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gp120-derived amyloidogenic peptides form amyloid fibrils that increase HIV-1 infectivity

Cellular & Molecular Immunology (2024)Cite this article

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Abstract

Apart from mediating viral entry, the function of the free HIV-1 envelope protein (gp120) has yet to be elucidated. Our group previously showed that EP2 derived from one β-strand in gp120 can form amyloid fibrils that increase HIV-1 infectivity. Importantly, gp120 contains ~30 β-strands. We examined whether gp120 might serve as a precursor protein for the proteolytic release of amyloidogenic fragments that form amyloid fibrils, thereby promoting viral infection. Peptide array scanning, enzyme degradation assays, and viral infection experiments in vitro confirmed that many β-stranded peptides derived from gp120 can indeed form amyloid fibrils that increase HIV-1 infectivity. These gp120-derived amyloidogenic peptides, or GAPs, which were confirmed to form amyloid fibrils, were termed gp120-derived enhancers of viral infection (GEVIs). GEVIs specifically capture HIV-1 virions and promote their attachment to target cells, thereby increasing HIV-1 infectivity. Different GAPs can cross-interact to form heterogeneous fibrils that retain the ability to increase HIV-1 infectivity. GEVIs even suppressed the antiviral activity of a panel of antiretroviral agents. Notably, endogenous GAPs and GEVIs were found in the lymphatic fluid, lymph nodes, and cerebrospinal fluid (CSF) of AIDS patients in vivo. Overall, gp120-derived amyloid fibrils might play a crucial role in the process of HIV-1 infectivity and thus represent novel targets for anti-HIV therapeutics.

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Acknowledgements

We thank Yelena Oksov for her help in performing the TEM experiment. This work was supported by grants from the Natural Science Foundation of China (82072276 and 81772194 to ST, 82073898 and 31370781 to SL, and 81630090 to SJ).

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  1. These authors contributed equally: Suiyi Tan, Wenjuan Li, Chan Yang.

Authors and Affiliations

  1. Guangdong-Hong Kong-Macao Joint Laboratory for New Drug Screening, NMPA Key Laboratory for Research and Evaluation of Drug Metabolism, Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, 510515, China

    Suiyi Tan, Wenjuan Li, Chan Yang, Qingping Zhan, Kunyu Lu, Jinqing Li, Zhaofeng Li, Lin Li & Shuwen Liu

  2. Department of Infectious Disease, The Third People’s Hospital of Kunming, Kunming, 650041, China

    Jun Liu, Yong-Mei Jin & Jin-Song Bai

  3. Department of Pathology, The Third People’s Hospital of Kunming, Kunming, 650041, China

    Lin Wang

  4. Hebei Key Laboratory of Analysis and Control of Zoonotic Pathogenic Microorganism, College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China

    Fei Yu

  5. Department of Dermatology and Venereology, First Affiliated Hospital of Kunming Medical University, Kunming, 650032, China

    Yu-Ye Li

  6. Yunnan Provincial Infectious Disease Hospital, Kunming, 650301, China

    Yue-Xun Duan

  7. Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, School of Basic Medical Sciences, Fudan University, Shanghai, 200032, China

    Lu Lu & Shibo Jiang

  8. Beijing Key Laboratory for HIV/AIDS Research, Clinical and Research Center for Infectious Diseases, Beijing Youan Hospital, Capital Medical University, Beijing, 100069, China

    Tong Zhang & Jiaqi Wei

  9. State Key Laboratory of Genetic Evolution & Animal Models, Key Laboratory of Bioactive Peptides of Yunnan Province, KIZ-CUHK Joint Laboratory of Bioresources and Molecular Research in Common Diseases, Center for Biosafety Mega-Science, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan, 650223, China

    Yong-Tang Zheng

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Contributions

S.T., S.L., and S.J. conceived the study. S.T., W.L., C.Y., S.L., and S.J. contributed to the methodology. S.T., W.L., C.Y., Q.Z., K.L., J.L., Z.L., and F.Y. performed the experiments and analyzed the data. Y.Y.L., Y.X.D., J.L., Y.M.J., J.S.B., L.W., Y.T.Z., T.Z., and J.W. collected the clinical samples. S.T., S.L., and S.J. acquired the funding S.T., S.L., and S.J. supervised the study. S.T., W.L., and C.Y. drafted the manuscript. S.T., S.L., S.J., L.L., and L.L. reviewed and edited the manuscript.

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Correspondence to Suiyi Tan, Shibo Jiang or Shuwen Liu.

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Tan, S., Li, W., Yang, C. et al. gp120-derived amyloidogenic peptides form amyloid fibrils that increase HIV-1 infectivity. Cell Mol Immunol (2024). https://doi.org/10.1038/s41423-024-01144-y

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