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Glycobiology. 2014 Nov;24(11):1022-35. doi: 10.1093/glycob/cwu064. Epub 2014 Jul 4.

Galectin-3 promotes HIV-1 budding via association with Alix and Gag p6.

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Department of Medical Laboratory Science and Biotechnology Institute of Biomedical Sciences Center for AIDS Prevention and Research.
Institute of Biomedical Sciences.
Center for AIDS Prevention and Research.
Institute of Biomedical Sciences Department of Dermatology, University of California at Davis, Davis, USA.
Department of Optics and Photonics, National Central University, Chung-Li, Taiwan.
Research Center for Applied Sciences, Academia Sinica, Taipei, Taiwan.
Department of Microbiology, College of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan Center for AIDS Prevention and Research Department of Microbiology, School of Medicine, National Yang-Ming University, Taipei, Taiwan
Institute of Biomedical Sciences Department of Dermatology, University of California at Davis, Davis, USA


Galectin-3 has been reported to regulate the functions of a number of immune cell types. We previously reported that galectin-3 is translocated to immunological synapses in T cells upon T-cell receptor engagement, where it associates with ALG-2-interacting protein X (Alix). Alix is known to coordinate with the endosomal sorting complex required for transport (ESCRT) to promote human immunodeficiency virus (HIV)-1 virion release. We hypothesized that galectin-3 plays a role in HIV-1 viral budding. Cotransfection of cells of the Jurkat T line with galectin-3 and HIV-1 plasmids resulted in increased HIV-1 budding, and suppression of galectin-3 expression by RNAi in Hut78 and primary CD4+ T cells led to reduced HIV-1 budding. We used immunofluorescence microscopy to observe the partial colocalization of galectin-3, Alix and Gag in HIV-1-infected cells. Results from co-immunoprecipitation experiments indicate that galectin-3 expression promotes Alix-Gag p6 association, whereas the results of Alix knockdown suggest that galectin-3 promotes HIV-1 budding through Alix. HIV-1 particles released from galectin-3-expressing cells acquire the galectin-3 protein in an Alix-dependent manner, with proteins primarily residing inside the virions. We also found that the galectin-3 N-terminal domain interacts with the proline-rich region of Alix. Collectively, these results suggest that endogenous galectin-3 facilitates HIV-1 budding by promoting the Alix-Gag p6 association.


Alix; HIV-1; galectin-3; viral budding

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