Journal
MOLECULAR MEDICINE
Volume 13, Issue 5-6, Pages 229-239Publisher
SPRINGER
DOI: 10.2119/2007-00004.Liang
Keywords
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Funding
- NIAID NIH HHS [R01 AI033776, R29 AI033776, R29 AI040891, AI33776, R21 AI033776, AI40891, R01 AI040891, R21 AI040891] Funding Source: Medline
- NIGMS NIH HHS [GM63080, R01 GM063080] Funding Source: Medline
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HIV-1 Vpr plays a pivotal role in viral pathogenesis and is preferentially targeted by the host immune system. In this report, we demonstrate that a small heat shock protein, HSP27, exhibits Vpr-specific antiviral activity, as its expression is specifically responsive to vpr gene expression and increased levels of HSP27 inhibit Vpr-induced cell cycle G2 arrest and cell killing. We further show that overexpression of HSP27 reduces viral replication in T-lymphocytes in a Vpr-dependent manner. Mechanistically, Vpr triggers HSP27 expression through heat shock factor (HSF) 1, but inhibits prolonged expression of HSP27 under heat-shock conditions. Together, these data suggest a potential dynamic and antagonistic interaction between HIV-1 Vpr and a host cell HSP27, suggesting that HSP27 may contribute to cellular intrinsic immunity against HIV infection,
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