Tanox Biosystems, Inc.

Tanox, Inc.

Tse-wen Chang

Nancy T Chang

Bill Nai-Chau Sun

Cecily Rou-Yun Sun

Cecily R Sun

Bill N Sun

Michael S Fung

Young Woo Kim

Jean deVilliers

Sek C Fung

Wayne Gordon

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

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 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. The antibodies are used in immunotoxins which are specifically toxic to HIV-1 infected T cells.

Immunoconjugates which neutralize HIV-1 infection

Antibodies that bind soluble IgE but not IgE on the surface of B lymphocytes or basophils are described. The antibodies do not induce histamine release by basophils or mast cells.

Monoclonal antibodies that bind to soluble IGE but do not bind IGE on

Chimeric antibodies which bind to unique antigenic epitopes of IgE (designated ige.b1) which are present on IgE-bearing B lymphocytes but not basophils are described.

Chimeric anti-human IgE-monoclonal antibody which binds to secreted IgE

Methods of producing monoclonal antibodies that bind to unique antigenic epitopes of IgE (designated ige.bl) which are present on IgE-bearing B cells but not basophils are described. The monoclonal antibodies block binding of IgE to mast cells and basophils in vitro.

Methods for producing high affinity anti-human IgE-monoclonal antibodies

Anti-idiotypic monoclonal antibodies that recognize the paratope of monoclonal antibodies specific for unique antigenic epitopes of IgE (designated ige.bl) which are present on membrane-bound IgE-expressed by bearing B cells but not on IgE bound to Fc.epsilon.R on basophils are described.

Anti-idiotype antibodies specific for the parotope of antibodies which

Antigenic epitopes associated with the extracellular segment of the domain which anchors immunoglobulins to the B cell membrane are disclosed. For IgE, the epitopes are present on IgE-bearing B cells but not basophils or the secreted, soluble form of IgE. The epitope can be exploited for therapy and diagnosis. For example, antibodies or immunotoxins specific for the epitopes associated with the anchor domain of IgE can be used to selectively destroy IgE-bearing lymphocytes, thus blocking IgE-mediated allergic reactions.

Antigenic epitopes present on membrane-bound but not secreted IgE

Molecular conjugates which facilitate the attachment of macromolecular drugs onto cellular surfaces and their entry into cells are described. The molecular conjugates comprise a macromolecular drug linked to an 'inactivated' membrane blending agent which inserts into the cellular plasma membrane. The membrane blending agent is inactivated by cleavable linkage to a blocking agent which, until released from the conjugate under appropriate conditions, blocks and ability of the membrane blending agent to insert into the cellular membrane. Upon release of the blocking agent, the membrane blending agent is 'activated' and the conjugate can be inserted into a cellular plasma membrane. The membrane blending agents can be peptides such as fusogenic or ion channel forming peptides or long chain fatty acids. The blocking agents can be bulky or charged moieties which mask and prevent insertion of the membrane blending agent.

Molecular conjugates containing cell membrane-blending agents

Antigenic epitopes associated with the extracellular segment of the domain which anchors immunoglobulins to the B cell membrane are disclosed. For IgE, the epitopes are present on IgE-bearing B cells but not basophils or the secreted, soluble form of IgE. The epitope can be exploited for diagnosis.

Antigenic epitopes of IgE present on B cell but not basophil surface

Antigenic epitopes associated with the extracellular segment of the domain which anchors immunoglobulins to the B cell membrane are disclosed. For IgA, the epitopes are present on IgA-bearing B cells but not the secreted, soluble form of IgA. The epitopes can be exploited for therapy and prophylaxis. For example, antibodies specific for the epitopes associated with the anchor and peptide encompassing the epitope domain of IgA can be used to increase secretory IgA production for the purposes of treating patients with infectious diseases and IgE-mediated allergic diseases.

Antigenic epitopes present on membrane-bound but not secreted IgA

Antigenic epitopes associated with the extracellular segment of the domain which anchors immunoglobulins to the B cell membrane are disclosed. For IgA, the epitopes are present on IgA-bearing B cells but not the secreted, soluble form of IgA. The epitope can be exploited for therapy and prophylacsis. For example, antibodies specific for the epitopes associated with the anchor and peptide encompassing the epitope domain of IgA can be used to increase secretory IgA production for the purposes of treating patients susceptible with infectious diseases and IgE-mediated allergic diseases.

Growing community of inventors

Houston, TX, United States of America

Tse-wen Chang