The Brazilian variant of human immunodeficiency virus type 1 (HIV-1) subtype B, (serotype B"-GWGR), has a tryptophan replacing the proline in position 328 the HIV-1 envelope. A longer median time period from infection to acquired immunodeficiency syndrome (AIDS) for serotype B (B"-GWGR) infected subjects compared to the B-GPGR US/European strain was reported. In a cohort study, in São Paulo city, 10 B"-GWGR patients had a statistically significant increased avidity of the anti-V3 antibodies, from 79% +/- 33% to 85% +/- 75%, versus from 48% +/- 59% to 32% +/- 17% for the 10 B-GPGR subjects (p = 0.02). The T CD4+ cells showed a mean increase of + 0.45 cells/month for the B-GPGR subjects and for B"-GWGR the slope was + 1.24 cells/month (p = 0.06), for 62 and 55 months of follow up, respectively. RNA plasma viral load decreased from 3.98 +/- 1.75 to 2.16 +/- 1.54 log10 in the B"-GWGR group while B-GPGR patients showed one log10 reduction in viral load from 4.09 +/- 0.38 to 3.17 +/- 1.47 log10 over time (p = 0.23), with a decreasing slope of 0.0042 +/- log10,/month and 0.0080 +/- log10/month, for B-GPGR and B"-GWGR patients, respectively (p = 0.53). Neither group presented any AIDS defining events during the study, according to Center for Diseases Control criteria. Although the sample size is small, these results may indicate that differences in the pathogenicity of the 2 HIV-1 B serotypes which co-circulate in Brazil may be correlated to the avidity of anti-V3 antibodies.
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http://dx.doi.org/10.1590/s0074-02762004000100012 | DOI Listing |
Vaccine
November 2013
VA New York Harbor Healthcare System, Manhattan Campus and New York University School of Medicine, Department of Pathology, New York, NY 10010, United States.
HIV-1 envelope gp120 is the target for neutralizing antibodies (NAbs) against the virus. Various approaches have been explored to improve immunogenicity of broadly neutralizing epitopes on this antigen with limited success. We previously demonstrated that immunogenicity of gp120 and especially its V3 epitopes was enhanced when gp120 was co-administered as immune-complex vaccines with monoclonal antibodies (mAb) to the CD4-binding site (CD4bs).
View Article and Find Full Text PDFMem Inst Oswaldo Cruz
February 2004
Laboratório de Alergia e Imunologia Clínica e Experimental, Faculdade de Medicina, Universidade de São Paulo, São Paulo, SP, 05403-000, Brasil.
The Brazilian variant of human immunodeficiency virus type 1 (HIV-1) subtype B, (serotype B"-GWGR), has a tryptophan replacing the proline in position 328 the HIV-1 envelope. A longer median time period from infection to acquired immunodeficiency syndrome (AIDS) for serotype B (B"-GWGR) infected subjects compared to the B-GPGR US/European strain was reported. In a cohort study, in São Paulo city, 10 B"-GWGR patients had a statistically significant increased avidity of the anti-V3 antibodies, from 79% +/- 33% to 85% +/- 75%, versus from 48% +/- 59% to 32% +/- 17% for the 10 B-GPGR subjects (p = 0.
View Article and Find Full Text PDFInt J Infect Dis
November 1998
Instituto de Medicina Tropical Pedro Kourí, Ciudad Havana, Cuba.
Objectives: A retrospective study was conducted to evaluate the antibody response of Cuban patients infected with human immunodeficiency virus (HIV)-1 against two consensus peptides from the third variable domain (V3) loop of glycoprotein gp120.
Methods: The study included sera from 10 individuals at different stages of disease. Two 15-meric synthetic peptides designed from a consensus sequence, belonging to group B or C of HIV-1, were used to determine antibody titers and avidity indexes in an indirect enzyme-linked immunoassay.
Mol Immunol
April 1994
CNRS URA 1455, Laboratoire de Biochimie, Faculté de Médecine Nord, Marseille, France.
The V2 region of simian immunodeficiency virus (SIV) and V3 region of human immunodeficiency virus type 1 (HIV-1) have been reported to be neutralization epitopes. We analysed the corresponding regions in HIV-2. Synthetic peptides modeling the V2 (aa 149-168) and V3 (CV3: aa 298-315 and NV3: aa 306-324) regions of the HIV-2 external envelope glycoprotein were coupled to KLH and used as immunogens in rabbits.
View Article and Find Full Text PDFFEBS Lett
March 1994
Laboratoire de Biologie et Génétique des Pathologies Immunitaires, CNRS URA, Faculté de Médecine Pitié-Salpêtrière, Paris, France.
The gp160 envelope glycoprotein of human immunodeficiency virus type-1 (HIV-1) is an essential component of current vaccine trials. The glycans of gp160, part of which are highly sialylated, have been shown to influence gp160 immunogenicity. Here, using a panel of synthetic V3 peptides, we characterized the anti-V3 antibodies generated in rabbits immunized by desialylated recombinant gp160LAI.
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