Abstract: The subject invention concerns peptide mimetics of SOCS proteins and methods of use. In one embodiment, a peptide mimetic of the invention binds to a SOCS1 and a SOCS3 target protein. In a specific embodiment, a peptide mimetic of the invention comprises the amino acid sequence of SEQ ID NO:1 and/or SEQ ID NO:2 and/or SEQ ID NO:51, or a functional fragment or variant thereof. In a further embodiment, a peptide of the invention can comprise multiple copies of the mimetic sequence. In one embodiment, a peptide of the invention comprises two or more copies of SEQ ID NO:1 and/or SEQ ID NO:2 and/or SEQ ID NO:51. In a specific embodiment, a peptide mimetic of the invention comprises the amino acid sequence of SEQ ID NO:3 and/or SEQ ID NO:4 to and/or SEQ ID NO:52, or a functional fragment or variant thereof. The subject invention also pertains to methods of treating and/or preventing autoimmune conditions and/or disorders.

Abstract: The subject invention pertains to agonist peptides of type I interferons and methods of using the peptides. These peptides are based on the amino acid sequence of the C-terminus region of the type I IFN molecules and are capable of binding to the cytoplasmic domain of type I IFN receptors. Surprisingly, these peptides were found to possess the same or similar biological activity as that associated with the full-length, mature type I IFN proteins, even though these peptides do not bind to the extracellular domain of the type I IFN receptors. In one embodiment, the peptide is a peptide of IFN?. In another embodiment, the peptide is a peptide of IFN?. Exemplified peptides of the invention include those having SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:38, SEQ ID NO:39, and SEQ ID NO:40. The subject peptides have been shown to effect increased resistance to viral infection.

Abstract: The subject invention concerns peptide mimetics of SOCS proteins and methods of use. In one embodiment, a peptide mimetic of the invention binds to a SOCS1 and a SOCS3 target protein. In a specific embodiment, a peptide mimetic of the invention comprises the amino acid sequence of SEQ ID NO:1 and/or SEQ ID NO:2 and/or SEQ ID NO:51, or a functional fragment or variant thereof. In a further embodiment, a peptide of the invention can comprise multiple copies of the mimetic sequence. In one embodiment, a peptide of the invention comprises two or more copies of SEQ ID NO:1 and/or SEQ ID NO:2 and/or SEQ ID NO:51. In a specific embodiment, a peptide mimetic of the invention comprises the amino acid sequence of SEQ ID NO:3 and/or SEQ ID NO:4 to and/or SEQ ID NO:52, or a functional fragment or variant thereof. The subject invention also pertains to methods of treating and/or preventing autoimmune conditions and/or disorders.

Abstract: The subject invention pertains to agonist peptides of type I interferons and methods of using the peptides. These peptides are based on the amino acid sequence of the C-terminus region of the type I IFN molecules and are capable of binding to the cytoplasmic domain of type I IFN receptors. Surprisingly, these peptides were found to possess the same or similar biological activity as that associated with the full-length, mature type I IFN proteins, even though these peptides do not bind to the extracellular domain of the type I IFN receptors. In one embodiment, the peptide is a peptide of IFN?. In another embodiment, the peptide is a peptide of IFN?. Exemplified peptides of the invention include those having SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:38, SEQ ID NO:39, and SEQ ID NO:40. The subject peptides have been shown to effect increased resistance to viral infection.

Abstract: The subject invention pertains to agonist peptides of type I interferons and methods of using the peptides. These peptides are based on the amino acid sequence of the C-terminus region of the type I IFN molecules and are capable of binding to the cytoplasmic domain of type I IFN receptors. Surprisingly, these peptides were found to possess the same or similar biological activity as that associated with the full-length, mature type I IFN proteins, even though these peptides do not bind to the extracellular domain of the type I IFN receptors. In one embodiment, the peptide is a peptide of IFN?. In another embodiment, the peptide is a peptide of IFN?. Exemplified peptides of the invention include those having SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:38, SEQ ID NO:39, and SEQ ID NO:40. The subject peptides have been shown to effect increased resistance to viral infection.

Abstract: The subject invention concerns peptide molecules that specifically inhibit the enzymatic function of tyrosine kinases, including the JAK and EGF receptor (EGFR) family of kinases, to autophosphorylate, i.e., to transfer a phosphate group from ATP to an amino acid in the kinase. Phosphorylation of proteins is the most fundamental method for signal transduction among proteins in a cell. Inhibition of tyrosine kinase autophosphorylation activities inhibits the enzyme's signaling and shuts down the functioning pathways originating from the enzyme. The JAK2 and EGFR tyrosine kinases are involved in both inflammatory disorders and cancer. In these disorders, the tyrosine kinases can often be activated in an uncontrolled fashion. The subject application also concerns antibodies that bind to a tyrosine kinase autophosphorylation site.

Abstract: The subject invention concerns peptide molecules that specifically inhibit the enzymatic function of tyrosine kinases, including the JAK and EGF receptor (EGFR) family of kinases, to autophosphorylate, i.e., to transfer a phosphate group from ATP to an amino acid in the kinase. Phosphorylation of proteins is the most fundamental method for signal transduction among proteins in a cell. Inhibition of tyrosine kinase autophosphorylation activities inhibits the enzyme's signaling and shuts down the functioning pathways originating from the enzyme. The JAK2 and EGFR tyrosine kinases are involved in both inflammatory disorders and cancer. In these disorders, the tyrosine kinases can often be activated in an uncontrolled fashion. The subject application also concerns antibodies that bind to a tyrosine kinase autophosphorylation site.

