Expression and characterization of glycophospholipid-anchored human immunodeficiency virus type 1 envelope glycoproteins
Autor: | Eric Hunter, Patrick B. Johnston, Karl Salzwedel, John W. Dubay, S J Roberts |
---|---|
Rok vydání: | 1993 |
Předmět: |
Glycosylphosphatidylinositols
Recombinant Fusion Proteins viruses Molecular Sequence Data Restriction Mapping Immunology Fluorescent Antibody Technique Transfection Gp41 Genes env Giant Cells Microbiology Cell Line Viral envelope Virology Animals Humans Amino Acid Sequence chemistry.chemical_classification Syncytium Membrane Glycoproteins Base Sequence biology Gene Products env virus diseases Molecular biology Herpesvirus glycoprotein B Complementation Kinetics Membrane glycoproteins Oligodeoxyribonucleotides chemistry Insect Science Antigens Surface HIV-1 biology.protein Thy-1 Antigens Glycoprotein HeLa Cells Plasmids Research Article |
Zdroj: | Journal of Virology. 67:5279-5288 |
ISSN: | 1098-5514 0022-538X |
Popis: | Four chimeric human immunodeficiency virus type 1 (HIV-1) env genes were constructed which encoded the extracellular domain of either the wild-type or a cleavage-defective HIV-1 envelope glycoprotein (gp160) fused at one of two different positions in env to a C-terminal glycosyl-phosphatidylinositol (GPI) attachment signal from the mouse Thy-1.1 glycoprotein. All four of the constructs encoded glycoproteins that were efficiently expressed when Rev was supplied in trans, and the two cleavable forms were processed normally to gp120 and a chimeric "gp41." The chimeric glycoproteins, in contrast to the wild-type glycoprotein, could be cleaved from the surface of transfected cells by treatment with phosphatidylinositol-specific phospholipase C, indicating that they were anchored in the plasma membrane by a GPI moiety. These GPI-anchored glycoproteins were transported intracellularly at a rate only slightly lower than that of the full-length HIV-1 glycoprotein and were present on the cell surface in equivalent amounts. Nevertheless, all four glycoproteins were defective in mediating both cell-cell and virus-cell fusion as determined by syncytium formation in COS-1-HeLa-T4 cell mixtures and trans complementation of an env-defective HIV-1 genome. |
Databáze: | OpenAIRE |
Externí odkaz: |