Human immunodeficiency virus inhibiting protein (HIVIP) has been isolated from
a poisonous snake, the Australian Taipan, Oxyuranus Scutellatus. HIVIP is characterized
as a potent inhibitor of HIV-1 and HIV-2 viruses in cell culture. HIVIP is characterized
as a stable, non toxic component of venom, having molecular weight 13,500 Daltons
revealed by gel electrophoresis. The partial sequence of HIVIP for its first fifteen
N-terminal amino acids is given by SEQ. ID. No: 1:
Asn Leu Ala Gln Phe Gly Phe Met Ile Arg Cys Ala Asn Gly Gly.
The active domain of HIVIP was isolated and determined to be SEQ. ID. NO.: 2:
Ala Lys Ala Gly Ser Asp Asn Thr Lys Gly Gly Val Try Pro Met Phe Gly Met.
Various peptides containing at least a portion of this sequence from the
N-terminal have been shown to inhibit other RNA viruses in cell culture and are
collectively termed RIPs, RNA virus Inhibitor Peptides. Such peptides can be made
in abundance and cheaply to provide a synthetic therapeutic for the infections
caused by RNA viruses.
