Localization of a Neutralizing Epitope on the Envelope Protein of Dengue Virus Type 2

Lin, Bo; Parrish, Colin R.; Murray, Julie M.; Wright, P.J.

doi:10.1006/viro.1994.1410

Cited by 89 publications

(70 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The site of the junction between the dengue-2 virus and the dengue-3 virus portions of this E protein was chosen so as not to disrupt disulfide bridges (Lin et al, 1994) or change the predicted hydrophilic characteristics of the native proteins. Both dengue-2 and dengue-3 virus-specific epitopes as well as dengue virus and flavivirus cross-reactive epitopes were preserved on the hybrid molecule (Table 1).…”

Section: Discussionmentioning

confidence: 99%

“…MAb neutralization escape mutants of flaviviruses have been used to delineate epitopes which might be involved in binding to and\or fusion of these viruses with host cell membranes. In the flaviviruses studied, regions surrounding amino acids 71-72, 128, 224-227, 270, 303-311, 333 and 402-403 appear to be important, directly or indirectly, for the binding and\or fusion of the virus to host cell membranes (Lobigs et al, 1987 ;Cecilia & Gould, 1991 ;Jiang et al, 1993 ;Lin et al, 1994). Our own studies suggest that some of these regions (adjacent to amino acids 128, 224-227 and 333) also contain epitopes commonly recognized by antibodies from human dengue patients (Aaskov et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Analysis of a recombinant dengue-2 virus-dengue-3 virus hybrid envelope protein expressed in a secretory baculovirus system.

Bielefeldt‐Ohmann

Beasley

FitzPatrick

et al. 1997

Journal of General Virology

View full text Add to dashboard Cite

In a step towards a tetravalent dengue virus subunit vaccine which is economical to produce, highly immunogenic and stable, a hybrid dengue virus envelope (E) protein molecule has been constructed. It consists of 36 amino acids from the membrane protein, the N-terminal 288 amino acids of the dengue-2 virus E protein plus amino acids 289-424 of the dengue-3 virus E protein. It has been engineered for secretory expression by fusion to a mellitin secretory signal sequence and truncation of the hydrophobic transmembrane segment. Using the baculovirus expression system and serumfree conditions, more than 95 % of recombinant dengue-2 virus-dengue-3 virus hybrid E protein (rD2D3E) was secreted into the cell culture supernatant in a stable form with multiple features indicative of preserved conformation. The hybrid molecule reacted with a panel of dengue virus-and

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Analysis of a recombinant dengue-2 virus-dengue-3 virus hybrid envelope protein expressed in a secretory baculovirus system.

Bielefeldt‐Ohmann

Beasley

FitzPatrick

et al. 1997

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…We have previously shown that the recombinant vaccine contains epitopes reactive with DEN-2 type-specific neutralizing monoclonal antibodies 3H5 and 6B6 and several other DEN-2-specific, neutralizing, monoclonal antibodies have also been mapped to the B domain of the DEN-2 virus envelope protein. [22][23][24]26 It is conceivable that the amount of protein produced by the plasmid DNA in the cell may be too low for optimal CD4 ϩ T cell stimulation and subsequent B-cell proliferation and differentiation. The advantage of DNA vaccines is thought to reside in their ability to express foreign antigen inside the cell and access the endogenous pathway, leading to presentation by class I major histocompatibility antigens (MHC I).…”

Section: Virusmentioning

confidence: 99%

Characterization of antibody responses to combinations of a dengue-2 DNA and dengue-2 recombinant subunit vaccine.

Simmons¹,

Murphy²,

Kochel³

et al. 2001

The American Journal of Tropical Medicine and Hygiene

View full text Add to dashboard Cite

Abstract. A dengue-2 (DEN-2) DNA vaccine coding for the premembrane and envelope (E) proteins and a recombinant fusion protein containing the B domain of the DEN-2 E protein fused to the maltose-binding protein (MBP) of Escherichia coli both elicited neutralizing antibody in mice. In order to achieve more rapid protective immunity as well as to increase the persistence of neutralizing antibody, we primed mice with the DNA vaccine (D), the recombinant MBP protein (R), or both (RD) given simultaneously, and then boosted twice with either the R ( (40), and the D/R/R group had a slightly higher titer (156) than these 2 groups. The predominant antibody subclass for the D/D/D mice was immunoglobulin (Ig) G2a, similar to mice infected with live virus. The R/R/R mice showed an exclusive IgG1 antibody response, and the RD/RD/RD response also was predominantly IgG1. The antibody subclass pattern of the R/D/D and D/R/R mice showed a more balanced distribution of both IgG1 and IgG2a. Investigating the neutralizing capacity of antibody subclasses suggested that both IgG1 and IgG2a could neutralize DEN-2 virus. Our observations indicate that the combination RD prime-boost regimen warrants further investigation as a vaccine strategy to prevent dengue infection.

show abstract

“…Blood was collected and serum pooled from three animals at 9-11 weeks after primary immunization. These sera were used for immunoprecipitation (Lin et al, 1994) and immunoblotting (Li et al, 1997 a) as previously described. $&S-labelled proteins were quantified using a Fuji phosphorimager, while densitometry of scanned immunoblots was performed using NIH Image software.…”

Section: Only the Non-glycosylated Fraction Of Hepatitis E Virus Capsmentioning

confidence: 99%

Only the non-glycosylated fraction of hepatitis E virus capsid (open reading frame 2) protein is stable in mammalian cells.

Torresi

Locarnini

et al. 1999

Journal of General Virology

View full text Add to dashboard Cite

Hepatitis E virus (HEV) is a non-enveloped, positivestrand RNA virus, with the genome encoding three open reading frames (ORFs) of which ORF 2 directs translation of the capsid protein, PORF2. Following pulse-labelling and cell fractionation of PORF2 expressed in mammalian cells using the Semliki Forest virus replicon, the capsid protein was detected as three major species of 78 (PORF2), 82 and 86 kDa, with P82 and P86 being N-glycosylated (gPORF2 and ggPORF2, respectively). Although gPORF2 and ggPORF2 species represented 79 % of total PORF2 after 20 min metabolic labelling and were largely membrane-associated, the glycosylated PORF2 species were much less stable than non-glycosylated PORF2, which was present in the cytosol and represented the major product accumulated in the cell. In the absence of detectable surface expression or export of PORF2, this suggests that glycosylated ORF 2 proteins may not be intermediates in HEV capsid assembly.

show abstract

Localization of a Neutralizing Epitope on the Envelope Protein of Dengue Virus Type 2

Cited by 89 publications

References 0 publications

Analysis of a recombinant dengue-2 virus-dengue-3 virus hybrid envelope protein expressed in a secretory baculovirus system.

Analysis of a recombinant dengue-2 virus-dengue-3 virus hybrid envelope protein expressed in a secretory baculovirus system.

Characterization of antibody responses to combinations of a dengue-2 DNA and dengue-2 recombinant subunit vaccine.

Only the non-glycosylated fraction of hepatitis E virus capsid (open reading frame 2) protein is stable in mammalian cells.

Contact Info

Product

Resources

About