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Published on: March 8, 2012
Linear B-cell epitopes of the major core protein of human immunodeficiency virus types 1 and 2
B Janvier1, P Archinard, B Mandrand
1Département de Microbiologie Médicale et Moléculaire, URA CNRS 1334, CHRU Bretonneau, Tours, France.
Insights
Researchers identified four linear epitopes on the human immunodeficiency virus type 1 (HIV-1) p24 core protein. Two conserved epitopes may aid in diagnosing and predicting outcomes of HIV-1 infections.
Area of Science:
- Immunology
- Virology
- Molecular Biology
Background:
- The human immunodeficiency virus type 1 (HIV-1) p24 major core protein is a key target for immune responses.
- Understanding the antigenic domains of p24 is crucial for developing diagnostic and therapeutic strategies.
Purpose of the Study:
- To characterize the antigenic domains of the HIV-1 p24 protein.
- To identify conserved epitopes for potential diagnostic and prognostic applications.
Main Methods:
- Epitope mapping using the Pepscan system on nine murine monoclonal antibodies against HIV-1 p24.
- Western blotting to assess cross-reactivity with HIV-2 and simian immunodeficiency virus (SIV) proteins.
Main Results:
- Four distinct linear epitopes were identified on the HIV-1 p24 protein.
- Three epitopes showed cross-reactivity with HIV-2 p26, while one was specific to HIV-1.
- The specific HIV-1 epitope sequence (179-188) is conserved across HIV-2 and SIV isolates, suggesting phylogenetic relevance.
- Two conserved epitopes (AAEWDRVHP and EIYKRWII) were identified as potentially immunogenic during natural infection.
Conclusions:
- The study successfully mapped linear epitopes on HIV-1 p24, revealing conserved regions across primate lentiviruses.
- Identified conserved epitopes hold promise for developing improved diagnostic and prognostic tools for HIV-1 infection.
Abstract:
Nine murine monoclonal antibodies directed to the major core protein p24 of human immunodeficiency virus type 1 (HIV-1) were obtained and then tested by using an epitope mapping system (Pepscan) covering the whole p24HIV1 protein to characterize antigenic domains. Four different linear epitopes were identified. Monoclonal antibodies recognizing three of these epitopes also reacted to p26HIV2 in Western blotting (immunoblotting). A monoclonal antibody specific for the fourth epitope, located at position 179 to 188 of the gag polyprotein p55HIV1 (human T-cell lymphotropic virus type 3B strain), did not react with HIV type 2 (HIV-2) core proteins. The corresponding sequence is constant in all known HIV-2 and simian immunodeficiency virus (SIV) isolates, including a very divergent SIV strain from African green monkeys (SIVagm/tyo). This observation may be relevant to the phylogeny of primate lentiviruses. Two of the conserved epitopes might be immunogenic during natural infection and could therefore be used for diagnosis and prognosis purposes. These two epitopes are AAEWDRVHP and EIYKRWII, starting at positions 209 and 260 of the polyprotein p55HIV1, respectively.
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