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Start Over Author "Fengwen Xu" Journal retrovirology
4 results on '"Fengwen Xu"'

1. The interferon-induced MxB protein inhibits an early step of HIV-1 infection

Author

Fengwen Xu, Jin Qian, Chen Liang, Shan Cen, Shilei Ding, Zhenlong Liu, Fei Guo, Jinming Zhou, and Qinghua Pan

Subjects
biology, business.industry, RNA, Virology, Virus, chemistry.chemical_compound, Infectious Diseases, Protein structure, chemistry, Interferon, Poster Presentation, biology.protein, Medicine, Antibody, business, Gene, DNA, Function (biology), medicine.drug
Abstract

Background Interferon protects cells from virus infection by inducing the expression of genes with antiviral activities. One such antiviral gene is Mx (myxovirus resistance) that was first identified in mice for its protection against influenza virus infection. Humans carry two Mx genes, MxA and MxB. Although MxA has been reported to inhibit a number of RNA and DNA viruses, the antiviral function of MxB has just begun to be revealed.

Published
2013

2. Identification of novel key amino acids at the interface of the transmembrane domains of human BST-2 and HIV-1 Vpu

Author

Jinming Zhou, Qi Jin, Shan Mei, Fengwen Xu, Siqi Hu, Shan Cen, Fei Guo, Jian Li, and Xiao-Jing Pang

Subjects
Bioluminescence Resonance Energy Transfer Techniques, Models, Molecular, animal diseases, viruses, Human Immunodeficiency Virus Proteins, Human immunodeficiency virus type 1, Plasma protein binding, Biology, Molecular Dynamics Simulation, medicine.disease_cause, GPI-Linked Proteins, Cell Line, Protein structure, Antigens, CD, Virology, Protein Interaction Mapping, Vpu, medicine, Humans, Viral Regulatory and Accessory Proteins, chemistry.chemical_classification, Mutation, Research, virus diseases, BST-2, biochemical phenomena, metabolism, and nutrition, Molecular biology, Transmembrane protein, Cell biology, Amino acid, Transmembrane domain, Infectious Diseases, chemistry, Cell culture, Tetherin, Bioluminescence resonance energy transfer assay, Protein Binding
Abstract

Background BST-2 (bone marrow stromal cell antigen 2) is an interferon-inducible protein that inhibits virus release by tethering viral particles to the cell surface. This antiviral activity of BST-2 is antagonized by HIV-1 accessory protein Vpu. Vpu physically interacts with BST-2 through their mutual transmembrane (TM) domains. In this study, we utilized the BRET assay and molecular dynamics (MD) simulation method to further characterize the interaction of BST-2 and Vpu. Results Amino acids I34, L37, P40 and L41 in the TM domain of BST-2, and L11, A18 and W22 in the TM domain of Vpu were identified to be critical for the interaction between BST-2 and Vpu. The residues P40 in the TM domain of BST-2 and L11 in the TM domain of Vpu were shown, for the first time, to be important for their interaction. Furthermore, triple-amino-acid substitutions, 14–16 (AII to VAA) and 26–28 (IIE to AAA) in Vpu TM, not the single-residue mutation, profoundly disrupted BST-2/Vpu interaction. The results of MD simulation revealed significant conformational changes of the BST-2/Vpu complex as a result of mutating P40 of BST-2 and L11, 14–16 (AII to VAA) and 26–28 (IIE to AAA) of Vpu. In addition, disrupting the interaction between BST-2 and Vpu rendered BST-2 resistant to Vpu antagonization. Conclusions Through use of the BRET assay, we identified novel key residues P40 in the TM domain of BST-2 and L11 in the TM domain of Vpu that are important for their interaction. These results add new insights into the molecular mechanism behind BST-2 antagonization by HIV-1 Vpu.

Published
2013

3. Identification of novel key amino acids at the interface of the transmembrane domains of human BST-2 and HIV-1 Vpu.

Author

Xiaojing Pang, Siqi Hu, Jian Li, Fengwen Xu, Shan Mei, Jinming Zhou, Shan Cen, Qi Jin, and Fei Guo

Subjects
MESENCHYMAL stem cells, AMINO acids, CELLULAR signal transduction, HIV, FLUORESCENCE resonance energy transfer, MOLECULAR dynamics
Abstract

Background: BST-2 (bone marrow stromal cell antigen 2) is an interferon-inducible protein that inhibits virus release by tethering viral particles to the cell surface. This antiviral activity of BST-2 is antagonized by HIV-1 accessory protein Vpu. Vpu physically interacts with BST-2 through their mutual transmembrane (TM) domains. In this study, we utilized the BRET assay and molecular dynamics (MD) simulation method to further characterize the interaction of BST-2 and Vpu. Results: Amino acids I34, L37, P40 and L41 in the TM domain of BST-2, and L11, A18 and W22 in the TM domain of Vpu were identified to be critical for the interaction between BST-2 and Vpu. The residues P40 in the TM domain of BST-2 and L11 in the TM domain of Vpu were shown, for the first time, to be important for their interaction. Furthermore, triple-amino-acid substitutions, 14–16 (AII to VAA) and 26–28 (IIE to AAA) in Vpu TM, not the single-residue mutation, profoundly disrupted BST-2/Vpu interaction. The results of MD simulation revealed significant conformational changes of the BST-2/Vpu complex as a result of mutating P40 of BST-2 and L11, 14–16 (AII to VAA) and 26–28 (IIE to AAA) of Vpu. In addition, disrupting the interaction between BST-2 and Vpu rendered BST-2 resistant to Vpu antagonization. Conclusions: Through use of the BRET assay, we identified novel key residues P40 in the TM domain of BST-2 and L11 in the TM domain of Vpu that are important for their interaction. These results add new insights into the molecular mechanism behind BST-2 antagonization by HIV-1 Vpu. [ABSTRACT FROM AUTHOR]

Published
2013
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4. The interferon-induced MxB protein inhibits an early step of HIV-1 infection.

Author

Zhenlong Liu, Qinghua Pan, Shilei Ding, Jin Qian, Fengwen Xu, Jinming Zhou, Shan Cen, Fei Guo, and Liang, Chen

Subjects
HIV infections, INTERFERONS
Abstract

An abstract of the article "The interferon-induced MxB protein inhibits an early step of HIV-1 infection" by Zhenlong Liu, Qinhua Pan, Shilei Ding, Jin Qian, Fengwen Xu, Jinming Zhou, Shan Cen, Fei Guo and Chen Liang is presented.

Published
2013
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