N-linked glycosylation of the West Nile virus envelope protein is not a requisite for avian virulence or vector competence.
The N-linked glycosylation motif at amino acid position 154-156 of the envelope (E) protein of West Nile virus (WNV) is linked to enhanced murine neuroinvasiveness, avian pathogenicity and vector competence. Naturally occurring isolates with altered E protein glycosylation patterns have been observe...
Published in: | PLOS Neglected Tropical Diseases |
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ftdoajarticles:oai:doaj.org/article:c074d38fd0b049d9a322a42893c3e9d0 2023-05-15T15:13:28+02:00 N-linked glycosylation of the West Nile virus envelope protein is not a requisite for avian virulence or vector competence. Payal D Maharaj Stanley A Langevin Bethany G Bolling Christy C Andrade Xavier A Engle Wanichaya N Ramey Angela Bosco-Lauth Richard A Bowen Todd A Sanders Claire Y-H Huang William K Reisen Aaron C Brault 2019-07-01T00:00:00Z https://doi.org/10.1371/journal.pntd.0007473 https://doaj.org/article/c074d38fd0b049d9a322a42893c3e9d0 EN eng Public Library of Science (PLoS) https://doi.org/10.1371/journal.pntd.0007473 https://doaj.org/toc/1935-2727 https://doaj.org/toc/1935-2735 1935-2727 1935-2735 doi:10.1371/journal.pntd.0007473 https://doaj.org/article/c074d38fd0b049d9a322a42893c3e9d0 PLoS Neglected Tropical Diseases, Vol 13, Iss 7, p e0007473 (2019) Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 article 2019 ftdoajarticles https://doi.org/10.1371/journal.pntd.0007473 2022-12-31T11:01:42Z The N-linked glycosylation motif at amino acid position 154-156 of the envelope (E) protein of West Nile virus (WNV) is linked to enhanced murine neuroinvasiveness, avian pathogenicity and vector competence. Naturally occurring isolates with altered E protein glycosylation patterns have been observed in WNV isolates; however, the specific effects of these polymorphisms on avian host pathogenesis and vector competence have not been investigated before. In the present study, amino acid polymorphisms, NYT, NYP, NYF, SYP, SYS, KYS and deletion (A'DEL), were reverse engineered into a parental WNV (NYS) cDNA infectious clone to generate WNV glycosylation mutant viruses. These WNV glycosylation mutant viruses were characterized for in vitro growth, pH-sensitivity, temperature-sensitivity and host competence in American crows (AMCR), house sparrows (HOSP) and Culex quinquefasciatus. The NYS and NYT glycosylated viruses showed higher viral replication, and lower pH and temperature sensitivity than NYP, NYF, SYP, SYS, KYS and A'DEL viruses in vitro. Interestingly, in vivo results demonstrated asymmetric effects in avian and mosquito competence that were independent of the E-protein glycosylation status. In AMCRs and HOSPs, all viruses showed comparable viremias with the exception of NYP and KYS viruses that showed attenuated phenotypes. Only NYP showed reduced vector competence in both Cx. quinquefasciatus and Cx. tarsalis. Glycosylated NYT exhibited similar avian virulence properties as NYS, but resulted in higher mosquito oral infectivity than glycosylated NYS and nonglycosylated, NYP, NYF, SYP and KYS mutants. These data demonstrated that amino acid polymorphisms at E154/156 dictate differential avian host and vector competence phenotypes independent of E-protein glycosylation status. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic PLOS Neglected Tropical Diseases 13 7 e0007473 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
spellingShingle |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 Payal D Maharaj Stanley A Langevin Bethany G Bolling Christy C Andrade Xavier A Engle Wanichaya N Ramey Angela Bosco-Lauth Richard A Bowen Todd A Sanders Claire Y-H Huang William K Reisen Aaron C Brault N-linked glycosylation of the West Nile virus envelope protein is not a requisite for avian virulence or vector competence. |
topic_facet |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
