Characterization of the Envelope Glycoprotein of a Novel Filovirus, Lloviu Virus

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Published inJournal of Virology Vol. 88; no. 1; pp. 99 - 109
Main Authors Maruyama, Junki, Miyamoto, Hiroko, Kajihara, Masahiro, Ogawa, Hirohito, Maeda, Ken, Sakoda, Yoshihiro, Yoshida, Reiko, Takada, Ayato
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.01.2014
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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList Lloviu virus (LLOV), a novel filovirus detected in bats, is phylogenetically distinct from viruses in the genera Ebolavirus and Marburgvirus in the family Filoviridae . While filoviruses are known to cause severe hemorrhagic fever in humans and/or nonhuman primates, LLOV is biologically uncharacterized, since infectious LLOV has never been isolated. To examine the properties of LLOV, we characterized its envelope glycoprotein (GP), which likely plays a key role in viral tropism and pathogenicity. We first found that LLOV GP principally has the same primary structure as the other filovirus GPs. Similar to the other filoviruses, virus-like particles (VLPs) produced by transient expression of LLOV GP, matrix protein, and nucleoprotein in 293T cells had densely arrayed GP spikes on a filamentous particle. Mouse antiserum to LLOV VLP was barely cross-reactive to viruses of the other genera, indicating that LLOV is serologically distinct from the other known filoviruses. For functional study of LLOV GP, we utilized a vesicular stomatitis virus (VSV) pseudotype system and found that LLOV GP requires low endosomal pH and cathepsin L, and that human C-type lectins act as attachment factors for LLOV entry into cells. Interestingly, LLOV GP-pseudotyped VSV infected particular bat cell lines more efficiently than viruses bearing other filovirus GPs. These results suggest that LLOV GP mediates cellular entry in a manner similar to that of the other filoviruses while showing preferential tropism for some bat cells.
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Lloviu virus (LLOV), a novel filovirus detected in bats, is phylogenetically distinct from viruses in the genera Ebolavirus and Marburgvirus in the family Filoviridae. While filoviruses are known to cause severe hemorrhagic fever in humans and/or nonhuman primates, LLOV is biologically uncharacterized, since infectious LLOV has never been isolated. To examine the properties of LLOV, we characterized its envelope glycoprotein (GP), which likely plays a key role in viral tropism and pathogenicity. We first found that LLOV GP principally has the same primary structure as the other filovirus GPs. Similar to the other filoviruses, virus-like particles (VLPs) produced by transient expression of LLOV GP, matrix protein, and nucleoprotein in 293T cells had densely arrayed GP spikes on a filamentous particle. Mouse antiserum to LLOV VLP was barely cross-reactive to viruses of the other genera, indicating that LLOV is serologically distinct from the other known filoviruses. For functional study of LLOV GP, we utilized a vesicular stomatitis virus (VSV) pseudotype system and found that LLOV GP requires low endosomal pH and cathepsin L, and that human C-type lectins act as attachment factors for LLOV entry into cells. Interestingly, LLOV GP-pseudotyped VSV infected particular bat cell lines more efficiently than viruses bearing other filovirus GPs. These results suggest that LLOV GP mediates cellular entry in a manner similar to that of the other filoviruses while showing preferential tropism for some bat cells.Lloviu virus (LLOV), a novel filovirus detected in bats, is phylogenetically distinct from viruses in the genera Ebolavirus and Marburgvirus in the family Filoviridae. While filoviruses are known to cause severe hemorrhagic fever in humans and/or nonhuman primates, LLOV is biologically uncharacterized, since infectious LLOV has never been isolated. To examine the properties of LLOV, we characterized its envelope glycoprotein (GP), which likely plays a key role in viral tropism and pathogenicity. We first found that LLOV GP principally has the same primary structure as the other filovirus GPs. Similar to the other filoviruses, virus-like particles (VLPs) produced by transient expression of LLOV GP, matrix protein, and nucleoprotein in 293T cells had densely arrayed GP spikes on a filamentous particle. Mouse antiserum to LLOV VLP was barely cross-reactive to viruses of the other genera, indicating that LLOV is serologically distinct from the other known filoviruses. For functional study of LLOV GP, we utilized a vesicular stomatitis virus (VSV) pseudotype system and found that LLOV GP requires low endosomal pH and cathepsin L, and that human C-type lectins act as attachment factors for LLOV entry into cells. Interestingly, LLOV GP-pseudotyped VSV infected particular bat cell lines more efficiently than viruses bearing other filovirus GPs. These results suggest that LLOV GP mediates cellular entry in a manner similar to that of the other filoviruses while showing preferential tropism for some bat cells.
