Rutgers, The State University of New Jersey

The Public Health Research Institute of the City of New York, Inc.

The State University of New York

New York University

University of Massachusetts

Research, Incorporated

University of Medicine and Dentistry of New Jersey

Molsoft LLC

Abraham Pinter

Alok K Choudhary

Samuel Kayman

Fred Russell Kramer

Maxim Totrov

Susan Zolla-Pazner

Timothy J Cardozo

Shan Lu

Ruben Abagyan

Karl A Drlica

Miroslaw K Gorny

Xiang-peng Kong

David Dubnau

Shermaine A Tilley

Deendayal Patel

The present invention broadly provides different compositions, kits, vectors, and methods including monoclonal antibodies directed to epitopes found within lipoarabinomannan (LAM) and phosphatidyl-myo-inositol mannoside 6 (PIM6) for the diagnosis and treatment ofinfections.

Anti-LAM and anti-PIM6/LAM monoclonal antibodies for diagnosis and treatment ofinfections

The present invention relates to a novel composition of HIV-1 Env proteins that contain structurally and immunologically distinct VI/V2 domains. Methods of isolating such proteins, and methods of using such proteins as immunogens, therapeutic agents, vaccines, and test compounds for use in identifying a HIV antiviral are also provided.

HIV-1 antigens with discrete conformational forms in the V1/V2 domain and methods of use thereof

This invention features polypeptides, variants thereof, and fragments thereof useful in eliciting an immune response (e.g., neutralizing antibodies) against a broad spectrum of HIV-1 isolates. The polypeptides, variants, and fragments include a portion of the gp120 V2 domain of HIV-1. The polypeptides, variants, and fragments display an epitope that is recognized by at least one antibody which neutralizes at least one HIV-1 primary isolate. This invention also features nucleic acid sequences encoding those polypeptides. In addition, the invention provides methods of screening for inhibitors of HIV-1 entry into cells, as well as methods of treatment using the inhibitors.

Neutralizing antibodies that bind to the HIV-1 Env V2 critical neutralization domain

Insertion of HIV-1 V3 loop peptides from the viral glycoprotein gp120 into selected, immunogenic scaffold proteins results in a recombinant polypeptide that is a potent V3 immunogen. V3 immunogens include natural and consensus V3 sequences and cyclic and reverse peptides. Preferred scaffold proteins are Cholera Toxin subunit B and homologues thereof including closely relatedenterotoxins. Such immunogenic polypeptides induce broadly reactive anti-gp120 antibodies specific for V3 epitopes that can neutralize heterologous HIV-1 subtypes and strains. These polypeptide, methods for preparing them, and methods for inducing anti-gp120 (V3-specific) antibody) responses using them are disclosed.

Immunogen comprising the HIV GP120 V3 loop in a conformation that induces broadly neutralizing antibodies

The invention relates to isolated monoclonal antibodies which specifically bind to the C-terminal heptad repeat region of gp41 (HR2) and neutralize an HIV-1 primary isolate.

HIV-1 GP41 neutralization domain and use thereof

The invention features a protein which includes a gp120 V1/V2 domain of an HIV-1 strain and not a gp120 V3 domain of an HIV-1 strain, which protein does not substantially bind CD4. The gp120 V1/V2 domain of the protein displays an epitope which is recognized by an antibody which neutralizes at least one HIV-1 primary isolate with a ND of less than 100 &mgr;g/ml.

HIV-1 gp120 V1/V2 domain epitopes capable of generating neutralizing antibodies

Novel expression vectors are provided for expressing a fusion glycoprotein. The fusion glycoprotein contains the N-terminal globular domain of a retroviral env surface protein linked to a selected glycopeptide. Truncation glycoproteins as well as insertion glycoproteins are expressed using the vectors.

Fusion glycoproteins

A synergistic combination of antibodies specific for HIV envelope glycoprotein gp120 is described. One of the antibodies specific for the V3 loop and the other is specific for the CD-4 binding site of gp120.

Synergistic neutralization of HIV-1 by human monoclonal antibodies and

Mutant ribozymes are screened by culturing cells whose survival is dependant upon cleavage of RNA by a ribozyme, which cleavage causes the cells to survive in the presence of an agent which otherwise would kill the cells, and selecting cells which survive.

Selection of ribozymes that efficiently cleave target RNA

Non-denatured [gp90] is isolated from oncornavirus envelopes including feline and murine leukemia virus envelopes and utilized as vaccines. The materials as isolated may be used directly on in various compositions.

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Brooklyn, NY, United States of America

Abraham Pinter