Recombinant peptides derived from the env-gene of HIV-2 in the serodiagnosis of HIV-2 infections

Schulz, Thomas F.; Oberhuber, W.; J, Hofbauer; Hengster, Paul; Larcher, Clara; Gürtler, Leo; Tedder, Richard S.; Wachter, H; Dierich, Manfred P.

doi:10.1097/00002030-198903000-00007

Cited by 14 publications

(8 citation statements)

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“…The mean S/CO ratio was significantly higher for the rgp36 antigen than that for rpC2-C3 (8.27 [SD, 1.49] versus 4.89 [SD, 2.51]; P Ͻ 0.0001). These results suggest that the gp36 ectodomain is the immunodominant antigenic region in the HIV-2 envelope and are consistent with previous studies showing that recombinant gp36 proteins derived from several laboratory strains of HIV-2 are highly immunogenic (18,40,50). Most commercial and homemade ELISAs report similar sensitivities using substantially more sera per reaction compared to our assay (50 to 200 l versus 1 l) (38,43,48).…”

supporting

confidence: 91%

“…Six immunogenic regions were identified in the HIV-2 envelope glycoproteins: three in gp125 (amino acids 234 to 248 in C2, 296 to 337 in V3, and 472 to 507 in C5) and three in the gp36 ectodomain (amino acids 573 to 595, 634 to 649, and 644 to 658) (11,13,18,27,30,34,40,50). The gp36 ectodomain is highly conserved and elicits a type-specific antibody response (13,33).…”

mentioning

confidence: 99%

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Use of a New Dual-Antigen Enzyme-Linked Immunosorbent Assay To Detect and Characterize the Human Antibody Response to the Human Immunodeficiency Virus Type 2 Envelope gp125 and gp36 Glycoproteins

et al. 2006

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A dual-antigen enzyme-linked immunosorbent assay specific for human immunodeficiency virus type 2 (HIV-2) envelope proteins, ELISA-HIV2, was developed with two new recombinant polypeptides, rpC2-C3 and rgp36, derived from the HIV-2 envelope. The diagnostic performance was determined with HIV-2, HIV-1, and HIV-1/2 samples. Both polypeptides showed 100% specificity. Clinical sensitivity was 100% for rgp36 and 93.4% for rpC2-C3. ELISA-HIV2 may be used for the specific diagnosis and confirmation of HIV-2 infection.

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confidence: 91%

mentioning

confidence: 99%

Use of a New Dual-Antigen Enzyme-Linked Immunosorbent Assay To Detect and Characterize the Human Antibody Response to the Human Immunodeficiency Virus Type 2 Envelope gp125 and gp36 Glycoproteins

et al. 2006

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“…Furthermore, six immunogenic regions have been identified in the HIV-2 envelope glycoproteins. Three of them are in gp125 (amino acids 234 to 248 in C2, 296 to 337 in V3, and 472 to 507 in C5), and the others are in the ectodomain of gp36 (amino acids 573 to 595, 634 to 649, and 644 to 658) [42][43][44][45][46][47][48][49][50]. Recently, Barroso and his co-workers have shown that the HIV-2 C2 and C3 are well exposed in the envelope complex and are under strong diversifying selection [41].…”

Section: Introductionmentioning

confidence: 99%

HIV-2 A-subtype gp125C2-V3-C3 mutations and their association with CCR5 and CXCR4 tropism

et al. 2011

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The early events of the HIV replication cycle involve the interaction between viral envelope glycoproteins and their cellular CD4-chemokine (CCR5/CXCR4) receptor complex. In this study, for the first time, the HIV-2 A-subtype gp125 C2-V3-C3 mutations and their tropism association were characterized by analyzing 149 HIV-2 sequences from the Los Alamos database. The analysis has strengthened the importance of C2-V3-C3 region as a determinant factor for co-receptor selection. Moreover, statistically significant correlations were observed between C2-V3-C3 mutations, and several correlated mutations were associated with CXCR4 and CCR5 co-receptor usage. A dendrogram showed two distinct clusters, with numerous associated mutations grouped, thus dividing CCR5-and CXCR4-tropic viruses. Fourteen X4-tropic virus mutations, all in V3 and C3 domains and forming highly significant subclusters, were found. Finally, R5 associations, two strong subclusters were observed, grouping several C2-V3-C3 mutated positions. These data indicate the possible contribution of C2-V3-C3 mutational patterns in regulating HIV-2 tropism.

