1. [Neutralising properties for HIV virus of hybrid protein MalE-CD4 expressed in E. coli and purified in 1 step].
- Author
-
Clément JM, Szmelcman S, Jehanno M, Martineau P, Schwartz O, and Hofnung M
- Subjects
- Amino Acid Sequence, Antibodies, Monoclonal, Chromatography, Affinity, Cloning, Molecular, Escherichia coli genetics, HIV Envelope Protein gp120, Immunoassay, Immunosorbent Techniques, Maltose metabolism, Maltose-Binding Proteins, Molecular Sequence Data, Polysaccharides metabolism, Receptors, HIV, Receptors, Virus genetics, Recombinant Fusion Proteins isolation & purification, Recombinant Fusion Proteins metabolism, Retroviridae Proteins metabolism, ATP-Binding Cassette Transporters, Antigens, Differentiation, T-Lymphocyte genetics, Carrier Proteins genetics, Carrier Proteins metabolism, Carrier Proteins pharmacology, Escherichia coli metabolism, Escherichia coli Proteins, HIV drug effects, Monosaccharide Transport Proteins, Periplasmic Binding Proteins, Recombinant Fusion Proteins pharmacology, Recombinant Proteins pharmacology
- Abstract
Genetic fusions allowing the expression in E. coli of hybrid proteins between a bacterial periplasmic maltose binding protein (MalE) and the CD4 molecule (the receptor of the HIV virus) have been constructed. One of them has kept most of the properties of each constituent: it is exported, can be purified in one step on an affinity column, interacts with anti-MalE and anti-CD4 antibodies, binds HIV gp 120 protein and inactivates HIV virus in an in vitro test.
- Published
- 1989