Lloviu virus (LLOV), a novel filovirus detected in bats, is phylogenetically distinct from viruses in the genera Ebolavirus and Marburgvirus in the family Filoviridae. While filoviruses are known to cause severe hemorrhagic fever in humans and/or nonhuman primates, LLOV is biologically uncharacterized, since infectious LLOV has never been isolated. To examine the properties of LLOV, we characterized its envelope glycoprotein (GP), which likely plays a key role in viral tropism and pathogenicity. We first found that LLOV GP principally has the same primary structure as the other filovirus GPs. Similar to the other filoviruses, virus-like particles (VLPs) produced by transient expression of LLOV GP, matrix protein, and nucleoprotein in 293T cells had densely arrayed GP spikes on a filamentous particle. Mouse antiserum to LLOV VLP was barely cross-reactive to viruses of the other genera, indicating that LLOV is serologically distinct from the other known filoviruses. For functional study of LLOV GP, we utilized a vesicular stomatitis virus (VSV) pseudotype system and found that LLOV GP requires low endosomal pH and cathepsin L, and that human C-type lectins act as attachment factors for LLOV entry into cells. Interestingly, LLOV GP-pseudotyped VSV infected particular bat cell lines more efficiently than viruses bearing other filovirus GPs. These results suggest that LLOV GP mediates cellular entry in a manner similar to that of the other filoviruses while showing preferential tropism for some bat cells.
Author Ken Maeda
Hirohito Ogawa
Masahiro Kajihara
Hiroko Miyamoto
Yoshihiro Sakoda
Reiko Yoshida
Junki Maruyama
Ayato Takada
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  organization: Division of Global Epidemiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo, Japan
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  givenname: Hiroko
  surname: Miyamoto
  fullname: Miyamoto, Hiroko
  organization: Division of Global Epidemiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo, Japan
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  givenname: Masahiro
  surname: Kajihara
  fullname: Kajihara, Masahiro
  organization: Division of Global Epidemiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo, Japan
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  givenname: Hirohito
  surname: Ogawa
  fullname: Ogawa, Hirohito
  organization: Hokudai Center for Zoonosis Control in Zambia, School of Veterinary Medicine, The University of Zambia, Lusaka, Zambia, Hokkaido University Research Center for Zoonosis Control, Sapporo, Japan
– sequence: 5
  givenname: Ken
  surname: Maeda
  fullname: Maeda, Ken
  organization: Laboratory of Veterinary Microbiology, Faculty of Agriculture, Yamaguchi University, Yamaguchi, Japan
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  givenname: Yoshihiro
  surname: Sakoda
  fullname: Sakoda, Yoshihiro
  organization: Laboratory of Microbiology, Department of Disease Control, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Japan
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  givenname: Reiko
  surname: Yoshida
  fullname: Yoshida, Reiko
  organization: Division of Global Epidemiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo, Japan
– sequence: 8
  givenname: Ayato
  surname: Takada
  fullname: Takada, Ayato
  organization: Division of Global Epidemiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo, Japan, School of Veterinary Medicine, the University of Zambia, Lusaka, Zambia
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Snippet Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
Lloviu virus (LLOV), a novel filovirus detected in bats, is phylogenetically distinct from viruses in the genera Ebolavirus and Marburgvirus in the family...
Lloviu virus (LLOV), a novel filovirus detected in bats, is phylogenetically distinct from viruses in the genera Ebolavirus and Marburgvirus in the family...
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StartPage 99
SubjectTerms Amino Acid Sequence
Animals
Base Sequence
Blotting, Western
Cross Reactions
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Female
Filoviridae
Filoviridae - metabolism
Filoviridae - physiology
Filovirus
HEK293 Cells
Humans
Mice
Mice, Inbred BALB C
Microscopy, Electron, Scanning
Microscopy, Electron, Transmission
Molecular Sequence Data
Primates
Vesicular stomatitis virus
Viral Envelope Proteins - metabolism
Viral Tropism
Virus-Cell Interactions
Title Characterization of the Envelope Glycoprotein of a Novel Filovirus, Lloviu Virus
URI http://jvi.asm.org/content/88/1/99.abstract
https://www.ncbi.nlm.nih.gov/pubmed/24131711
https://www.proquest.com/docview/1490739198
https://www.proquest.com/docview/1492645513
https://pubmed.ncbi.nlm.nih.gov/PMC3911722
Volume 88
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