Epitopic Analysis of Antigenic Determinants on the Surface of Dengue-2 Virions Using Monoclonal Antibodies *

Henchal, Erik A.; McCown, Jack M.; Burke, Donald S.; Seguin, M C; Brandt, Walter E.

doi:10.4269/ajtmh.1985.34.162

Cited by 192 publications

(147 citation statements)

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“…By recognizing the consensus sequence Arg/Lys-X-Arg/Lys-Arg the same enzyme appears to be responsible for the cleavage and activation of the fusogenic potential of a number of viral envelope glycoproteins (Strauss et al, 1987). The presence of prM in Langat virus grown in chick embryo cells, as shown in the present work, as well as the demonstration of prM in purified preparations of other flaviviruses (Henchal et al, 1985;Kimura-Kuroda & Yasui, 1983;Wengler et al, 1987) suggest that cleavage at the consensus sequence may depend on both host and viral factors.…”

Section: Discussionsupporting

confidence: 81%

Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions

Guirakhoo

Heinz²,

Mandl³

et al. 1991

Journal of General Virology

170

156

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The fusion activity of flaviviruses [tick-borne encephalitis (TBE) virus and Japanese encephalitis virus] was assessed by inducing fusion from without of C6/36 mosquito cells with purified virus preparations. Membrane fusion and polykaryocyte formation was observed only after incubating the viruses at acidic pH. Two groups of monoclonal antibodies reacting with distinct non-overlapping antigenic domains on the TBE virus protein E inhibited fusion from without. One of these domains contains the most highly conserved and putative fusion-active sequence of the flavivirus protein E. Of five TBE virus monoclonal antibody escape mutants, each defined by a single amino acid substitution in the envelope protein E, one revealed a reduced fusion activity and another one a lower pH threshold. TBE virus grown in the presence of ammonium chloride as well as Langat virus purified from the supernatant of infected chick embryo cells contained the precursor of protein M (prM) rather than M itself. These 'immature' virions did not cause fusion from without, suggesting that the proteolytic processing of prM may be necessary for the generation of fusion-competent virions.

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Section: Discussionsupporting

confidence: 81%

Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions

Guirakhoo

Heinz²,

Mandl³

et al. 1991

Journal of General Virology

170

156

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“…However, these MAbs were able to increase the survival of challenged mice when combined with another non-protective antibody, 27-12/4. While it is possible that, when combined, these MAbs may have enhanced binding as has been found with some anti-E MAbs (Henchal et al, 1985), these effects were not demonstrated in competitive binding assays using solubilized antigen (Henchal et al, 1987). The paradoxical increase in morbidity when protective MAbs 68-5/16 and 63-15 were combined may be related to their mutual competition for overlapping binding sites (Henchal et al, 1987) and unknown dynamic changes in antigen conformation.…”

Section: Short Communicationmentioning

confidence: 95%

Synergistic Interactions of Anti-NS1 Monoclonal Antibodies Protect Passively Immunized Mice from Lethal Challenge with Dengue 2 Virus

Henchal

Schlesinger

1988

Journal of General Virology

Self Cite

196

145

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“…The hybridoma line D1-4G2-415, which produces antibody to the E protein of DEN-2, was obtained from the American Type Culture Collection. This cell line produces an IgG2a MAb (4G2) that reacts with a flavivirus group-specific epitope and has neutralizing and HI activity (Henchal et al, 1985). Production and purification of rabbit antibodies to MVE have been previously described (Hall et al, 1987).…”

Section: Characterization Of Mabsmentioning

confidence: 99%

Epitope Analysis of the Envelope and Non-structural Glycoproteins of Murray Valley Encephalitis Virus

Hall

Kay

Burgess

et al. 1990

Journal of General Virology

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Previous studies have shown that antibodies produced against strategic flavivirus epitopes play an important role in recovery and immunity. Definition of the conformation and location of these epitopes and the degree of their conservation among flaviviruses is important to understanding the humoral response to flavivirus infection. In this study we have examined epitopes recognized by 14 monoclonal antibodies (MAbs) produced to the envelope (E) and nonstructural (NS1) proteins of Murray Valley encephalitis virus (MVE). These antibodies were analysed for specificity, neutralization, haemagglutination inhibition (HI) and competitive binding. We have identified six distinct epitopes on the E protein which are located in four non-overlapping domains. MAbs to epitopes in one domain neutralized virus, were specific for MVE and Japanese encephalitis virus, and reacted with epitopes resistant to reduction. Two other E domains, one specific to MVE and the other shared by all flaviviruses, also contained neutralization sites and were stabilized by disulphide bonds. The fourth domain on E was conserved among the flaviviruses, sensitive to SDS denaturation and did not induce neutralizing antibody. Studies with MVE NS 1 MAbs revealed that they were mostly type-specific, unreactive with conserved epitopes, and unreactive in HI and neutralization tests. The six epitopes identified on NS 1 did not overlap and represent antigenic domains either resistant or sensitive to reduction. Immunoblotting of viral proteins in MVE-infected C6/36 cells revealed two distinct forms of NS1 and high Mr proteins of 97K and 108K that represented disulphide-linked heterodimers of E and NS1.

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Epitopic Analysis of Antigenic Determinants on the Surface of Dengue-2 Virions Using Monoclonal Antibodies *

Cited by 192 publications

References 0 publications

Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions

Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions

Synergistic Interactions of Anti-NS1 Monoclonal Antibodies Protect Passively Immunized Mice from Lethal Challenge with Dengue 2 Virus

Epitope Analysis of the Envelope and Non-structural Glycoproteins of Murray Valley Encephalitis Virus

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