Polypeptide inducing antibodies neutralizing HIV

Details Polypeptide inducing antibodies neutralizing HIV Polypeptide inducing antibodies neutralizing HIV

2005-03-01

2005-03-01

Stucker, Jeffrey (Department: 1648)

Chemistry: molecular biology and microbiology

Vector, per se

C435S005000, C435S325000, C536S023720, C530S324000, C530S350000, C530S826000, C424S188100, C424S193100, C424S208100, C424S200100

Reexamination Certificate

active

06861253

ABSTRACT:
The present invention thus provides a polypeptide capable of forming a structure corresponding to or mimicking the intermediate of gp41 as well as its use in a vaccine for treating or preventing HIV infections.

REFERENCES:
patent: WO 00 08167 (2000-02-01), None
patent: WO 00 40616 (2000-07-01), None
patent: WO 01 44286 (2001-06-01), None
patent: WO 01 70262 (2001-09-01), None
Shu, et al., “Helical Interactions in the HIV-1 gp41 Core Reveal Structural Basis for the Inhibitory Activity of gp41 Peptides,” Biochemistry 2000, 39, 1634-1642.
Louis, et al., “Design and Properties of NCCG-gp41, a Chimeric gp41 Molecule with Nanomolar HIV Fusion Inhibitory Activity,” vol. 276, No. 31, Issue of Aug. 3, pp. 29485-29489, 2001.
Wingfield, et al., “The extracellular Domain of Immunodeficiency Virus gp41 Protein: Expression inEscherichia coli, Purification, and Crystallization,” Protein Science (1997), 6:1653-1660, Cambridge University Press.
DeRosny, et al., “Peptides Corresponding to the Heptad Repeat Motifs in the Transmembrane Protein (gp41) of Human Immunodeficiency Virus Type 1 Elicit Antibodies of Receptor-Activated Conformations of the Envelope Glycoprotein,” Journal of Virology, Sep. 2001, pp. 8859-8863.
Yang, et al., “The Crystal Structure of the SIV gp41 Ectodomain at 1.47 A Resolution,” Journal of Structural Biology, 126, 131-144 (1999).
Caffrey, et al., “Three-Dimensional Solution Structure of the 44 kDa Ectodomain of SIV gp41,” The EMBO Journal vol. 17, No. 16, pp. 4572-4584, 1998.
Weng, Yongkai and Weiss, Carol D., “Mutational Analysis of Residues in the Coiled-Coil Domain of Human Immunofeficiency Virus Type 1 Transmembrane Protein gp41,” Journal of Virology, Dec. 1998, pp. 9676-9682.
Cao, et al., “Effects of Amino Acid Changes in the Extracellular Domain of the Human Immunodeficiency Virus Type 1 gp41 Envelope Glycoprotein,” Journal of Virology, May 1993, pp. 2747-2755.
Weng, et al., “Structure-Function Studies of the Self-Assembly Domain of the Human Immunodficiency Virus Type 1 Transmembrane Protein gp41,” Journal of Virology, Jun. 2000, pp. 5368-5372.
LaCasse, et al., “Fusion-Competent Vaccines: Broad Neutralization of Primary Isolates of HIV,” Research Articles, Jan. 15, 1999 vol. 383.
Weissenhorn, et al., “Atomic Structure of the Ectodomain from HIV-1 gp41,” Nature, vol. 387, May 1997.
Malashkevich, et al., “Crystal Structure of the Simian Immunodeficiency Virus (SIV) gp41 core: Conserved Helical Interactions Underlie the Broad Inhibitory Activity of gp41 Peptides,” Proc. Natl. Acad. Sci. USA vol. 95, pp. 9134-9139, Aug. 1998 Biochemistry.
Montefiori, David C. and Evans, Thomas G., “Toward an HIV Type 1 Vaccine that Generates Potent, Broadly Cross-Reactive Neutralizing Antibodies,” Aids Research and Human Retroviruses, vol. 15, No. 8, 1999, pp. 689-698.

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