane in infected cells for EBOV virions to acquire it. Currently, the intracellular dynamics of phosphatidylserine during EBOV infection are poorly understood. Here, we explored the role of XK-related protein (Xkr) 8, which is a scramblase responsible for exposure of phosphatidylserine in the plasma membrane of apoptotic cells, to understand its significance in phosphatidylserine-dependent entry of EBOV. We found that Xkr8 and transiently expressed EBOV glycoprotein GP often co-localized in intracellular vesicles and the plasma membrane. We also found that co-expression of GP and viral major matrix protein VP40 promoted incorporation of Xkr8 into ebolavirus-like particles (VLPs) and exposure of phosphatidylserine on their surface, although only a limited amount of phosphatidylserine was exposed on the surface of the cells expressing GP and/or VP40. Downregulating Xkr8 or blocking caspase-mediated Xkr8 activation did not affect VLP production, but they reduced the amount of phosphatidylserine on the VLPs and their uptake in recipient cells. Taken together, our findings indicate that Xkr8 is trafficked to budding sites via GP-containing vesicles, is incorporated into VLPs, and then promote the entry of the released EBOV to cells in a phosphatidylserine-dependent manner.
AbstractList Cell surface receptors for phosphatidylserine contribute to the entry of Ebola virus (EBOV) particles, indicating that the presence of phosphatidylserine in the envelope of EBOV is important for the internalization of EBOV particles. Phosphatidylserine is typically distributed in the inner layer of the plasma membrane in normal cells. Progeny virions bud from the plasma membrane of infected cells, suggesting that phosphatidylserine is likely flipped to the outer leaflet of the plasma membrane in infected cells for EBOV virions to acquire it. Currently, the intracellular dynamics of phosphatidylserine during EBOV infection are poorly understood. Here, we explored the role of XK-related protein (Xkr) 8, which is a scramblase responsible for exposure of phosphatidylserine in the plasma membrane of apoptotic cells, to understand its significance in phosphatidylserine-dependent entry of EBOV. We found that Xkr8 and transiently expressed EBOV glycoprotein GP often co-localized in intracellular vesicles and the plasma membrane. We also found that co-expression of GP and viral major matrix protein VP40 promoted incorporation of Xkr8 into ebolavirus-like particles (VLPs) and exposure of phosphatidylserine on their surface, although only a limited amount of phosphatidylserine was exposed on the surface of the cells expressing GP and/or VP40. Downregulating Xkr8 or blocking caspase-mediated Xkr8 activation did not affect VLP production, but they reduced the amount of phosphatidylserine on the VLPs and their uptake in recipient cells. Taken together, our findings indicate that Xkr8 is trafficked to budding sites via GP-containing vesicles, is incorporated into VLPs, and then promote the entry of the released EBOV to cells in a phosphatidylserine-dependent manner.
Cell surface receptors for phosphatidylserine contribute to the entry of Ebola virus (EBOV) particles, indicating that the presence of phosphatidylserine in the envelope of EBOV is important for the internalization of EBOV particles. Phosphatidylserine is typically distributed in the inner layer of the plasma membrane in normal cells. Progeny virions bud from the plasma membrane of infected cells, suggesting that phosphatidylserine is likely flipped to the outer leaflet of the plasma membrane in infected cells for EBOV virions to acquire it. Currently, the intracellular dynamics of phosphatidylserine during EBOV infection are poorly understood. Here, we explored the role of XK-related protein (Xkr) 8, which is a scramblase responsible for exposure of phosphatidylserine in the plasma membrane of apoptotic cells, to understand its significance in phosphatidylserine-dependent entry of EBOV. We found that Xkr8 and transiently expressed EBOV glycoprotein GP often co-localized in intracellular vesicles and the plasma membrane. We also found that co-expression of GP and viral major matrix protein VP40 promoted incorporation of Xkr8 into ebolavirus-like particles (VLPs) and exposure of phosphatidylserine on their surface, although only a limited amount of phosphatidylserine was exposed on the surface of the cells expressing GP and/or VP40. Downregulating Xkr8 or blocking caspase-mediated Xkr8 activation did not affect VLP production, but they reduced the amount of phosphatidylserine on the VLPs and their uptake in recipient cells. Taken together, our findings indicate that Xkr8 is trafficked to budding sites via GP-containing vesicles, is incorporated into VLPs, and then promote the entry of the released EBOV to cells in a phosphatidylserine-dependent manner. Although Ebola virus causes severe hemorrhagic fever with a high mortality rate, there are no approved therapeutics. The viral entry process is one of the targets for antiviral development. Previous studies suggest that binding of phosphatidylserine, a component of the viral envelop, to the receptors promotes the entry of Ebola virus. Ebola virus is released from the surface membrane of infected cells. However, phosphatidylserine normally distributes in the inner layer of the cell surface membrane, suggesting that phosphatidylserine is likely flipped to the outer leaflet of the membrane in infected cells for Ebola virus to acquire it. Because the mechanism by which phosphatidylserine changes its orientation in Ebola virus-infected cells is poorly understood, we studied and identified a cellular enzyme, XK-related protein 8 (Xkr8), as a responsible factor involved in this process. We demonstrated that the Ebola virus glycoprotein promoted the incorporation of Xkr8 in viral particles, which flips phosphatidylserine on their surface, enhancing their entry to cells. Our findings provide new insights into the mechanism of Ebola virus infection, which may be exploited for the development of therapeutics against Ebola virus infection.