description |
The N-linked glycosylation motif at amino acid position 154-156 of the envelope (E) protein of West Nile virus (WNV) is linked to enhanced murine neuroinvasiveness, avian pathogenicity and vector competence. Naturally occurring isolates with altered E protein glycosylation patterns have been observed in WNV isolates; however, the specific effects of these polymorphisms on avian host pathogenesis and vector competence have not been investigated before. In the present study, amino acid polymorphisms, NYT, NYP, NYF, SYP, SYS, KYS and deletion (A'DEL), were reverse engineered into a parental WNV (NYS) cDNA infectious clone to generate WNV glycosylation mutant viruses. These WNV glycosylation mutant viruses were characterized for in vitro growth, pH-sensitivity, temperature-sensitivity and host competence in American crows (AMCR), house sparrows (HOSP) and Culex quinquefasciatus. The NYS and NYT glycosylated viruses showed higher viral replication, and lower pH and temperature sensitivity than NYP, NYF, SYP, SYS, KYS and A'DEL viruses in vitro. Interestingly, in vivo results demonstrated asymmetric effects in avian and mosquito competence that were independent of the E-protein glycosylation status. In AMCRs and HOSPs, all viruses showed comparable viremias with the exception of NYP and KYS viruses that showed attenuated phenotypes. Only NYP showed reduced vector competence in both Cx. quinquefasciatus and Cx. tarsalis. Glycosylated NYT exhibited similar avian virulence properties as NYS, but resulted in higher mosquito oral infectivity than glycosylated NYS and nonglycosylated, NYP, NYF, SYP and KYS mutants. These data demonstrated that amino acid polymorphisms at E154/156 dictate differential avian host and vector competence phenotypes independent of E-protein glycosylation status. |
format |
Article in Journal/Newspaper |
author |
Payal D Maharaj Stanley A Langevin Bethany G Bolling Christy C Andrade Xavier A Engle Wanichaya N Ramey Angela Bosco-Lauth Richard A Bowen Todd A Sanders Claire Y-H Huang William K Reisen Aaron C Brault |
author_facet |
Payal D Maharaj Stanley A Langevin Bethany G Bolling Christy C Andrade Xavier A Engle Wanichaya N Ramey Angela Bosco-Lauth Richard A Bowen Todd A Sanders Claire Y-H Huang William K Reisen Aaron C Brault |
author_sort |
Payal D Maharaj |
title |
N-linked glycosylation of the West Nile virus envelope protein is not a requisite for avian virulence or vector competence. |
title_short |
N-linked glycosylation of the West Nile virus envelope protein is not a requisite for avian virulence or vector competence. |
title_full |
N-linked glycosylation of the West Nile virus envelope protein is not a requisite for avian virulence or vector competence. |
title_fullStr |
N-linked glycosylation of the West Nile virus envelope protein is not a requisite for avian virulence or vector competence. |
title_full_unstemmed |
N-linked glycosylation of the West Nile virus envelope protein is not a requisite for avian virulence or vector competence. |
title_sort |
n-linked glycosylation of the west nile virus envelope protein is not a requisite for avian virulence or vector competence. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2019 |
url |
https://doi.org/10.1371/journal.pntd.0007473 https://doaj.org/article/c074d38fd0b049d9a322a42893c3e9d0 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
PLoS Neglected Tropical Diseases, Vol 13, Iss 7, p e0007473 (2019) |
op_relation |
https://doi.org/10.1371/journal.pntd.0007473 https://doaj.org/toc/1935-2727 https://doaj.org/toc/1935-2735 1935-2727 1935-2735 doi:10.1371/journal.pntd.0007473 https://doaj.org/article/c074d38fd0b049d9a322a42893c3e9d0 |
op_doi |
https://doi.org/10.1371/journal.pntd.0007473 |
container_title |
PLOS Neglected Tropical Diseases |
container_volume |
13 |
container_issue |
7 |
container_start_page |
e0007473 |
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1766344016681500672 |