Abstract
Bone marrow stromal cell antigen 2 (BST-2) inhibits the release of HIV-1 and other enveloped viruses from the cell surface. HIV-1 Vpu binds to BST-2 through an interaction between transmembrane domains (TMD) of the two proteins and induces the downregulation of cell surface BST-2, thereby counteracting its antiviral activity. In this study, we designed and prepared a modified peptide BST2-TM-P1, which include the sequence of BST-2 TMD, keeping its property competing with BST-2 to bind with Vpu. Biological assay results indicate BST2-TM-P1 could increase the BST-2 level at the cell surface in Vpu dependent manner and significantly inhibit the replication of HIV-1 virion. Our studies indicate that blocking the interaction of Vpu and BST-2 is an effective way to combat HIV-1 infection.
Keywords:
Vpu; anti-HIV-1; bone marrow stromal cell antigen 2; drug design.
© 2014 Wiley Periodicals, Inc.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antigens, CD / metabolism*
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Biological Assay
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Cell Membrane / metabolism
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Enzyme-Linked Immunosorbent Assay
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Flow Cytometry
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HIV-1 / drug effects
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HIV-1 / physiology
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HeLa Cells
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Human Immunodeficiency Virus Proteins / metabolism*
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Humans
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Membrane Glycoproteins / metabolism
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Models, Molecular
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Molecular Sequence Data
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Peptides / chemical synthesis
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Peptides / chemistry
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Peptides / pharmacology*
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Protein Binding / drug effects
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Protein Structure, Tertiary
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Quartz Crystal Microbalance Techniques
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Solid-Phase Synthesis Techniques
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Vesicular stomatitis Indiana virus / metabolism
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Viral Envelope Proteins / metabolism
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Viral Regulatory and Accessory Proteins / metabolism*
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Virus Replication / drug effects
Substances
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Antigens, CD
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G protein, vesicular stomatitis virus
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Human Immunodeficiency Virus Proteins
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Membrane Glycoproteins
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Peptides
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Viral Envelope Proteins
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Viral Regulatory and Accessory Proteins
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vpu protein, Human immunodeficiency virus 1