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CTL Escape Mediated by Proteasomal Destruction of an HIV-1 Cryptic
Epitope


Cytotoxic CD8+ T cells (CTLs) play a critical role in controlling viral

infections. HIV-infected individuals develop CTL responses against epitopes

derived from viral proteins, but also against cryptic epitopes encoded by viral

alternative reading frames (ARF). We studied here the mechanisms of HIV-1 escape

from CTLs targeting one such cryptic epitope, Q9VF, encoded by an

HIVgag ARF and presented by HLA-B*07. Using PBMCs of

HIV-infected patients, we first cloned and sequenced proviral DNA encoding for

Q9VF. We identified several polymorphisms with a minority of proviruses encoding

at position 5 an aspartic acid (Q9VF/5D) and a majority encoding an asparagine

(Q9VF/5N). We compared the prevalence of each variant in PBMCs of

HLA-B*07+ and HLA-B*07- patients. Proviruses encoding Q9VF/5D were

significantly less represented in HLA-B*07+ than in HLA-B*07-

patients, suggesting that Q9FV/5D encoding viruses might be under selective

pressure in HLA-B*07+ individuals. We thus analyzed ex

vivo
CTL responses directed against Q9VF/5D and Q9VF/5N. Around

16% of HLA-B*07+ patients exhibited CTL responses targeting Q9VF

epitopes. The frequency and the magnitude of CTL responses induced with Q9VF/5D

or Q9VF/5N peptides were almost equal indicating a possible cross-reactivity of

the same CTLs on the two peptides. We then dissected the cellular mechanisms

involved in the presentation of Q9VF variants. As expected, cells infected with

HIV strains encoding for Q9VF/5D were recognized by Q9VF/5D-specific CTLs. In

contrast, Q9VF/5N-encoding strains were neither recognized by Q9VF/5N- nor by

Q9VF/5D-specific CTLs. Using in vitro proteasomal digestions

and MS/MS analysis, we demonstrate that the 5N variation introduces a strong

proteasomal cleavage site within the epitope, leading to a dramatic reduction of

Q9VF epitope production. Our results strongly suggest that HIV-1 escapes CTL

surveillance by introducing mutations leading to HIV ARF-epitope destruction by

proteasomes.


Vyšlo v časopise: CTL Escape Mediated by Proteasomal Destruction of an HIV-1 Cryptic Epitope. PLoS Pathog 7(5): e32767. doi:10.1371/journal.ppat.1002049
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1002049

Souhrn

Cytotoxic CD8+ T cells (CTLs) play a critical role in controlling viral

infections. HIV-infected individuals develop CTL responses against epitopes

derived from viral proteins, but also against cryptic epitopes encoded by viral

alternative reading frames (ARF). We studied here the mechanisms of HIV-1 escape

from CTLs targeting one such cryptic epitope, Q9VF, encoded by an

HIVgag ARF and presented by HLA-B*07. Using PBMCs of

HIV-infected patients, we first cloned and sequenced proviral DNA encoding for

Q9VF. We identified several polymorphisms with a minority of proviruses encoding

at position 5 an aspartic acid (Q9VF/5D) and a majority encoding an asparagine

(Q9VF/5N). We compared the prevalence of each variant in PBMCs of

HLA-B*07+ and HLA-B*07- patients. Proviruses encoding Q9VF/5D were

significantly less represented in HLA-B*07+ than in HLA-B*07-

patients, suggesting that Q9FV/5D encoding viruses might be under selective

pressure in HLA-B*07+ individuals. We thus analyzed ex

vivo
CTL responses directed against Q9VF/5D and Q9VF/5N. Around

16% of HLA-B*07+ patients exhibited CTL responses targeting Q9VF

epitopes. The frequency and the magnitude of CTL responses induced with Q9VF/5D

or Q9VF/5N peptides were almost equal indicating a possible cross-reactivity of

the same CTLs on the two peptides. We then dissected the cellular mechanisms

involved in the presentation of Q9VF variants. As expected, cells infected with

HIV strains encoding for Q9VF/5D were recognized by Q9VF/5D-specific CTLs. In

contrast, Q9VF/5N-encoding strains were neither recognized by Q9VF/5N- nor by

Q9VF/5D-specific CTLs. Using in vitro proteasomal digestions

and MS/MS analysis, we demonstrate that the 5N variation introduces a strong

proteasomal cleavage site within the epitope, leading to a dramatic reduction of

Q9VF epitope production. Our results strongly suggest that HIV-1 escapes CTL

surveillance by introducing mutations leading to HIV ARF-epitope destruction by

proteasomes.


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Hygiena a epidemiológia Infekčné lekárstvo Laboratórium

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