Nucleotide changes responsible for loss of neuroinvasiveness in Japanese encephalitis virus neutralization-resistant mutants

Cecilia, D.; Gould, Ernest A.

doi:10.1016/0042-6822(91)90471-m

Cited by 155 publications

(88 citation statements)

References 19 publications

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“…Amino-acid substitutions at position E-366 were also found in peptides with T-helper cell epitopes for Murray Valley encephalitis (MVE) virus (36). Phenotype changes among flaviviruses have also been found to be associated with the amino-acid alteration of E proteins (7,19,24,34).…”

Section: Discussionmentioning

confidence: 99%

Antigenic and Genetic Variations among Japanese Encephalitis Virus Strains Belonging to Genotype 1

Ali

Igarashi

1997

Microbiology and Immunology

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Hyperimmune antisera against four Japanese encephalitis (JE) virus strains, ThCMAr4492 and ThCMAr6793 from Thailand and Nakayama and JaGAr01 from Japan, were used to analyze the antigenic relationships among 12 Thai strains belonging to genotype 1, and two Japanese strains and one Chinese strain belonging to genotype 3. The antiserum for ThCMAr6793 significantly neutralized nine of the 12 Thai strains, none of which was significantly neutralized by antisera for the Nakayama and JaGAr01 strains. The antiserum for ThCMAr4492 neutralized only its homologous strain; therefore, ThCMAr4492 was antigenically different from all other strains. Two Thai strains (Subin and KE-093/83) were significantly less neutralized by all four of the antisera tested. In the deduced amino-acid sequence of the E protein, the 12 Thai strains revealed 100 to 98.2 % identity among them and 90.0 to 98.8 % identity with the published strains, respectively. Among significant amino-acid substitutions, three residues at positions E-222, E-327 and E-366 were shared by all of the Thai strains, whereas residues at E-89, E-123, E-131, E-178, E-293, E-351 and E-373 seemed to be strain-specific. The amino acids at positions E-178, E-327, E-351, E-373 and E-366 are found either in the peptides with functional T-helper cell epitopes or in the ectodomain of the E protein of other flaviviruses. These amino acids may therefore be responsible for determining the antigenic heterogeneity of these strains.

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Section: Discussionmentioning

confidence: 99%

Antigenic and Genetic Variations among Japanese Encephalitis Virus Strains Belonging to Genotype 1

Ali

Igarashi

1997

Microbiology and Immunology

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“…The substitution of an amino acid in OHF virus at position 67 exactly coincides with that of an escape mutant of TBE virus (Holzmann et al, 1990) and this is the position of the N-glycosylation site in dengue virus. Amino acids 271 to 282 encompass a cluster of amino acid changes in OHF virus and an amino acid codon change within this region was identified in a Japanese encephalitis virus neutralization-resistant mutant (Cecilia & Gould, 1991). Moreover, the vaccine strain of yellow fever (YF) virus also shows two amino acid codon substitutions in this region (Rice et al, 1985) as compared with most other flaviviruses.…”

Section: Short Communicationmentioning

confidence: 99%

Nucleotide and deduced amino acid sequence of the envelope glycoprotein of Omsk haemorrhagic fever virus; comparison with other flaviviruses

Грицун¹,

Lashkevich

Gould³

1993

Journal of General Virology

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The gene encoding the envelope glycoprotein of Omsk haemorrhagic fever (OHF) virus was cloned and sequenced. A freeze-dried preparation of infected suckling mouse brain suspension was used as the source material for viral RNA. The derived cDNA was amplified using the polymerase chain reaction and the cloned DNA sequenced by dideoxynucleotide sequencing. Alignment of the OHF virus sequence with those of other known tick-borne flaviviruses showed that they shared Nglycosylation sites, cysteine residues, the fusion peptide and a hexapeptide (EHLPTA) that identifies tick-borne flaviviruses. OHF virus was distinguishable from the other viruses but shared closest amino acid identity (93-0%) with the tick-borne encephalitis viruses. A sequence of three amino acids (AQN; amino acids 232 to 234), which was previously shown to be specific for the tick-borne encephalitis viruses, was altered to MVG in OHF virus. This is predicted to have a higher hydrophobicity than the AQN sequence and may therfore have significant implications for the phenotypic characteristics of OHF virus. The results demonstrate close phylogenetic relationships between these viruses but also show their distinct evolutionary development. Sequence changes within the envelope glycoprotein of OHF virus have been identified that may be responsible for the distinct tropism of this flavivirus. These results support and enlarge upon previous data obtained from serological analysis.

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“…Amino acids 308 to 312 show one substitution for OHF virus and two for the YF vaccine strain (Rice et al, 1985), whilst amino acids 384 to 393 show amino acid substitutions for OHF virus, two escape mutants of TBE virus (Holzmann et al, 1990), the vaccine strain of YF virus and attenuated Murray Valley encephalitis virus (Lobigs et al, 1990). Despite the fact that a single codon change can reduce the virulence for mice of flaviviruses (Holzmann et al, 1990;Cecilia & Gould, 1991) the observations reported above imply that changes in several domains within the viral E glycoprotein may be required for alteration of the pathogenetic characteristics of these viruses. There is not a single motif that identifies the haemorrhagic flaviviruses.…”

Section: Short Communicationmentioning

confidence: 99%

Nucleotide and deduced amino acid sequence of the envelope gene of the Vasilchenko strain of TBE virus; comparison with other flaviviruses

Грицун¹,

Фролова²,

Pogodina³

et al. 1993

Virus Research

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Nucleotide changes responsible for loss of neuroinvasiveness in Japanese encephalitis virus neutralization-resistant mutants

Cited by 155 publications

References 19 publications

Antigenic and Genetic Variations among Japanese Encephalitis Virus Strains Belonging to Genotype 1

Antigenic and Genetic Variations among Japanese Encephalitis Virus Strains Belonging to Genotype 1

Nucleotide and deduced amino acid sequence of the envelope glycoprotein of Omsk haemorrhagic fever virus; comparison with other flaviviruses

Nucleotide and deduced amino acid sequence of the envelope gene of the Vasilchenko strain of TBE virus; comparison with other flaviviruses

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