[Cloning and expression of the CD4 receptor gene from human T-lymphocytes in Escherichia coli cells].
The gene for the CD4-membrane glycoprotein-receptor for HIV has been cloned. The 179 amino acids fragment of the CD4-receptor responsible for binding of gp120 HIV glycoprotein has been fused with beta-galactosidase and shown to be expressed in Escherichia coli cells. The recombinant protein in ELISA and immunoblotting techniques reacts with the monoclonal antibodies OKT4A and Leu3A known to block the interaction between the CD4 and gp120 HIV glycoprotein. The recombinant protein can be used for different scientific and practical purposes including studying of the mechanisms for HIV interaction with the sensitive cells as well as for viral gp120 protein purification, etc.
Zverev
V V
VV
Shakhov
A N
AN
Nedospasov
S A
SA
Pugach
A V
AV
Sidorov
A V
AV
Maliushova
V V
VV
Andzhaparidze
O G
OG
D001483:Base Sequence; D015153:Blotting, Western; D015704:CD4 Antigens / Q000235:genetics* / Q000276:immunology; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D015870:Gene Expression; D015488:HIV Antigens / Q000235:genetics / Q000276:immunology; D015699:HIV Envelope Protein gp120 / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D010957:Plasmids; D015183:Restriction Mapping; D013601:T-Lymphocytes / Q000276:immunology*
D015704:CD4 Antigens; D015488:HIV Antigens; D015699:HIV Envelope Protein gp120