scholarly journals Molecular Characterization of a Hamster Viscerotropic Strain of Yellow Fever Virus

2003 ◽  
Vol 77 (2) ◽  
pp. 1462-1468 ◽  
Author(s):  
Monica A. McArthur ◽  
Miguel T. Suderman ◽  
John-Paul Mutebi ◽  
Shu-Yuan Xiao ◽  
Alan D. T. Barrett
Keyword(s):  
Amino Acid ◽  
Molecular Characterization ◽  
Yellow Fever ◽  
Yellow Fever Virus ◽  
Clinical Signs ◽  
Serial Passage ◽  
Severe Illness ◽  
Amino Acid Substitutions ◽  
E Protein

ABSTRACT A hamster viscerotropic strain of yellow fever (YF) virus has been derived after serial passage of strain Asibi through hamsters. The parental Asibi/hamster p0 virus causes a mild and transient viremia in hamsters with no outward, clinical signs of illness. In contrast, the viscerotropic Asibi/hamster p7 virus causes a robust viremia, severe illness, and death in subadult hamsters. The genome of the hamster viscerotropic Asibi/hamster p7 virus has been sequenced and compared with the parental nonviscerotropic Asibi/hamster p0 virus identifying 14 nucleotide changes encoding only seven amino acid substitutions. The majority of these substitutions (five of seven) fall within the envelope (E) protein at positions Q27H, D28G, D155A, K323R, and K331R. These results support an important role for the E protein in determining YF virus viscerotropism.

Outbreak of jaundice and hemorrhagic fever in the Southeast of Brazil in 2001: Detection and molecular characterization of yellow fever virus

2002 ◽  
Vol 68 (4) ◽  
pp. 620-627 ◽  
Author(s):  
A.M.B. de Filippis ◽  
R.M.R. Nogueira ◽  
H.G. Schatzmayr ◽  
D.S. Tavares ◽  
A.V. Jabor ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Yellow Fever ◽  
Yellow Fever Virus ◽  
Hemorrhagic Fever ◽  
Fever Virus

scholarly journals Interaction of Yellow Fever Virus French Neurotropic Vaccine Strain with Monkey Brain: Characterization of Monkey Brain Membrane Receptor Escape Variants

2000 ◽  
Vol 74 (6) ◽  
pp. 2903-2906 ◽  
Author(s):  
Haolin Ni ◽  
Kate D. Ryman ◽  
Heiman Wang ◽  
Mohammad F. Saeed ◽  
Robin Hull ◽  
...  
Keyword(s):  
Amino Acid ◽  
Yellow Fever ◽  
Mouse Brain ◽  
Amino Acid Substitution ◽  
Yellow Fever Virus ◽  
Fever Virus ◽  
Monkey Brain ◽  
Intracerebral Inoculation ◽  
E Protein ◽  
Monkey Liver

ABSTRACT Binding of yellow fever virus wild-type strains Asibi and French viscerotropic virus and vaccine strains 17D and FNV to monkey brain and monkey liver cell membrane receptor preparations (MRPs) was investigated. Only FNV bound to monkey brain MRPs, while French viscerotropic virus, Asibi, and FNV all bound to monkey liver MRPs. Four monkey brain and two mouse brain MRP escape (MRPR) variants of FNV were selected at pH 7.6 and 6.0. Three monkey brain MRPR variants selected at pH 7.6 each had only one amino acid substitution in the envelope (E) protein in domain II (E-237, E-260, or E274) and were significantly attenuated in mice following intracerebral inoculation. Two of the variants were tested in monkeys and retained parental neurotropism following intracerebral inoculation at the dose tested. We speculate that this region of domain II is involved in binding of FNV E protein to monkey brain and is, in part, responsible for the enhanced neurotropism of FNV for monkeys. A monkey brain MRPR variant selected at pH 6.0 and two mouse brain MRPR variants selected at pH 7.6 were less attenuated in mice, and each had an amino acid substitution in the transmembrane region of the E protein (E-457 or E-458).

scholarly journals Genome Characterization of Yellow Fever Virus Wild-Type Strain Asibi, Parent to Live-Attenuated 17D Vaccine, from Three Different Sources

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1383
Author(s):  
Emily H. Davis ◽  
Jill K. Thompson ◽  
Steven G. Widen ◽  
Alan D. T. Barrett
Keyword(s):  
Yellow Fever ◽  
Wild Type Strain ◽  
Yellow Fever Virus ◽  
Serial Passage ◽  
Vaccine Virus ◽  
Fever Virus ◽  
Wild Type ◽  
Chicken Tissue ◽  
Different Sources

The yellow fever virus vaccine, 17D, was derived through the serial passage of the wild-type (WT) strain Asibi virus in mouse and chicken tissue. Since its derivation, the mechanism of attenuation of 17D virus has been investigated using three 17D substrains and WT Asibi virus. Although all three substrains of 17D have been sequenced, only one isolate of Asibi has been examined genetically and all interpretation of attenuation is based on this one isolate. Here, we sequenced the genome of Asibi virus from three different laboratories and show that the WT strain is genetically homogenous at the amino acids that distinguish Asibi from 17D vaccine virus.

scholarly journals Molecular Characterization of Hamster-Adapted Yellow Fever Virus

