Citation: FENG Hui-xing, HUANG Li-qin, GONG Rui, PENG Xiao-xue, KANG Shu-li, TIEN Po, XIAO Geng-fu*. Influence of Intramolecular Disulfide Bond on Fusion Core Structure of Envelope Protein of HERV .VIROLOGICA SINICA, 2006, 21(5) : 437-442.

Influence of Intramolecular Disulfide Bond on Fusion Core Structure of Envelope Protein of HERV

  • Available online: 20 September 2006
  • Syncytin, a captive retroviral envelope protein, is possibly involved in the morphogenesis of the placental syncytiotrophoblast layer generated by trophoblast cell fusion. It is found that syncytin and HIV-1 envelope proteins share similar structural profiles and membrane fusion mechanisms. In this article, we carried a mutagenesis by PCR to the conserved intramolecular disulfide bond of the linker between the heptad repeats HR1 and HR2 in the fusion core. We expressed and purified the mutant protein and subsequently the structure and stability were tested. After comparing the characteristics between the native and the mutant proteins, we got the concluded that this conserved intramolecular disulfide bond made a certain function in the correct protein structure formation and stability.

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    Influence of Intramolecular Disulfide Bond on Fusion Core Structure of Envelope Protein of HERV

    • 1. State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China

    Abstract: Syncytin, a captive retroviral envelope protein, is possibly involved in the morphogenesis of the placental syncytiotrophoblast layer generated by trophoblast cell fusion. It is found that syncytin and HIV-1 envelope proteins share similar structural profiles and membrane fusion mechanisms. In this article, we carried a mutagenesis by PCR to the conserved intramolecular disulfide bond of the linker between the heptad repeats HR1 and HR2 in the fusion core. We expressed and purified the mutant protein and subsequently the structure and stability were tested. After comparing the characteristics between the native and the mutant proteins, we got the concluded that this conserved intramolecular disulfide bond made a certain function in the correct protein structure formation and stability.

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