CD4-independent HIV envelope proteins as vaccines and therapeutics - Inhibitors of serine protease activity, methods and compositions for treatment of viral infections - Treating the syndrome of lipodystrophy - Antigen constructs useful in the detection and differentiation of antibodies to HIV - .alpha.- and .beta.-amino acid hydroxyethylamino sulfonamides useful as retroviral protease inhibitors - Regulatory/unfolding peptides of ezrin

CD4-independent HIV envelope proteins as vaccines and therapeutics

The invention relates to novel CD4-independent HIV Envelope proteins and uses therefor.

Hoxie, James A.; LaBranche, Celia C.; Doms, Robert W.; Hoffman, Trevor L.
The Trustees of the University of Pennsylvania; February 01, 02005
#6849261

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Inhibitors of serine protease activity, methods and compositions for treatment of viral infections

A novel method of treating and preventing viral infection is provided. In particular a method of blocking viral infection facilitated by a serine proteolytic (SP) activity is disclosed, which consists of administering to a subject suffering or about to suffer from viral infection a therapeutically effective amount of a compound having a serine protease inhibitory or serpin activity. Among compounds are .alpha..sub.1 -antitrypsin (AAT), peptide derivatives from the carboxyterminal end of AAT, and man-made, synthetic compounds mimicking the action of such compounds. The preferred viral infections include retroviral infection such as human immunodeficiency virus (HIV) infection.

Shapiro, Leland
The Trustees of University Technology Corporation; February 01, 02005
#6849605

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Method of treating the syndrome of lipodystrophy

Methods of treating a human suffering from the Syndrome of Lipodystrophy or one or more HIV-related abnormalities included therein are provided. One method may include administering, by a pharmaceutically effective mode, a drug composition comprising an opioidergic agent, or alternatively, an opioidergic agent and an insulin secretagogue. The method may also include administering, by a pharmaceutically effective mode, a drug composition comprising an opiate agonist and opiate antagonist, or alternatively, an opiate agonist, opiate antagonist and an insulin secretagogue.

Clemens, Anton H.
CPD, LLC; January 25, 02005
#6846831

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Antigen constructs useful in the detection and differentiation of antibodies to HIV

Isolated HIV-1 Group O env polypeptides obtained from the HIV-1 isolate HAM112 are claimed, as well as (a) antigen constructs comprising fusions of one or more of each of HIV-1 Group O env polypeptides and HIV-1 Group M env polypeptide and (b) further antigen constructs containing additional Group O sequences and especially the gp41 IDR of isolate HAM112. Also claimed are polynucleotide sequences encoding the above, expression vectors comprising the same, host cells transformed thereby, and immunoassay methods and kits utilizing the antigen constructs of the invention.

Hackett, Jr., John R.; Yamaguchi, Julie; Golden, Alan M.; Brennan, Catherine A.; Hickman, Robert K.; Devare, Sushil G.
Abbott Laboratories; January 25, 02005
#6846905

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.alpha.- and .beta.-amino acid hydroxyethylamino sulfonamides useful as retroviral protease inhibitors

.alpha.- and .beta.-amino acid hydroxyethylamino sulfonamide compounds are effective as retroviral protease inhibitors, and in particular as inhibitors of HIV protease.

Vazquez, Michael L; Mueller, Richard A.; Talley, John J.; Getman, Daniel P; DeCrescenzo, Gary A.; Freskos, John N.; Heintz, Robert M.; Bertenshaw, Deborah E.
G. D. Searle & Co.; January 25, 02005
#6846954

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Regulatory/unfolding peptides of ezrin

This invention describes novel charged molecules which specifically bind to the Hepreceptor, a regulatory site which I have discovered in human ezrin. My invention is that when peptides or other charged molecules bind to the Hepreceptor, medically useful immune responses are induced. These charged molecules can be administered orally and by other routes for the treatment of various infectious diseases and cancer. I have determined that the Hepreceptor (human ezrin 308-373) comprises of two adjacent alpha helical domains which are folded together at a hinge region (M339-M340) and stabilised by complimentary side chain charges of the primary amino acid sequence in the soluble cytoplasmic conformation of ezrin. I have determined that in the unfolded membrane associated conformation of ezrin, the Hepreceptor is pushed through the cell membrane and is exposed on the outer surface of the cell. Hepreceptor-Domain A (amino acid numbers 308-339 of human ezrin), comprises of the following 32 amino acid sequence. SEQ ID 1 AREEKHQKQLERQQLETEKKRRETVEREKEQM Hepreceptor-Domain B (amino acid numbers 340-373 of human ezrin), comprises of the following 34 amino acid sequence (Tyrosine 353 [Y] may be phosphorylated to phosphotyrosine [Yp] in the membrane associated conformation of ezrin): SEQ ID 2 MREKEELMLRLQDY(p)EEKTKKAERELIEQIQRALQ.

Holms, Rupert Donald
February 01, 02005
#6849596

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