Identification of a Gag Protein Epitope Conserved Among All Four Groups of Primate Immunodeficiency Viruses by Using Monoclonal Antibodies

Otteken, Ahlert; Nick, Sigrid; Bergter, Wolfgang; Voss, Gérald; Faisst, Arne-Christian; Stahl–Hennig∥, Christiane; Hunsmann, Gerhard

doi:10.1099/0022-1317-73-10-2721

Cited by 7 publications

(2 citation statements)

References 26 publications

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“…This is in agreement with sequence comparison showing that HIV-2 is more closely related to SIVmac than to HIV-1 [1,5,13] and with our peptide mapping results. Establishing a connection to results previously published from our group, this highly conserved epitope is obviously related to high immunogenicity [19].…”

Section: Discussionsupporting

confidence: 58%

Generation, characterization and cross-reactivities of monoclonal antibodies against the p24 core protein and the gp130 envelope glycoprotein of HIV-2ben

Otteken

Nick

et al. 1993

Med Microbiol Immunol

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The purpose of this study was to characterize antigenic determinants on structural polypeptides of human immunodeficiency virus type 2 (HIV-2ben). Therefore, three HIV-2-specific monoclonal antibodies (mAbs) against the p24 core protein (gag) and one mAb against the gp130 envelope glycoprotein (env) were produced. In addition to p24 the anti-core mAbs recognized the primary translation product of the viral gag gene p55 and an intermediate cleavage product p41. Core mAbs cross-reacted with another HIV-2 isolate (HIV-2rod), and several simian immunodeficiency viruses (SIVagm TYO7 and SIVmac), but not with SIVmnd and the HIV-1 isolates investigated (HIV-1han and HIV-1lai). The env mAb cross-reacted with HIV-2rod and SIVmac but not with SIVagm, SIVmnd or HIV-1. In competition assays and with epitope mapping possible binding sites for the mAbs were identified. The processing of HIV-2 core proteins is compared in retrovirus-infected T cell lines and during the expression by recombinant vaccinia virus. Finally, the mAb XIV DC10 which recognized a highly conserved epitope could be useful for an assay to detect HIV-1 and HIV-2 simultaneously. II D8 is the first mAb raised against HIV-2 env glycoprotein.

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Section: Discussionsupporting

confidence: 58%

Generation, characterization and cross-reactivities of monoclonal antibodies against the p24 core protein and the gp130 envelope glycoprotein of HIV-2ben

Otteken

Nick

et al. 1993

Med Microbiol Immunol

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“…In general, antibodies against the capsid proteins of viral particles, such as human immunodeficiency virus (HIV) Gag protein and influenza virus nucleoprotein, have been used in antigen-capture diagnosis kits14,15 because of their wide range of cross-reactivity, even with other subtypes, compared with that of the envelope proteins 16,17. Similar approaches using antigen-capture diagnostic or enzyme-linked immunoassay kits have been used for other viruses, such as Rift Valley fever virus,18 hepatitis B virus,19 hepatitis C virus,20 and Ebola virus 21.…”

Section: Introductionmentioning

confidence: 99%

Limited cross-reactivity of mouse monoclonal antibodies against Dengue virus capsid protein among four serotypes

Noda¹,

Masrinoul²,

Punkum³

et al. 2012

BTT

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BackgroundDengue illness is one of the important mosquito-borne viral diseases in tropical and subtropical regions. Four serotypes of dengue virus (DENV-1, DENV-2, DENV-3, and DENV-4) are classified in the Flavivirus genus of the family Flaviviridae. We prepared monoclonal antibodies against DENV capsid protein from mice immunized with DENV-2 and determined the cross-reactivity with each serotype of DENV and Japanese encephalitis virus.Methods and resultsTo clarify the relationship between the cross-reactivity of monoclonal antibodies and the diversity of these viruses, we examined the situations of flaviviruses by analyses of phylogenetic trees. Among a total of 60 prepared monoclonal antibodies specific for DENV, five monoclonal antibodies stained the nuclei of infected cells and were found to be specific to the capsid protein. Three were specific to DENV-2, while the other two were cross-reactive with DENV-2 and DENV-4. No monoclonal antibodies were cross-reactive with all four serotypes. Phylogenetic analysis of DENV amino acid sequences of the capsid protein revealed that DENV-2 and DENV-4 were clustered in the same branch, while DENV-1 and DENV-3 were clustered in the other branch. However, these classifications of the capsid protein were different from those of the envelope and nonstructural 1 proteins. Phylogenetic distances between the four serotypes of DENV were as different as those of other flaviviruses, such as Japanese encephalitis virus and West Nile virus. Large variations in the DENV serotypes were comparable with the differences between species of flavivirus. Furthermore, the diversity of flavivirus capsid protein was much greater than that of envelope and nonstructural 1 proteins.ConclusionIn this study, we produced specific monoclonal antibodies that can be used to detect DENV-2 capsid protein, but not a cross-reactive one with all serotypes of DENV capsid protein. The high diversity of the DENV capsid protein sequence by phylogenetic analysis supported the low cross-reactivity of monoclonal antibodies against DENV capsid protein.

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The Simian Retroviruses SIV and SRV

1994

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Identification of a Gag Protein Epitope Conserved Among All Four Groups of Primate Immunodeficiency Viruses by Using Monoclonal Antibodies

Cited by 7 publications

References 26 publications

Generation, characterization and cross-reactivities of monoclonal antibodies against the p24 core protein and the gp130 envelope glycoprotein of HIV-2ben

Generation, characterization and cross-reactivities of monoclonal antibodies against the p24 core protein and the gp130 envelope glycoprotein of HIV-2ben

Limited cross-reactivity of mouse monoclonal antibodies against Dengue virus capsid protein among four serotypes

The Simian Retroviruses SIV and SRV

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