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“…"12 The low antigenic cross reactivity between the env exterior glycoprotein of HIV-1 compared with HIV-2 and SIV, provided the basis for the sérologie detection of HIV-2, followed by isolation and characterization of the virus.5-1U3-'6 However, antigenic cross reactivity between HIV-1 and HIV-2 env glycoproteins evident in selected sérologie assays decreases or complicates the utility of full-length envelope gene products as discriminatory targets. [17][18][19][20] As an alternative to full-length envelope proteins, synthetic (poly)peptides derived from the immunodominant regions (IDR) of HIV-1 and HIV-2 transmembrane proteins have been employed as serological targets in enzyme immunoassays (ElA) to discriminate between individuals seropositive to HIV-1 and HIV-2.21"26 Site-directed serology employing these small immunodominant regions with limited sequence homology limits the potential for antigenic cross reactivity apparently found within the full-length native or recombinant TMPs. The lack of antigenic cross reactivity between IDR peptides also was demonstrated when they were employed as competitive inhibitors against human antibodies specific for the immunodominant regions.22 Monoclonal antibodies, directed to specific epitopes within selected serological targets, may be employed as competitive probes against human serum antibody to achieve site-directed serology.…”

Section: Introductionmentioning

confidence: 99%

Discrimination Between HIV-1 and HIV-2-Seropositive Individuals Using Mouse Monoclonal Antibodies Directed to HIV Transmembrane Proteins

Hunt¹,

Johnson-Paepke²,

Boardway³

et al. 1990

AIDS Research and Human Retroviruses

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Mouse monoclonal antibodies directed against the transmembrane proteins of HIV-1 or HIV-2 provided site-directed, unambiguous discrimination between HIV-1 and HIV-2 antibody-positive sera, when employed in immunoassays as competitive probes against serum antibodies. These monoclonal antibodies mapped to epitopes outside of the well-characterized immunodominant regions (IDR) of the transmembrane proteins. The monoclonal competitive immunoassay was a superior method for discrimination compared with immunoprecipitation of metabolically radiolabeled HIV envelope glycoproteins, Western blot against viral envelope glycoproteins, or noncompetitive enzyme immunoassays employing HIV recombinant transmembrane proteins or synthetic IDR peptides as serological targets. The monoclonal competitive assay was not affected by antigenic cross reactivity or nonspecific reactivity exhibited by selected serum samples toward envelope proteins or peptides, respectively. Results of the monoclonal competitive immunoassay were supported by results of a peptide inhibition assay employing free IDR peptides in competition with IDR peptides on a solid support for binding of serum antibody. IDR peptide inhibition clearly demonstrated non-cross-reactive antigenic specificity of sera toward either the HIV-1 IDR or the HIV-2 IDR. The monoclonal competitive assay also identified samples containing antibody to both HIV-1 and HIV-2 transmembrane proteins. Analysis of these samples by IDR peptide inhibition indicated they contained two distinct, non-cross-reactive populations of antibodies, one directed to the HIV-1 IDR and the other directed to the HIV-2 IDR.

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Recombinant peptides derived from the env-gene of HIV-2 in the serodiagnosis of HIV-2 infections

Cited by 14 publications

References 0 publications

Use of a New Dual-Antigen Enzyme-Linked Immunosorbent Assay To Detect and Characterize the Human Antibody Response to the Human Immunodeficiency Virus Type 2 Envelope gp125 and gp36 Glycoproteins

Use of a New Dual-Antigen Enzyme-Linked Immunosorbent Assay To Detect and Characterize the Human Antibody Response to the Human Immunodeficiency Virus Type 2 Envelope gp125 and gp36 Glycoproteins

HIV-2 A-subtype gp125C2-V3-C3 mutations and their association with CCR5 and CXCR4 tropism

Discrimination Between HIV-1 and HIV-2-Seropositive Individuals Using Mouse Monoclonal Antibodies Directed to HIV Transmembrane Proteins

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