Abstract: The subject invention concerns novel methods and materials for treating patients afflicted with allergic conditions, such as allergic rhinitis, atopic dermatitis, bronchial asthma and food allergy. The method of the subject invention comprises administering interferon tau (IFN&tgr;) or a chimeric IFN (ovine IFN&tgr; (1-27)/human IFN&agr;D (28-166)) to a person afflicted with an allergic condition. When administered, INF&tgr; and chimeric IFN suppress the production of IgE antibodies without toxic side effects. The subject invention also concerns chimeric ovine/human IFNs which can be used in the methods of the invention.

Abstract: The subject invention pertains to novel methods for treating autoimmune-related diseases, such as Multiple Sclerosis (MS). One embodiment of the method of the invention comprises administering interleukin-10 (IL-10) and transforming growth factor-beta (TGF-&bgr;), in combination, to a person afflicted with or predisposed to an autoimmune disease. When administered in combination, these cytokines act in a synergistic manner as suppressor factors to inhibit the activation of self-reactive T cells that are involved in autoimmune disease.

Abstract: The invention relates to superantigen mediated expansion of antigen-specific T cells for cancer and infectious agent treatment/prophylaxis. Mice were injected with inactivated B16F10 mouse melanoma cells, followed by injection with a combined SEA/SEB injection or a sham injection on days 3 and 6, followed by day 4 challenge with live melanoma cells. The SEA/SEB recipient mice survived longer post-challenge and had a higher CTLs against tumor cells than did the sham injected mice. SEA/SEB TCR activation has been reported to be independent of antigen specificity of TCRs. This invention provides a method whereby a combination of Staphylococcal enterotoxin superantigens is used to enhance specific immune responses to activating antigens to enhance immune responses against cancers and infectious agents.

Abstract: The invention describes a method of reducing the cytotoxicity of interferon-alpha by making defined amino acid substitutions in the N-terminal portion of the polypeptide sequence. Also described are human interferon-alpha analogs with low cytotoxicity, and therapeutic applications of the low toxicity interferon-alpha analogs.

Abstract: The subject invention concerns novel peptides of gamma interferon (IFN.gamma.) and methods of use of these peptides. Specifically exemplified are peptides from the C-terminus of IFN.gamma.. The subject peptides, once internalized into a cell, have biological activity which is comparable to the full-length IFN.gamma. protein.

Abstract: The subject invention pertains to novel methods for treating autoimmune-related diseases, such as Multiple Sclerosis (MS). One embodiment of the method of the invention comprises administering interleukin-10 (IL-10) and transforming growth factor-beta (TGF-.beta.), in combination, to a person afflicted with or predisposed to an autoimmune disease. When administered in combination, these cytokines act in a synergistic manner as suppressor factors to inhibit the activation of self-reactive T cells that are involved in autoimmune disease.

Abstract: The human immunodeficiency virus (HIV) contains, in addition to the canonical genes gag, pol, and env, an open reading frame in the 3' region of the genome that overlaps with the 3' long terminal repeat (LTR). Initial studies on the protein encoded by this ORF revealed a negative effect on HIV replication in vitro and this gene product was subsequently designated the negative factor, or Nef. The nef gene product is 25-29 kDa protein that localizes primarily to the cytoplasm of HIV-infected cells. The subject of this invention pertains to the discovery of a superantigen activity associated with this peptide and peptidic fragments derived therefrom. Superantigens are powerful T-cell mitogens that bind directly to major histocompatibility complex (MHC) class II molecules and form a binary complex with the variable .beta. (V.sub..beta.) region of the T-cell antigen receptor (TCR).

Abstract: The subject invention concerns novel peptide agonists and antagonists of staphylococcal enterotoxin A. Specifically exemplified are peptide agonists which stimulate T cell proliferation.

Abstract: The subject invention concerns novel peptides of gamma interferon (IFN.gamma.) and methods of use of these peptides. Specifically exemplified are peptides from the C-terminus of IFN.gamma.. The subject peptides, once internalized into a cell, have biological activity which is comparable to the full-length IFN.gamma. protein.

Abstract: The subject invention concerns novel peptide agonists and antagonists of staphylococcal enterotoxin A. Specifically exemplified are peptide agonists which stimulate T cell proliferation.

Abstract: The subject invention concerns novel superantigen proteins and peptides and methods of use of these superantigens. Specifically exemplified are peptide agonists from mouse mammary tumor virus, feline immunodeficiency virus and human immunodeficiency virus. The peptides can also be used to produce, purify and detect antibodies that bind to superantigens. These superantigens and their corresponding peptides can be used in both diagnostic and therapeutic protocols.

Abstract: The invention concerns novel AVP-binding peptides having the formula:Thr-Met-X-Val-Leu-Thr-Gly-Ser-Pro-Bwherein X is selected from the group consisting of Lys, Arg, and Asp; B is OH, NH.sub.2, NHAlk, wherein Alk is lower alkyl of 1-4 carbons, inclusive. These peptides block AVP function, and, therefore, are useful in many areas among which is the control of hypertension.