Cell surface receptors for phosphatidylserine contribute to the entry of Ebola virus (EBOV) particles, indicating that the presence of phosphatidylserine in the envelope of EBOV is important for the internalization of EBOV particles. Phosphatidylserine is typically distributed in the inner layer of the plasma membrane in normal cells. Progeny virions bud from the plasma membrane of infected cells, suggesting that phosphatidylserine is likely flipped to the outer leaflet of the plasma membrane in infected cells for EBOV virions to acquire it. Currently, the intracellular dynamics of phosphatidylserine during EBOV infection are poorly understood. Here, we explored the role of XK-related protein (Xkr) 8, which is a scramblase responsible for exposure of phosphatidylserine in the plasma membrane of apoptotic cells, to understand its significance in phosphatidylserine-dependent entry of EBOV. We found that Xkr8 and transiently expressed EBOV glycoprotein GP often co-localized in intracellular vesicles and the plasma membrane. We also found that co-expression of GP and viral major matrix protein VP40 promoted incorporation of Xkr8 into ebolavirus-like particles (VLPs) and exposure of phosphatidylserine on their surface, although only a limited amount of phosphatidylserine was exposed on the surface of the cells expressing GP and/or VP40. Downregulating Xkr8 or blocking caspase-mediated Xkr8 activation did not affect VLP production, but they reduced the amount of phosphatidylserine on the VLPs and their uptake in recipient cells. Taken together, our findings indicate that Xkr8 is trafficked to budding sites via GP-containing vesicles, is incorporated into VLPs, and then promote the entry of the released EBOV to cells in a phosphatidylserine-dependent manner.Cell surface receptors for phosphatidylserine contribute to the entry of Ebola virus (EBOV) particles, indicating that the presence of phosphatidylserine in the envelope of EBOV is important for the internalization of EBOV particles. Phosphatidylserine is typically distributed in the inner layer of the plasma membrane in normal cells. Progeny virions bud from the plasma membrane of infected cells, suggesting that phosphatidylserine is likely flipped to the outer leaflet of the plasma membrane in infected cells for EBOV virions to acquire it. Currently, the intracellular dynamics of phosphatidylserine during EBOV infection are poorly understood. Here, we explored the role of XK-related protein (Xkr) 8, which is a scramblase responsible for exposure of phosphatidylserine in the plasma membrane of apoptotic cells, to understand its significance in phosphatidylserine-dependent entry of EBOV. We found that Xkr8 and transiently expressed EBOV glycoprotein GP often co-localized in intracellular vesicles and the plasma membrane. We also found that co-expression of GP and viral major matrix protein VP40 promoted incorporation of Xkr8 into ebolavirus-like particles (VLPs) and exposure of phosphatidylserine on their surface, although only a limited amount of phosphatidylserine was exposed on the surface of the cells expressing GP and/or VP40. Downregulating Xkr8 or blocking caspase-mediated Xkr8 activation did not affect VLP production, but they reduced the amount of phosphatidylserine on the VLPs and their uptake in recipient cells. Taken together, our findings indicate that Xkr8 is trafficked to budding sites via GP-containing vesicles, is incorporated into VLPs, and then promote the entry of the released EBOV to cells in a phosphatidylserine-dependent manner.
