NRP2 and CD63 Are Host Factors for Lujo Virus Cell Entry

Arenaviruses cause fatal hemorrhagic disease in humans. Old World arenavirus glycoproteins (GPs) mainly engage α-dystroglycan as a cell-surface receptor, while New World arenaviruses hijack transferrin receptor. However, the Lujo virus (LUJV) GP does not cluster with New or Old World arenaviruses. U...

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Vydáno v:	Cell host & microbe Ročník 22; číslo 5; s. 688
Hlavní autoři:	Raaben, Matthijs, Jae, Lucas T, Herbert, Andrew S, Kuehne, Ana I, Stubbs, Sarah H, Chou, Yi-Ying, Blomen, Vincent A, Kirchhausen, Tomas, Dye, John M, Brummelkamp, Thijn R, Whelan, Sean P
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 08.11.2017
Témata:	Carrier Proteins Cell Line Host-Pathogen Interactions - physiology Human Umbilical Vein Endothelial Cells Humans Lujo virus - genetics Lujo virus - pathogenicity Lujo virus - physiology Neuropilin-2 - metabolism Protein Interaction Domains and Motifs Receptors, Cell Surface - metabolism Receptors, Transferrin Tetraspanin 30 - metabolism Viral Fusion Proteins - genetics Viral Fusion Proteins - metabolism Viral Proteins - genetics Viral Proteins - metabolism Virus Internalization CD63 arenavirus NRP2 Lujo virus LUJV haploid genetics entry receptor
ISSN:	1934-6069, 1934-6069
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Abstract	Arenaviruses cause fatal hemorrhagic disease in humans. Old World arenavirus glycoproteins (GPs) mainly engage α-dystroglycan as a cell-surface receptor, while New World arenaviruses hijack transferrin receptor. However, the Lujo virus (LUJV) GP does not cluster with New or Old World arenaviruses. Using a recombinant vesicular stomatitis virus containing LUJV GP as its sole attachment and fusion protein (VSV-LUJV), we demonstrate that infection is independent of known arenavirus receptor genes. A genome-wide haploid genetic screen identified the transmembrane protein neuropilin 2 (NRP2) and tetraspanin CD63 as factors for LUJV GP-mediated infection. LUJV GP binds the N-terminal domain of NRP2, while CD63 stimulates pH-activated LUJV GP-mediated membrane fusion. Overexpression of NRP2 or its N-terminal domain enhances VSV-LUJV infection, and cells lacking NRP2 are deficient in wild-type LUJV infection. These findings uncover this distinct set of host cell entry factors in LUJV infection and are attractive focus points for therapeutic intervention.
AbstractList	Arenaviruses cause fatal hemorrhagic disease in humans. Old World arenavirus glycoproteins (GPs) mainly engage α-dystroglycan as a cell-surface receptor, while New World arenaviruses hijack transferrin receptor. However, the Lujo virus (LUJV) GP does not cluster with New or Old World arenaviruses. Using a recombinant vesicular stomatitis virus containing LUJV GP as its sole attachment and fusion protein (VSV-LUJV), we demonstrate that infection is independent of known arenavirus receptor genes. A genome-wide haploid genetic screen identified the transmembrane protein neuropilin 2 (NRP2) and tetraspanin CD63 as factors for LUJV GP-mediated infection. LUJV GP binds the N-terminal domain of NRP2, while CD63 stimulates pH-activated LUJV GP-mediated membrane fusion. Overexpression of NRP2 or its N-terminal domain enhances VSV-LUJV infection, and cells lacking NRP2 are deficient in wild-type LUJV infection. These findings uncover this distinct set of host cell entry factors in LUJV infection and are attractive focus points for therapeutic intervention. Arenaviruses cause fatal hemorrhagic disease in humans. Old World arenavirus glycoproteins (GPs) mainly engage α-dystroglycan as a cell-surface receptor, while New World arenaviruses hijack transferrin receptor. However, the Lujo virus (LUJV) GP does not cluster with New or Old World arenaviruses. Using a recombinant vesicular stomatitis virus containing LUJV GP as its sole attachment and fusion protein (VSV-LUJV), we demonstrate that infection is independent of known arenavirus receptor genes. A genome-wide haploid genetic screen identified the transmembrane protein neuropilin 2 (NRP2) and tetraspanin CD63 as factors for LUJV GP-mediated infection. LUJV GP binds the N-terminal domain of NRP2, while CD63 stimulates pH-activated LUJV GP-mediated membrane fusion. Overexpression of NRP2 or its N-terminal domain enhances VSV-LUJV infection, and cells lacking NRP2 are deficient in wild-type LUJV infection. These