Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Patent
1994-07-18
1997-09-09
Scheiner, Toni R.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
4353201, 435 697, 4352523, 536 2353, 536 234, C12N 120, C12N 1513, C07H 2104
Patent
active
056655690
DESCRIPTION:
BRIEF SUMMARY
BACKGROUND
The present invention relates, in general, to materials and methods useful in the prevention and treatment of Human Immunodeficiency Virus (HIV-1) infection. More particularly, the invention relates to monoclonal antibodies useful in passive immunization of HIV-1 susceptible or infected animals, especially humans.
The infective process of HIV-1 in vivo has recently been the subject of a review article by McCune, Cell, 64, pp. 351-363 (1991). Briefly, HIV-1 infects a variety of cell lineages, such as T-cells, monocytes/macrophages and neuronal cells, which express the CD4 receptor. Because the vast majority of CD4.sup.+ cells in the body are "resting" or quiescent and divide only in response to specific signals, infection with HIV-1 results in CD4.sup.+ cells harboring transcriptionally inactive virus. Stimulation of the immune system of infected animals, including active immunization, may result in polyclonal activation and the signaling of resting CD4.sup.+ cells to go into the S phase of the cell cycle. The replicating cells then actively produce viral particles, provoking spread of the infection. Considering this negative effect of stimulating the immune system of an HIV-1-infected animal, it is possible that the most effective method of preventing or treating HIV-1 infection is passive immunization, that is, administering anti-HIV-1 antibodies to a susceptible or infected animal.
Jackson et al., Lancet, 2, pp. 647-652 (1988) reports that a single administration of anti-HIV-I antibodies in the form of plasma to human patients afflicted with advanced acquired immunodeficiency syndrome (AIDS, the syndrome of progressive immune system deterioration associated with HIV-I infection) temporarily resulted in: fewer symptoms, a transient increase in T lymphocytes, a reduction in the frequency of opportunistic infections and a decline in the rate at which HIV-1 could be cultured from plasma or lymphocytes of the patients. See also, Karpas et al., Proc. Nat. Acad. Sci. USA, 85, pp. 9234-9237 (1988). Moreover, Emini et al., Nature, 355, pp. 728-730 (1992) reports that the administration of an antibody specifically reactive with HIV-1 to a chimpanzee before the animal was exposed to HIV-1 resulted in the chimpanzee remaining free of signs of viral infection. These studies indicate that antibodies capable of neutralizing HIV-1 can be useful in the prevention/treatment of HIV-1 infection.
The HIV-1 major external envelope glycoprotein, gp120, binds to the cellular CD4 receptor and facilitates the internalization of the virus. Several epitopes of the glycoprotein have been associated with the development of neutralizing antibodies. Ho et al., Science, 239, pp. 1021-1023 (1988) reports that amino acids 254-274 of gp120 elicit polyclonal antisera capable of group-specific neutralization of three different isolates of HIV-1. Conformation-dependent epitopes, epitopes not consisting of primary sequences of amino acids, on gp120 have also been implicated in eliciting antibodies that neutralize diverse strains of the virus by Haigwood et al., Vaccines 90, pp. 313-320 (1990) and Ho et al., J. Virol., 65(1), pp. 489-493 (1991). The so-called "principal neutralizing determinant" (PND) of HIV-1 gp120 has been localized to the "V.sub.3 loop" of gp120. See Putney et al., Science, 234, pp. 1392-1395 (1986); Rusche et al., Proc. Natl. Acad. Sci. USA, 85, pp. 3198-3202 (1988); Goudsmit et al., Proc. Natl. Acad. Sci. USA, 85, pp. 4478-4482 (1988); Palker et al., Proc. Natl. Acad. Sci. USA, 85, pp. 1932-1936 (1988); and Holley et al., Proc. Natl. Acad. Sci. USA, 85 ,pp. 6800-6804 (1991). The V.sub.3 loop consists of a hypervariable domain which is established by disulfide bonding between cysteine residues flanking the domain. The V.sub.3 loop of HIV-1.sub.MN, for example, is formed by a disulfide bond between the cysteine residues at positions 302 and 336 of gp120.
Recombinant and synthetic protein fragments including the series of amino acid residues of the V.sub.3 loop from various HIV isolates have been reported to elici
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Nissin Shokuhin Kabushiki Kaisha
Scheiner Toni R.
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