http://www.cnr.it/ontology/cnr/individuo/prodotto/ID9082

HIV-1 Gag p17 presented as virus-like particles on the E2 scaffold from Geobacillus stearothermophilus induces sustained humoral and cellular immune responses in the absence of IFN³ production by CD4+ T cells (Articolo in rivista)

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HIV-1 Gag p17 presented as virus-like particles on the E2 scaffold from Geobacillus stearothermophilus induces sustained humoral and cellular immune responses in the absence of IFN³ production by CD4+ T cells (Articolo in rivista) (literal)

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Alternative label

Caivano A.; Doria-Rose N.A.; Buelow B.; Sartorius R.; Trovato M., D'Apice L.; Domingo G.J.; Sutton W.F.; Haigwood N.L.; De Berardinis P. (2010)
HIV-1 Gag p17 presented as virus-like particles on the E2 scaffold from Geobacillus stearothermophilus induces sustained humoral and cellular immune responses in the absence of IFN³ production by CD4+ T cells
in Virology (N.Y.N.Y., Print); Elsevier, Amsterdam (Paesi Bassi)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Caivano A.; Doria-Rose N.A.; Buelow B.; Sartorius R.; Trovato M., D'Apice L.; Domingo G.J.; Sutton W.F.; Haigwood N.L.; De Berardinis P. (literal)

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Institute of Protein Biochemistry, C.N.R., via P. Castellino 111, 80131 Naples, Italy Seattle Biomedical Research Institute, 307 Westlake Av, Seattle, WA 98109-5240, USA Dept. of Molecular and Cell Biology, University of Washington, Seattle, WA 98124-6108, USA Dept. of Pathobiology, University of Washington, Seattle, WA 98124-6108, USA (literal)

Titolo

HIV-1 Gag p17 presented as virus-like particles on the E2 scaffold from Geobacillus stearothermophilus induces sustained humoral and cellular immune responses in the absence of IFN³ production by CD4+ T cells (literal)

Abstract

We have constructed stable virus-like particles displaying the HIV-1 Gag(p17) protein as an N-terminal fusion with an engineered protein domain from the Geobacillus stearothermophilus pyruvate dehydrogenase subunit E2. Mice immunized with the Gag(p17)-E2 60-mer scaffold particles mounted a strong and sustained antibody response. Antibodies directed to Gag(p17) were boosted significantly with additional immunizations, while anti-E2 responses reached a plateau. The isotype of the induced antibodies was biased towards IgG1, and the E2-primed CD4+ T cells did not secrete IFN³. Using transgenic mouse model systems, we demonstrated that CD8+ T cells primed with E2 particles were able to exert lytic activity and produce IFN³. These results show that the E2 scaffold represents a powerful vaccine delivery system for whole antigenic proteins or polyepitope engineered proteins, evoking antibody production and antigen specific CTL activity even in the absence of IFN³-producing CD4+ T cells. (literal)

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