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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
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
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
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
.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
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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