Abstract: Fc fusion proteins of human EPO with increased biological activities relative to rHuEPO on a molar basis are disclosed. The HuEPO-L-vFc fusion protein comprises HuEPO, a flexible peptide linker of about 20 or fewer amino acids, and a human IgG Fc variant. The Fc variant is of a non-lytic nature and shows minimal undesirable Fc-mediated side effects. A method is also disclosed to make or produce such fusion proteins at high expression levels. Such HuEPO-L-vFc fusion proteins exhibit extended serum half-life and increased biological activities, leading to improved pharmacokinetics and pharmacodynamics, thus fewer injections will be needed within a period of time.

Abstract: Fc fusion proteins of human G-CSF with increased biological activities relative to rhG-CSF on a molar basis are disclosed. The hG-CSF-L-vFc fusion protein comprises hG-CSF, a flexible peptide linker of about 20 or fewer amino acids, and a human IgG Fc variant. The Fc variant is of a non-lytic nature and shows minimal undesirable Fc-mediated side effects. A method is also disclosed to make or produce such fusion proteins at high expression levels. Such hG-CSF-L-vFc fusion proteins exhibit extended serum half-life and increased biological activities, leading to improved pharmacokinetics and pharmacodynamics, thus fewer injections will be needed within a period of time.

Abstract: The invention relates to C5 inhibitors, which inhibit type II endothelial cell activation, wherein the inhibition is manifested by the suppression of E-selectin. These inhibitors are useful in treatment of delayed xenograft rejection or acute vascular rejection. The inhibitors include antibody molecules, as well as homologues, analogues and modified or derived forms thereof, including immunoglobulin fragments like Fab, F(ab′)2 and Fv, small molecules, including peptides, oligonucleotides, peptidomimetics and organic compounds. Examples of monoclonal antibodies, which bind to and inhibit C5, were generated and are designated MAb 137-76 and MAb 137-30.

Abstract: The invention relates to factor D inhibitors, which bind to factor D and block the functional activity of factor D in complement activation. The inhibitors include antibody molecules, as well as homologues, analogues and modified or derived forms thereof, including immunoglobulin fragments like Fab, F(ab′)2 and Fv, small molecules, including peptides, oligonucleotides, peptidomimetics and organic compounds. A monoclonal antibody which bound to factor D and blocked its ability to activate complement was generated and designated 166-32. The hybridoma producing this antibody was deposited at the American Type Culture Collection, 10801 University Blvd., Manassas, Va. 20110-2209, under Accession Number HB-12476.

Abstract: The invention relates to C5 inhibitors, which inhibit type II endothelial cell activation, wherein the inhibition is manifested by the suppression of E-selectin. These inhibitors are useful in treatment of delayed xenograft rejection or acute vascular rejection. The inhibitors include antibody molecules, as well as homologues, analogues and modified or derived forms thereof, including immunoglobulin fragments like Fab, F(ab′)2 and Fv, small molecules, including peptides, oligonucleotides, peptidomimetics and organic compounds. Examples of monoclonal antibodies, which bind to and inhibit C5, were generated and are designated MAb 137-76 and MAb 137-30.

Abstract: A particular epitope located within the CD4-binding region of gpl20 of HIV-1, and antibodies specific for the epitope which can inhibit HIV-1 infection of human cells by diverse strains and isolates of the virus, is disclosed. The antibodies are useful for a number of purposes, including diagnosis of HIV-1 infection.

Abstract: The invention relates to C2a inhibitors, which bind to C2a and block the functional activity of C2a in complement activation. The inhibitors include antibody molecules, as well as homologues, analogues and modified or derived forms thereof, including immunoglobulin fragments like Fab, F(ab′)2 and Fv, small molecules, including peptides, oligonucleotides, peptidomimetics and organic compounds. A monoclonal antibody, which bound to C2a and blocked its ability to activate complement was generated and designated 175-62. The hybridoma producing this antibody was deposited at the American Type Culture Collection, 10801 University Blvd., Manassas, Va. 20110-2209, under Accession Number PTA-1553.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.