Article
Secretion of active truncated CD4 into Escherichia coli periplasm.
Applied microbiology and biotechnology - 1 Apr 1991
Rockenbach S K, Dupuis M J, Pitts T W, Marschke C K, Tomich C S
Abstract excerpt
A truncated molecule containing the first 183 amino acid residues of the HIV-1 receptor, CD4, was made by periplasmic secretion in Escherichia coli. The signal sequence from the E. coli proteins OmpA, PhoA, or OmpF was fused to the truncated CD4, under the control of either the trp or the lac promoter. The processed material secreted into the periplasm reacted with monoclonal antibodies and exhibited binding...
Topics
- Amino Acid Sequence
- Antibodies, Monoclonal
- Antigens, CD
- Bacterial Outer Membrane Proteins
- Escherichia coli
- HIV Envelope Protein gp120
- Lactose
- Molecular Sequence Data
- Mutation
- Plasmids
- Promoter Regions, Genetic