| Literature DB >> 28978437 |
Jinquan Chen1, Ruxia Ren2, Fei Yu3, Chunyan Wang4, Xuanxuan Zhang2, Wenjuan Li2, Suiyi Tan2, Shibo Jiang5, Shuwen Liu6, Lin Li7.
Abstract
Identification of the host or viral factors that enhance HIV infection is critical for preventing sexual transmission of HIV. Amyloid fibrils derived from human semen, including semen-derived enhancer of virus infection and semenogelins, enhance HIV-1 infection dramatically in vitro. In this study, we reported that a short-degraded peptide fragment 1 (DPF1) derived from native HIV-1 envelope protein gp120-loaded rat hepatocytes, formed fibrils by self-assembly and thus enhanced HIV-1 infection by promoting the binding of HIV-1 to target cells. Furthermore, DPF1-formed fibrils might be used as a crossing seed to accelerate the formation of semen-derived enhancer of virus infection and semenogelin fibrils. It will be helpful to clarify the viral factors that affect HIV-1 infection. DPF1 as an analog of gp120 containing the critical residues for CD4 binding might be useful for designing of HIV vaccines and developing HIV entry inhibitors.Entities:
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Year: 2017 PMID: 28978437 PMCID: PMC5627148 DOI: 10.1016/j.bpj.2017.08.005
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033