findings uncover this distinct set of host cell entry factors in LUJV infection and are attractive focus points for therapeutic intervention.Arenaviruses cause fatal hemorrhagic disease in humans. Old World arenavirus glycoproteins (GPs) mainly engage α-dystroglycan as a cell-surface receptor, while New World arenaviruses hijack transferrin receptor. However, the Lujo virus (LUJV) GP does not cluster with New or Old World arenaviruses. Using a recombinant vesicular stomatitis virus containing LUJV GP as its sole attachment and fusion protein (VSV-LUJV), we demonstrate that infection is independent of known arenavirus receptor genes. A genome-wide haploid genetic screen identified the transmembrane protein neuropilin 2 (NRP2) and tetraspanin CD63 as factors for LUJV GP-mediated infection. LUJV GP binds the N-terminal domain of NRP2, while CD63 stimulates pH-activated LUJV GP-mediated membrane fusion. Overexpression of NRP2 or its N-terminal domain enhances VSV-LUJV infection, and cells lacking NRP2 are deficient in wild-type LUJV infection. These findings uncover this distinct set of host cell entry factors in LUJV infection and are attractive focus points for therapeutic intervention.
Author	Herbert, Andrew S Kuehne, Ana I Brummelkamp, Thijn R Chou, Yi-Ying Kirchhausen, Tomas Raaben, Matthijs Stubbs, Sarah H Dye, John M Whelan, Sean P Jae, Lucas T Blomen, Vincent A
Author_xml	– sequence: 1 givenname: Matthijs surname: Raaben fullname: Raaben, Matthijs organization: Division of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, the Netherlands; Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA – sequence: 2 givenname: Lucas T surname: Jae fullname: Jae, Lucas T organization: Division of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, the Netherlands; Gene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany – sequence: 3 givenname: Andrew S surname: Herbert fullname: Herbert, Andrew S organization: U.S. Army Medical Research Institute of Infectious Diseases, Virology Division, 1425 Porter Street, Fort Detrick, MD 21702-5011, USA – sequence: 4 givenname: Ana I surname: Kuehne fullname: Kuehne, Ana I organization: U.S. Army Medical Research Institute of Infectious Diseases, Virology Division, 1425 Porter Street, Fort Detrick, MD 21702-5011, USA – sequence: 5 givenname: Sarah H surname: Stubbs fullname: Stubbs, Sarah H organization: Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA – sequence: 6 givenname: Yi-Ying surname: Chou fullname: Chou, Yi-Ying organization: Department of Cell Biology, Harvard Medical School, and Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA – sequence: 7 givenname: Vincent A surname: Blomen fullname: Blomen, Vincent A organization: Division of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, the Netherlands – sequence: 8 givenname: Tomas surname: Kirchhausen fullname: Kirchhausen, Tomas organization: Department of Cell Biology, Harvard Medical School, and Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA – sequence: 9 givenname: John M surname: Dye fullname: Dye, John M organization: U.S. Army Medical Research Institute of Infectious Diseases, Virology Division, 1425 Porter Street, Fort Detrick, MD 21702-5011, USA – sequence: 10 givenname: Thijn R surname: Brummelkamp fullname: Brummelkamp, Thijn R email: t.brummelkamp@nki.nl organization: Division of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, the Netherlands; CGC.nl; CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 14 Vienna, Austria. Electronic address: t.brummelkamp@nki.nl – sequence: 11 givenname: Sean P surname: Whelan fullname: Whelan, Sean P email: sean_whelan@hms.harvard.edu organization: Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: sean_whelan@hms.harvard.edu
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SubjectTerms	Carrier Proteins Cell Line Host-Pathogen Interactions - physiology Human Umbilical Vein Endothelial Cells Humans Lujo virus - genetics Lujo virus - pathogenicity Lujo virus - physiology Neuropilin-2 - metabolism Protein Interaction Domains and Motifs Receptors, Cell Surface - metabolism Receptors, Transferrin Tetraspanin 30 - metabolism Viral Fusion Proteins - genetics Viral Fusion Proteins - metabolism Viral Proteins - genetics Viral Proteins - metabolism Virus Internalization
Title	NRP2 and CD63 Are Host Factors for Lujo Virus Cell Entry
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