2020 ◽  
Vol 20 (3) ◽  
pp. 222-227
Author(s):  
Monica A. McArthur ◽  
Shuliu L. Zhang ◽  
Li Li ◽  
Robert B. Tesh ◽  
Alan D.T. Barrett
Keyword(s):  
Molecular Characterization ◽  
Yellow Fever ◽  
Yellow Fever Virus ◽  
Fever Virus

Detection and Molecular Characterization of Yellow Fever Virus, 2017, Brazil

EcoHealth ◽  
2018 ◽  
Vol 15 (4) ◽  
pp. 864-870 ◽  
Author(s):  
P. O. Figueiredo ◽  
A. T. S. Silva ◽  
J. S. Oliveira ◽  
P. E. Marinho ◽  
F. T. Rocha ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Yellow Fever ◽  
Yellow Fever Virus ◽  
Fever Virus

scholarly journals Molecular Basis for Attenuation of Neurovirulence of a Yellow Fever Virus/Japanese Encephalitis Virus Chimera Vaccine (ChimeriVax-JE)

2001 ◽  
Vol 75 (2) ◽  
pp. 934-942 ◽  
Author(s):  
Juan Arroyo ◽  
Farshad Guirakhoo ◽  
Sabine Fenner ◽  
Zhen-Xi Zhang ◽  
Thomas P. Monath ◽  
...  
Keyword(s):  
Amino Acid ◽  
Japanese Encephalitis Virus ◽  
Yellow Fever ◽  
Japanese Encephalitis ◽  
Yellow Fever Virus ◽  
Encephalitis Virus ◽  
Fever Virus ◽  
Single Amino Acid ◽  
E Protein ◽  
Viral Vaccine

ABSTRACT A yellow fever virus (YFV)/Japanese encephalitis virus (JEV) chimera in which the structural proteins prM and E of YFV 17D are replaced with those of the JEV SA14-14-2 vaccine strain is under evaluation as a candidate vaccine against Japanese encephalitis. The chimera (YFV/JEV SA14-14-2, or ChimeriVax-JE) is less neurovirulent than is YFV 17D vaccine in mouse and nonhuman primate models (F. Guirakhoo et al., Virology 257:363–372, 1999; T. P. Monath et al., Vaccine 17:1869–1882, 1999). Attenuation depends on the presence of the JEV SA14-14-2 E protein, as shown by the high neurovirulence of an analogous YFV/JEV Nakayama chimera derived from the wild JEV Nakayama strain (T. J. Chambers, A. Nestorowicz, P. W. Mason, and C. M. Rice, J. Virol. 73:3095–3101, 1999). Ten amino acid differences exist between the E proteins of ChimeriVax-JE and the YFV/JEV Nakayama virus, four of which are predicted to be neurovirulence determinants based on various sequence comparisons. To identify residues that are involved in attenuation, a series of intratypic YFV/JEV chimeras containing either single or multiple amino acid substitutions were engineered and tested for mouse neurovirulence. Reversions in at least three distinct clusters were required to restore the neurovirulence typical of the YFV/JEV Nakayama virus. Different combinations of cluster-specific reversions could confer neurovirulence; however, residue 138 of the E protein (E138) exhibited a dominant effect. No single amino acid reversion produced a phenotype significantly different from that of the ChimeriVax-JE parent. Together with the known genetic stability of the virus during prolonged cell culture and mouse brain passage, these findings support the candidacy of this experimental vaccine as a novel live-attenuated viral vaccine against Japanese encephalitis.

scholarly journals Mutagenesis of the Signal Sequence of Yellow Fever Virus prM Protein: Enhancement of Signalase Cleavage In Vitro Is Lethal for Virus Production

2000 ◽  
Vol 74 (1) ◽  
pp. 24-32 ◽  
Author(s):  
Eva Lee ◽  
Christine E. Stocks ◽  
Sean M. Amberg ◽  
Charles M. Rice ◽  
Mario Lobigs
Keyword(s):  
Amino Acid ◽  
Yellow Fever ◽  
Yellow Fever Virus ◽  
Signal Sequence ◽  
Virus Production ◽  
Fever Virus ◽  
Signal Peptidase ◽  
Amino Acid Substitutions ◽  
Prm Protein

ABSTRACT Proteolytic processing at the C-prM junction in the flavivirus polyprotein involves coordinated cleavages at the cytoplasmic and luminal sides of an internal signal sequence. We have introduced at the COOH terminus of the yellow fever virus (YFV) prM signal sequence amino acid substitutions (VPQAQA mutation) which uncoupled efficient signal peptidase cleavage of the prM protein from its dependence on prior cleavage in the cytoplasm of the C protein mediated by the viral NS2B-3 protease. Infectivity assays with full-length YFV RNA transcripts showed that the VPQAQA mutation, which enhanced signal peptidase cleavage in vitro, was lethal for infectious virus production. Revertants or second-site mutants were recovered from cells transfected with VPQAQA RNA. Analysis of these viruses revealed that single amino acid substitutions in different domains of the prM signal sequence could restore viability. These variants had growth properties in vertebrate cells which differed only slightly from those of the parent virus, despite efficient signal peptidase cleavage of prM in cell-free expression assays. However, the neurovirulence in mice of the VPQAQA variants was significantly attenuated. This study demonstrates that substitutions in the prM signal sequence which disrupt coordinated cleavages at the C-prM junction can impinge on the biological properties of the mutant viruses. Factors other than the rate of production of prM are vitally controlled by regulated cleavages at this site.

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