2. Academic Validation
  3. An amphipathic peptide targeting the gp41 cytoplasmic tail kills HIV-1 virions and infected cells

An amphipathic peptide targeting the gp41 cytoplasmic tail kills HIV-1 virions and infected cells

  • Sci Transl Med. 2020 Jun 3;12(546):eaaz2254. doi: 10.1126/scitranslmed.aaz2254.
Qian Wang 1,  Shan Su 1,  Jing Xue 2,  Fei Yu 3,  Jing Pu 1,  Wenwen Bi 1,  Shuai Xia 1,  Yu Meng 1,  Cong Wang 1,  Wenqian Yang 1,  Wei Xu 1,  Yun Zhu 4,  Qinwen Zheng 1,  Chuan Qin 5,  Shibo Jiang 6 7,  Lu Lu 6
Affiliations

Affiliations

  • 1 Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, 130 Dong An Rd., Xuhui District, Shanghai 200032, China.
  • 2 Key Laboratory of Human Disease Comparative Medicine, Chinese Ministry of Health, Beijing Key Laboratory for Animal Models of Emerging and Re-emerging Infectious Diseases, Institute of Laboratory Animal Science, Chinese Academy of Medical Sciences and Comparative Medicine Center, Peking Union Medical College, Beijing 100021, China.
  • 3 College of Life and Science, Hebei Agricultural University, Baoding 071001, China.
  • 4 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • 5 Key Laboratory of Human Disease Comparative Medicine, Chinese Ministry of Health, Beijing Key Laboratory for Animal Models of Emerging and Re-emerging Infectious Diseases, Institute of Laboratory Animal Science, Chinese Academy of Medical Sciences and Comparative Medicine Center, Peking Union Medical College, Beijing 100021, China. lul@fudan.edu.cn shibojiang@fudan.edu.cn qinchuan@pumc.edu.cn.
  • 6 Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, 130 Dong An Rd., Xuhui District, Shanghai 200032, China. lul@fudan.edu.cn shibojiang@fudan.edu.cn qinchuan@pumc.edu.cn.
  • 7 Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USA.
PMID: 32493792 DOI: 10.1126/scitranslmed.aaz2254
Abstract

HIV-associated morbidity and mortality have markedly declined because of combinational antiretroviral therapy, but HIV readily mutates to develop drug resistance. Developing antivirals against previously undefined targets is essential to treat existing drug-resistant HIV strains. Some Peptides derived from HIV-1 envelope glycoprotein (Env, gp120-gp41) have been shown to be effective in inhibiting HIV-1 Infection. Therefore, we screened a peptide library from HIV-1 Env and identified a peptide from the cytoplasmic region, designated F9170, able to effectively inactivate HIV-1 virions and induce necrosis of HIV-1-infected cells, and reactivated latently infected cells. F9170 specifically targeted the conserved cytoplasmic tail of HIV-1 Env and effectively disrupted the integrity of the viral membrane. Short-term monoadministration of F9170 controlled viral loads to below the limit of detection in chronically SHIV-infected macaques. F9170 can enter the brain and lymph nodes, anatomic reservoirs for HIV latency. Therefore, F9170 shows promise as a drug candidate for HIV treatment.

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Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-P10310
    HIV inhibitor
    HIV