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Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection.

Heat shock proteins (hsps) and cyclophilins (CypA) are intracellular chaperone molecules that facilitate protein folding and assembly. These proteins are selectively expressed in cells following exposure to a range of stress stimuli, including viral infection. Hsp species are highly immunogenic, eli...

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Detalles Bibliográficos
Autores principales: Brenner, B G, Wainberg, M A
Formato: Texto
Lenguaje:English
Publicado: 1999
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1784721/
https://www.ncbi.nlm.nih.gov/pubmed/10231014
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author Brenner, B G
Wainberg, M A
author_facet Brenner, B G
Wainberg, M A
author_sort Brenner, B G
collection PubMed
description Heat shock proteins (hsps) and cyclophilins (CypA) are intracellular chaperone molecules that facilitate protein folding and assembly. These proteins are selectively expressed in cells following exposure to a range of stress stimuli, including viral infection. Hsp species are highly immunogenic, eliciting humoral, cytotoxic T lymphocyte (CTL), and natural killer (NK) cell responses against viruses, tumours, and infectious diseases. This review discusses the roles of stress proteins in immunity and viral life cycles, vis-à-vis the development of Hsp-based therapeutic strategies against human immunodeficiency virus type-1 (HIV-1) infection. Cumulative findings are cited implicating the requirement of CypA in HIV-1 replication and formation of infectious virions. Studies by our group show the upregulated expression of hsp27 and hsp70 during single-cycle HIV infections. These species redistribute to the cell surface following HIV-infection and heat stress, serving as targets for NK and antibody-dependent cellular cytotoxicity. Co-immunoprecipitation and Western blot studies show that hsp27, hsp70, and hsp78 complex with HIV-1 viral proteins intracellularly. Hsp70, hsp56, and CypA are assembled into HIV-1 virions. The ability of hsps to interact with HIV-1 viral proteins, combined with their inherent adjuvant and immunogenic properties, indicates that hsps may serve as vehicles for antigen delivery and the design of vaccines against acquired immunodeficiency syndrome.
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spelling pubmed-17847212007-02-05 Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection. Brenner, B G Wainberg, M A Infect Dis Obstet Gynecol Research Article Heat shock proteins (hsps) and cyclophilins (CypA) are intracellular chaperone molecules that facilitate protein folding and assembly. These proteins are selectively expressed in cells following exposure to a range of stress stimuli, including viral infection. Hsp species are highly immunogenic, eliciting humoral, cytotoxic T lymphocyte (CTL), and natural killer (NK) cell responses against viruses, tumours, and infectious diseases. This review discusses the roles of stress proteins in immunity and viral life cycles, vis-à-vis the development of Hsp-based therapeutic strategies against human immunodeficiency virus type-1 (HIV-1) infection. Cumulative findings are cited implicating the requirement of CypA in HIV-1 replication and formation of infectious virions. Studies by our group show the upregulated expression of hsp27 and hsp70 during single-cycle HIV infections. These species redistribute to the cell surface following HIV-infection and heat stress, serving as targets for NK and antibody-dependent cellular cytotoxicity. Co-immunoprecipitation and Western blot studies show that hsp27, hsp70, and hsp78 complex with HIV-1 viral proteins intracellularly. Hsp70, hsp56, and CypA are assembled into HIV-1 virions. The ability of hsps to interact with HIV-1 viral proteins, combined with their inherent adjuvant and immunogenic properties, indicates that hsps may serve as vehicles for antigen delivery and the design of vaccines against acquired immunodeficiency syndrome. 1999 /pmc/articles/PMC1784721/ /pubmed/10231014 Text en
spellingShingle Research Article
Brenner, B G
Wainberg, M A
Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection.
title Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection.
title_full Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection.
title_fullStr Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection.
title_full_unstemmed Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection.
title_short Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection.
title_sort heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1784721/
https://www.ncbi.nlm.nih.gov/pubmed/10231014
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