PMID- 26038399
OWN - NLM
STAT- MEDLINE
DCOM- 20151201
LR  - 20191210
IS  - 1537-6613 (Electronic)
IS  - 0022-1899 (Print)
IS  - 0022-1899 (Linking)
VI  - 212 Suppl 2
IP  - Suppl 2
DP  - 2015 Oct 1
TI  - The Role of Conserved N-Linked Glycans on Ebola Virus Glycoprotein 2.
PG  - S204-9
LID - 10.1093/infdis/jiv201 [doi]
AB  - BACKGROUND: N-linked glycosylation is a common posttranslational modification 
      found on viral glycoproteins (GPs) and involved in promoting expression, cellular 
      attachment, protection from proteases, and antibody evasion. The GP subunit GP2 
      of filoviruses contains 2 completely conserved N-linked glycosylation sites 
      (NGSs) at N563 and N618, suggesting that they have been maintained through 
      selective pressures. METHODS: We assessed mutants lacking these glycans for 
      expression and function to understand the role of these sites during Ebola virus 
      entry. RESULTS: Elimination of either GP2 glycan individually had a modest effect 
      on GP expression and no impact on antibody neutralization of vesicular stomatitis 
      virus pseudotyped with Ebola virus GP. However, loss of the N563 glycan enhanced 
      entry by 2-fold and eliminated GP detection by a well-characterized monoclonal 
      antibody KZ52. Loss of both sites dramatically decreased GP expression and 
      abolished entry. Surprisingly, a GP that retained a single NGS at N563, 
      eliminating the remaining 16 NGSs from GP1 and GP2, had detectable expression, a 
      modest increase in entry, and pronounced sensitivity to antibody neutralization. 
      CONCLUSIONS: Our findings support the importance of the GP2 glycans in GP 
      expression/structure, transduction efficiency, and antibody neutralization, 
      particularly when N-linked glycans are also removed from GP1.
CI  - (c) The Author 2015. Published by Oxford University Press on behalf of the 
      Infectious Diseases Society of America. All rights reserved. For Permissions, 
      please e-mail: journals.permissions@oup.com.
FAU - Lennemann, Nicholas J
AU  - Lennemann NJ
AD  - Department of Microbiology, University of Iowa, Iowa City.
FAU - Walkner, Madeline
AU  - Walkner M
AD  - Department of Microbiology, University of Iowa, Iowa City.
FAU - Berkebile, Abigail R
AU  - Berkebile AR
AD  - Department of Microbiology, University of Iowa, Iowa City.
FAU - Patel, Neil
AU  - Patel N
AD  - Department of Microbiology, University of Iowa, Iowa City.
FAU - Maury, Wendy
AU  - Maury W
AD  - Department of Microbiology, University of Iowa, Iowa City.
LA  - eng
GR  - R01 AI077519/AI/NIAID NIH HHS/United States
GR  - T32 AI007533/AI/NIAID NIH HHS/United States
GR  - T32AI007533/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20150602
PL  - United States
TA  - J Infect Dis
JT  - The Journal of infectious diseases
JID - 0413675
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neutralizing)
RN  - 0 (Polysaccharides)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (envelope glycoprotein, Ebola virus)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antibodies, Neutralizing/immunology
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - Conserved Sequence/*genetics
MH  - Ebolavirus/*genetics/immunology/*pathogenicity
MH  - HEK293 Cells
MH  - Hemorrhagic Fever, Ebola/immunology/*virology
MH  - Humans
MH  - Mutation/genetics
MH  - Polysaccharides/*genetics
MH  - Vero Cells
MH  - Vesiculovirus/immunology
MH  - Viral Envelope Proteins/*genetics
MH  - Virus Internalization
PMC - PMC4564545
OTO - NOTNLM
OT  - Ebola virus
OT  - N-linked glycosylation
OT  - antibody neutralization
OT  - filovirus
OT  - glycan
OT  - glycoprotein
OT  - mutagenesis
OT  - virus entry
EDAT- 2015/06/04 06:00
MHDA- 2015/12/15 06:00
PMCR- 2016/10/01
CRDT- 2015/06/04 06:00
PHST- 2015/06/04 06:00 [entrez]
PHST- 2015/06/04 06:00 [pubmed]
PHST- 2015/12/15 06:00 [medline]
PHST- 2016/10/01 00:00 [pmc-release]
AID - jiv201 [pii]
AID - 10.1093/infdis/jiv201 [doi]
PST - ppublish
SO  - J Infect Dis. 2015 Oct 1;212 Suppl 2(Suppl 2):S204-9. doi: 10.1093/infdis/jiv201. 
      Epub 2015 Jun 2.