Hypervariable Epitope Constructs Representing Variability in Envelope Glycoprotein of SIV Induce a Broad Humoral Immune Response in Rabbits and Rhesus Macaques

1998 ◽  
Vol 14 (9) ◽  
pp. 751-760 ◽  
Author(s):  
DEBRA MEYER ◽  
DAVID E. ANDERSON ◽  
MURRAY B. GARDNER ◽  
JOSÉ V. TORRES
Keyword(s):  
Immune Response ◽  
Humoral Immune Response ◽  
Envelope Glycoprotein ◽  
Rhesus Macaques ◽  
Humoral Immune

scholarly journals DNA Encoding an HIV-1 Gag/Human Lysosome-Associated Membrane Protein-1 Chimera Elicits a Broad Cellular and Humoral Immune Response in Rhesus Macaques

PLoS ONE ◽  
2006 ◽  
Vol 1 (1) ◽  
pp. e135 ◽  
Author(s):  
Priya Chikhlikar ◽  
Luciana Barros de Arruda ◽  
Milton Maciel ◽  
Peter Silvera ◽  
Mark G. Lewis ◽  
...  
Keyword(s):  
Immune Response ◽  
Membrane Protein ◽  
Humoral Immune Response ◽  
Rhesus Macaques ◽  
Dna Encoding ◽  
Humoral Immune ◽  
Hiv 1

scholarly journals Sequential immunizations with rgp120s from independent isolates of human immunodeficiency virus type 1 induce the preferential expansion of broadly crossreactive B cells.

1991 ◽  
Vol 173 (4) ◽  
pp. 881-887 ◽  
Author(s):  
D M Klinman ◽  
K W Higgins ◽  
J Conover
Keyword(s):  
Immune Response ◽  
Human Immunodeficiency Virus ◽  
B Cells ◽  
Human Immunodeficiency Virus Type ◽  
Humoral Immune Response ◽  
Envelope Glycoprotein ◽  
Humoral Immune ◽  
Immunodeficiency Virus ◽  
Hiv 1

The gp120 envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) is a dominant target against which the host's humoral immune response is directed. Unfortunately, gp120 proteins from different isolates of HIV are antigenically distinct, complicating the use of the envelope glycoprotein in vaccines designed to prevent acquired immunodeficiency syndrome. Using an enzyme-linked immunosorbent spot assay (ELISA), BALB/c mice immunized and boosted with recombinant purified gp120 were studied at the single cell level for their humoral immune response to HIV-1 envelope proteins. Approximately 90% of responding B cells produced antibodies reactive with the immunizing form of gp120 but not with gp120s from other strains of HIV. A novel sandwich ELISA was then used to analyze the frequency with which individual in vivo activated B cells produced antibodies that crossreacted with heterologous gp120s. Repeated immunizations with a single gp120 or with a mixture of different gp120s resulted in the activation of primarily mono-specific (noncrossreactive) B cells. In contrast, the sequential immunization of mice with recombinant purified envelope proteins from different strains of HIV (IIIB, SF2, and Zr6) induced the selective expansion of B cells producing highly crossreactive antibodies.

Humoral Immune Response to Immunocomplexed HIV Envelope Glycoprotein 120

1996 ◽  
Vol 12 (10) ◽  
pp. 901-909 ◽  
Author(s):  
GALINA DENISOVA ◽  
BARUCH STERN ◽  
DAPHNA RAVIV ◽  
JUDITH ZWICKEL ◽  
NECHAMA I. SMORODINSKY ◽  
...  
Keyword(s):  
Immune Response ◽  
Humoral Immune Response ◽  
Envelope Glycoprotein ◽  
Humoral Immune ◽  
Hiv Envelope

scholarly journals Immunogenicity of HIV Virus-Like Particles in Rhesus Macaques by Intranasal Administration

2012 ◽  
Vol 19 (6) ◽  
pp. 970-973 ◽  
Author(s):  
Luigi Buonaguro ◽  
Maria Tagliamonte ◽  
Maria Luisa Visciano ◽  
Hanne Andersen ◽  
Mark Lewis ◽  
...  
Keyword(s):  
Immune Response ◽  
Humoral Immune Response ◽  
Intranasal Administration ◽  
Rhesus Macaques ◽  
Virus Like Particles ◽  
Humoral Immune ◽  
Hiv Dna ◽  
Hiv Virus ◽  
Female Rhesus ◽  
Female Rhesus Macaques

ABSTRACTFemale rhesus macaques were immunized with HIV virus-like particles (HIV-VLPs) or HIV DNA administered as sequential combinations of mucosal (intranasal) and systemic (intramuscular) routes, according to homologous or heterologous prime-boost schedules. The results show that in rhesus macaques only the sequential intranasal and intramuscular administration of HIV-VLPs, and not the intranasal alone, is able to elicit humoral immune response at the systemic as well as the vaginal level.

scholarly journals The Humoral Immune Response to Human T-Cell Lymphotropic Virus Type 1 Envelope Glycoprotein gp46 Is Directed Primarily against Conformational Epitopes

1999 ◽  
Vol 73 (2) ◽  
pp. 1205-1212 ◽  
Author(s):  
Kenneth G. Hadlock ◽  
Judy Rowe ◽  
Steven K. H. Foung
Keyword(s):  
Immune Response ◽  
Monoclonal Antibodies ◽  
T Cell ◽  
Humoral Immune Response ◽  
Envelope Glycoprotein ◽  
Humoral Immune ◽  
Conformational Epitopes ◽  
Human T Cell ◽  
Linear Epitopes

ABSTRACT Individuals infected with human T-cell lymphotropic virus type 1 (HTLV-1) develop a robust immune response to the surface envelope glycoprotein gp46 that is partially protective. The relative contribution of antibodies to conformation-dependent epitopes, including those mediating virus neutralization as part of the humoral immune response, is not well defined. We assess in this report the relationship between defined linear and conformational epitopes and the antibodies elicited to these domains. First, five monoclonal antibodies to linear epitopes within gp46 were evaluated for their ability to abrogate binding of three human monoclonal antibodies that inhibit HTLV-1-mediated syncytia formation and recognize conformational epitopes. Binding of antibodies to conformational epitopes was unaffected by antibodies to linear epitopes throughout the carboxy-terminal half and central domain of HTLV-1 gp46. Second, an enzyme-linked immunoadsorbent assay was developed and used to measure serum antibodies to native and denatured gp46 from HTLV-1-infected individuals. In sera from infected individuals, reactivity to denatured gp46 had an average of 15% of the reactivity observed to native gp46. Third, serum antibodies from 24 of 25 of HTLV-1-infected individuals inhibited binding of a neutralizing human monoclonal antibody, PRH-7A, to a conformational epitope on gp46 that is common to HTLV-1 and -2. Thus, antibodies to conformational epitopes comprise the majority of the immune response to HTLV-1 gp46, and the epitopes recognized by these antibodies do not appear to involve sequences in previously described immunodominant linear epitopes.

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