Audience Academic
Author Maruyama, Junki
Ohba, Yusuke
Kawaoka, Yoshihiro
Ujie, Michiko
Fujioka, Yoichiro
Imai, Masaki
Nishide, Shinya
Nanbo, Asuka
Takada, Ayato
AuthorAffiliation University of Texas Medical Branch, UNITED STATES
1 Department of Cell Physiology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo, Hokkaido, Japan
2 Division of Global Epidemiology, Hokkaido University Research Center for Zoonosis Control, Sapporo, Hokkaido, Japan
3 Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo, Japan
5 Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, Wisconsin, United States of America
4 Global Station for Zoonosis Control, Global Institution for Collaborative Research and Education, Hokkaido University, Sapporo, Hokkaido, Japan
6 Department of Special Pathogens, International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Tokyo, Japan
AuthorAffiliation_xml – name: 6 Department of Special Pathogens, International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Tokyo, Japan
– name: 3 Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo, Japan
– name: 2 Division of Global Epidemiology, Hokkaido University Research Center for Zoonosis Control, Sapporo, Hokkaido, Japan
– name: 5 Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, Wisconsin, United States of America
– name: 4 Global Station for Zoonosis Control, Global Institution for Collaborative Research and Education, Hokkaido University, Sapporo, Hokkaido, Japan
– name: University of Texas Medical Branch, UNITED STATES
– name: 1 Department of Cell Physiology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo, Hokkaido, Japan
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/29338048$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright COPYRIGHT 2018 Public Library of Science
2018 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Nanbo A, Maruyama J, Imai M, Ujie M, Fujioka Y, Nishide S, et al. (2018) Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles. PLoS Pathog 14(1): e1006848. https://doi.org/10.1371/journal.ppat.1006848
2018 Nanbo et al 2018 Nanbo et al
2018 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Nanbo A, Maruyama J, Imai M, Ujie M, Fujioka Y, Nishide S, et al. (2018) Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles. PLoS Pathog 14(1): e1006848. https://doi.org/10.1371/journal.ppat.1006848
Copyright_xml – notice: COPYRIGHT 2018 Public Library of Science
– notice: 2018 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Nanbo A, Maruyama J, Imai M, Ujie M, Fujioka Y, Nishide S, et al. (2018) Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles. PLoS Pathog 14(1): e1006848. https://doi.org/10.1371/journal.ppat.1006848
– notice: 2018 Nanbo et al 2018 Nanbo et al
– notice: 2018 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Nanbo A, Maruyama J, Imai M, Ujie M, Fujioka Y, Nishide S, et al. (2018) Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles. PLoS Pathog 14(1): e1006848. https://doi.org/10.1371/journal.ppat.1006848
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Snippet Cell surface receptors for phosphatidylserine contribute to the entry of Ebola virus (EBOV) particles, indicating that the presence of phosphatidylserine in...
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StartPage e1006848
SubjectTerms Analysis
Animals
Apoptosis
Biology and life sciences
Budding
Caspase
Cell surface
Cercopithecus aethiops
Ebola virus
Ebolavirus
Ebolavirus - physiology
Endoplasmic reticulum
Epidemics
Epidemiology
Exposure
Funding
Glycoproteins
HEK293 Cells
Hemorrhagic Fever, Ebola - metabolism
Hemorrhagic Fever, Ebola - virology
Host-Pathogen Interactions
Host-virus relationships
Humans
Immunology
Infections
Infectious diseases
Internalization
Intracellular
Life sciences
Matrix protein
Medicine
Medicine and Health Sciences
Membrane vesicles
Membranes
Phosphatidylserine
Phosphatidylserines
Phosphatidylserines - metabolism
Phospholipid Transfer Proteins - physiology
Physiology
Plasma
Progeny
Proteins
R&D
Receptors
Research & development
Research and Analysis Methods
Vero Cells
Vesicles
Viral Core Proteins - metabolism
Virion - metabolism
Virions
Virology
Virus Release
Viruses
VP40 protein
Zoonoses
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Title Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles
URI https://www.ncbi.nlm.nih.gov/pubmed/29338048
https://www.proquest.com/docview/2002619005
https://www.proquest.com/docview/1989573736
https://pubmed.ncbi.nlm.nih.gov/PMC5786336
https://doaj.org/article/8975f23a30744bbda48001586a239a3d
http://dx.doi.org/10.1371/journal.ppat.1006848
Volume 14
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