Tanox Biosystems, Inc.

Tanox, Inc.

Tanux Biosystems, Inc.

Bill N Sun

Cecily R Sun

Michael S Fung

Liming Yu

Young Woo Kim

Tse W Chang

Nancy T Chang

Tse-wen Chang

Monoclonal antibodies are revealed which bind to the gp 120 protein on the envelope of HIV-1. These antibodies neutralize HIV-1. They inhibit the rate of infection of T cells, and also inhibit syncytium formation. Further, the antibodies are group-specific and neutralize different strains and isolates of HIV-1. These antibodies have a variety of uses, including the treatment and prevention of AIDS and ARC.

Chimeric monoclonal antibodies which neutralize HIV-1 infection and

Murine monoclonal antibodies and related products such as antibody fragments, immunotoxins, human and humanized antibodies are disclosed, all of which bind to the gp120 protein on the envelope of HIV-1. These antibodies and related products neutralize HIV-1. They inhibit the infection of T cells, and also inhibit syncytium formation. Further, the antibodies are preferably group-specific and neutralize various strains and isolates of HIV-1. These antibodies have a variety of uses, including the treatment of AIDS and ARC, the prevention of HIV-1 infection, as well as a diagnostic application, in that they can be used for assaying of unknown fluid samples for HIV-1.

Monoclonal antibodies which neutralize HIV-1 infection

Disclosed are immunogens and peptides based on the binding site of gC1q-R for HIV-1 gp120, and immunogens and peptides based on the binding site of HIV-1 gp120 for gC1q-R. The sequence of the gC1q-R binding site for gp120 is shown in SEQ ID NO.: 2. The sequence of the HIV-1 gp120 binding site for gC1q-R is shown in SEQ ID NO.: 3. Also disclosed are antibodies and binding molecules to all such immunogens and peptides, and inducing the endogenous production of such antibodies.

gC1q receptor, HIV-1 gp120 region binding thereto, and related peptides

Disclosed are immunogens and peptides based on the binding site of gClq-R for HIV-1 gp120, and immunogens and peptides based on the binding site of HIV-1 gp120 for gClq-R. The sequence of the gClq-R binding site for gp120 is shown in SEQ ID NO.: 2. The sequence of the HIV-1 gp120 binding site for gClq-R is shown in SEQ ID NO.: 3. Also disclosed are antibodies and binding molecules to all such immunogens and peptides, and inducing the endogenous production of such antibodies.

Disclosed are immunogens and peptides based on the binding site of gC1q-R for HIV-1 gp120, and immunogens and peptides based on the binding site of HIV-1 gp120 for gC1q-R. The sequence of the gC1q-R binding site for gp120 is shown in SEQ D NO.: 2. The sequence of the HIV-1 gp120 binding site for gC1q-R is shown in SEQ ID NO.: 3. Also disclosed are antibodies and binding molecules to all such immunogens and peptides, and inducing the endogenous production of such antibodies.

GC1q receptor, HIV-1 gp120 region binding thereto, and related peptides

Disclosed are immunogens and peptides based on the binding site of gC1q-R for HIV-1 gp120 and immunogens and peptides based on the binding site of HIV-1 gp120 for gC1q-R. The sequence of the gC1q-R binding site for gp120 is shown in SEQ ID NO.: 2. The sequence of the HIV-1 gp120 binding site for gC1q-R is shown in SEQ ID NO.: 3. Also disclosed are antibodies and binding molecules to all such immunogens and peptides, and inducing the endogenous production of such antibodies.

Disclosed are monoclonal antibodies and related products which bind to the second variable region of HIV-1 gp120 and synthetic peptides and anti-idiotypic antibodies which induce endogenous production of antibodies with these same properties.

Antibodies which target a neutralization site within the second variable

The monoclonal antibodies (mAbs) of the invention bind to a neutralizing epitope on the gp120 glycoprotein of HIV-1. The binding seems to be conformation-dependent, in the sense that altering the conformation of gp120 (by deglycosylating the gp120, by reducing the cysteine bonds in the peptide backbone) will inhibit the binding. The mAbs of the invention are group specific and can neutralize different strains and different isolates of HIV-1. The binding of these mAbs to gp120 is enhanced by the binding of other antibodies to the principal neutralizing determinant (amino acid residue numbers 296-331) of gp120.

Growing community of inventors

Bellaire, TX, United States of America

Bill N Sun