Purified gp120 compositions retaining natural conformation

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Glycoprotein – e.g. – mucins – proteoglycans – etc.

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

530350, 4241841, 4241881, 4242041, C07K 100, C07K 1400, A61K 3900, A61K 3921

Patent

active

056146124

ABSTRACT:
A method for purifying recombinant HIV gp120 so as to provide a glycopeptide having protein/protein binding properties substantially identical to natural viral HIV gp120, which comprises fractionating a composition containing crude gp120 sequentially using (1) ion exchange chromatography, (2) hydrophobic-interaction chromatography, and (3) size exclusion filtration, collecting at each step a fraction that exhibits specific binding affinity for CD4 peptide. The process is carried out in the absence of any affinity purification steps or any steps (such as reverse-phase HPLC) that use contact protein with organic solvents. The product obtained by this method is a purified, full-length, non-fusion recombinant HIV gp120 glycoprotein having protein/protein-interaction properties substantially identical to gp120 as presented on an HIV virus, including binding affinity for CD4 and binding affinity for at least one antibody capable of neutralizing HIV infectivity.

REFERENCES:
Greene, "AIDS and the Immune System", Scientific American, Sep. 1993, pp. 99-105.
Brown, "AIDS Vaccine Trials Viewed With Caution", The Wash. Post Newspaper Jun. 10, 1993.
Robey, et al., 1986, "Prospect for prevention of human immunodeficiency . . . ", PNAS 83:7023-7027.
Haynes, 1993, "Scientific and Social Issues of . . . " Science 260:1279-1286.
Cohen, 1993, "Jitters Jeopardize AIDS vaccine . . . " Science 262:980-981.
U.S. Ser. Abstract No. 7,223,270, Berger, et al, No Date.
D.P. Bulognesi, Progress in Vaccine Against Aids, Science, 246:1233-34 (1989).
Phillip W. Berman, et al., Human immunodeficiency virus type 1 challenge of chimpanzees immunized with recombinant envelope glycoprotein gp120, Proc. Natl. Aca. Sci. USA 95:5200-5204, Jul. 1988.
Berman, et al., Expression and immunogenicity of the extracellular domain of the human immunodeficiency virus type 1 envelope glycoprotein, gp160, J. Virol. Aug. 1989, pp. 3489-3498.
Peter L. Nara, et al., Purified envelope glycoproteins from human immunodeficiency virus type 1 variants induce individual, type-specific neutralizing antibodies, J. Virol., Aug. 1988, pp. 2622-2628.
Larry O. Arthur, et al., Serological responses in chimpanzees inoculated with human immunodeficiency virus glycoprotein (gp120) subunit vaccine, Proc. Natl. Acad. Sci. USA, 84:8583-8587, Dec. 1987.
David J. Evans, et al., An engineered poliovirus chimaera elicits broadly reactive HIV-1 neutralizing antibodies, Nature, 339:385-388, 1 Jun. 1989.
Noel Barrett, et al., Large-scale production and purification of a vaccinia recombinant-derived HIV-1 gp160 and analysis of its immunogenicity, Aids research and human retroviruses, vol. 5, No. 2, 1989.
Patricia L. Earl, et al., Isolate- and group-specific immune responses to the envelope protein of human immunodeficiency virus induced by a live recombinant vaccinia virus in macaques, Aids Research and Human Retroviruses, vol. 5, No. 1, 1989.
Scott D. Putney, et al., HTLV-III/LAV-neutralizing antibodies to an E. coli- produced fragment of the virus envelope, Science, 234:1392-95, 1986.
Kathelyn S. Steimer, et al., Genetically engineered human immunodeficiency envelope glycoprotein gp120 produced in yeast is the target of neutralizing antibodies, Vaccines 87, 1987, pp. 236-241.
Kathelyn S. Steimer, et al., Recombinant env and gag polypeptides in characterizing HIV-1-neutralizing antibodies, Vaccines 88, 1988, pp. 347-354.
David D. Ho, et al., Human immunodeficiency virus neutralizing antibodies recognize several conserved domains on the envelope glycoproteins, J. Virol., Jun. 1987, pp. 2024-2028.
Thomas J. Palker, et al., Type-specific neutralization of the human immunodeficiency virus with antibodies to env-encoded synthetic peptides, Proc. Natl. Acad. Sci. USA, 85:1932-1936, Mar. 1988.
Christopher Fennie, et al., Model for intracellular folding of the human immunodeficiency virus type 1 gp120, J. Virol., Feb. 1989, pp. 639-646.
Stephen W. Pyle, et al., Immune response to immunostimulatory complexes (ISCOMs) prepared from human immunodeficiency virus type 1 (HIV-1) or the HIV-1 external envelope glycoprotein (gp120), Vaccine (1989) 7:465-473.
Laurence A. Lasky, et al., Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor, Cell, (1987) 50:975-985.
Douglas H. Smith, et al., Blocking of HIV-1 infectivity by a soluble, secreted form of the CD4 antigen, Science 238:1704-1707.
Paul Jay Maddon, et al., The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: a new member of the immunoglobulin gene family, Cell 42:93-104, Aug. 1985.
Dan R. Littman, et al., Nature, 325:453-455, 29 Jan. 1987.
Carl Scandella, et al., Purification of HIV-1 gp120 retaining receptor binding activity, Abstract Draft, First Conference on Advances in Purification of Recombinant Proteins, Interlaken, Switzerland, Mar. 14-17, 1989.
Susanne Modrow, et al., J. Virol., Feb. 1987, pp. 570-578.
A. Strinivasan, et al., Gene. 52(1987):71-82.
Robert Edelman, Reviews of Infectious Diseases, vol. 2, No. 3, May-Jun. 1980.
Jorg Kreuter, et al., Infection and Immunity, Feb. 1978, pp. 667-675.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Purified gp120 compositions retaining natural conformation does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Purified gp120 compositions retaining natural conformation, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Purified gp120 compositions retaining natural conformation will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2204448

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.