161 results about "Gp41" patented technology

The present invention relates to peptides which exhibit potent anti-retroviral activity. The peptides of the invention comprise DP178 (SEQ ID:1) peptide corresponding to amino acids 638 to 673 of the HIV-1LAI gp41 protein, and fragments, analogs and homologs of DP178. The invention further relates to the uses of such peptides as inhibitory of human and non-human retroviral, especially HIV, transmission to uninfected cells.

An immunogenic composition able to provide an immune response to Human Complement Factor H binding on one or more HIV glycoproteins is disclosed, which is characterized by at least one binding site epitope of the glycoproteins. Such immunogenic composition wherein the glycoprotein comprises gp120, gp41, or both glycoproteins gp120 and gp41 is hereby disclosed. Sialic acid is removed to enhance immune recognition of the composition and to impair Factor H binding. A medication having an inhibitive action on autoimmune response by specific inhibition of the cleavage of C3b by Factor H into inactive cell fragments.

A group of compounds that inhibit HIV replication by blocking HIV entry was identified. One representative compound, designated NB-206, and its analogs inhibited HIV replication (p24 production) with IC₅₀ values at nanomolar levels. It was proved that NB-206 and its analogs are HIV entry inhibitors by targeting the HIV gp41 since: 1) they inhibited HIV-mediated cell fusion; 2) they inhibited HIV replication only when they were added to the cells less than one hour after virus addition; 3) they blocked the formation of the gp41 core that is detected by sandwich enzyme linked immunosorbent assay (ELISA) using a conformation-specific MAb NC-1; and 4) they inhibited the formation of the gp41 six-helix bundle revealed by fluorescence native-polyacrylamide gel electrophoresis (FN-PAGE). These results suggested that NB-206 and its analogs may interact with the hydrophobic cavity and block the formation of the fusion-active gp41 coiled coil domain, resulting in inhibition of HIV-1 mediated membrane fusion and virus entry.

The present application is directed to stabilized envelope glycoprotein trimers. The trimers are stabilized by introducing disulfide bonds at certain sites in the gp41 ectodomain. DNA molecules encoding such trimers can be used to generate an immunogenic reaction.

The invention concerns a purified recombinant glycoprotein having the following properties: a) an adherence capacity to CD4; b) an affinity with a anti-gp120 antibody capable of neutralizing in vitro HIV cell infection; c) an affinity with an anti-gp41 antibody; d) a timeric form free from inter-chain disulphide bonds. The invention also concerns a vaccine comprising said purified glycoprotein and an adjuvant. The invention further concerns a method for obtaining said glycoprotein, which consists in expressing, by means of genetic recombining techniques, a glycoprotein corresponding to the properties a), b) and c) mentioned above; purifying it, and subjecting it to steps involving at least a reducing agent, an ionic detergent and/or a neutral detergent in conditions leading to a glycoprotein having said properties.

Provided are synthetic peptides based on a native sequence of HIV gp41 HR2 except that the synthetic peptides have a plurality of amino acid replacements comprising (a) a helix-promoting amino acid, or (b) a combination of helix-promoting amino acids, and charged amino acids introduced to form ion pairs in the synthetic peptide; wherein the synthetic peptides demonstrate an unexpected, improved biological activity, as compared to a peptide having an amino acid sequence without the plurality of amino acid substitutions. Also provided are polynucleotides encoding synthetic peptide, and methods of using these synthetic peptides in inhibition of, or as compositions to inhibit, transmission of HIV to a target cell.

The present invention relates to peptides which exhibit potent anti-retroviral activity. The peptides of the invention comprise DP178 (SEQ ID:1) peptide corresponding to amino acids 638 to 673 of the HIV-1LAI gp41 protein, and fragments, analogs and homologs of DP178. The invention further relates to the uses of such peptides as inhibitory of human and non-human retroviral, especially HIV, transmission to uninfected cells.

The present invention is based upon the surprising discovery that exposure of a non-resistant HIV to a first entry inhibitor, such as an anti-CD4 antibody or a co-receptor inhibitor, which like all current HIV drugs selects for mutations that result in a resistant HIV, surprisingly results in HIV viruses much more susceptible to neutralization by a second entry inhibitor, such as soluble CD4 (sCD4) or an HIV gp41 inhibitor. Therefore, the present invention provides methods and compositions for inhibiting HIV-1 infection in a subject that overcomes the problem of drug resistance.

The invention relates to a kind of affirmation regent for antibody of human immunodeficiency virus, and the diagnosing regent consists of HIV-I type specificity protein gp160, gp120, gp41, p66, p24, mixed fiber film which is encysted by HIV-II specificity protein gp36, enzyme conjugates and other component, and the principle of indirect process is provided for the affirmation of antibody of HIV-I and HIV-II type.

An isolated polypeptide that has an amino acid sequence that is substantially homologous to consecutive amino acids of a c-terminal portion of the membrane proximal external region (MPER) of gp41 includes an immunogenic epitope reactive with at least one anti-HIV antibody.

This invention relates to novel peptide immunogens that generate an immune response in mammals against HIV gp41, to pharmaceutical compositions that comprise such immunogens, and to methods of treating Immunodeficiency disease, especially HIV infection and AIDS, that employ such pharmaceutical compositions.

The invention discloses elastin-like polypeptides (ELP) for prokaryotic expression of fusion protein Prx by a non-digestion and non-chromatography purifying method and belongs to the field of genetic engineering. According to the elastin-like polypeptides, the type of the fourth amino acid in an elastin-like pentapeptide unit is changed and the elasticity function of the fourth amino acid is improved, and therefore, the reduction of the ELP length becomes possible. The ratio of K, V and F in the fourth basic group in the ELP pentapeptide unit is enabled to be 1: 6: 3. In terms of inteins, the high-efficiency intein gp41-1 is adopted; the C-terminal and the N-terminal of the intein are expressed separately, and the internal gene of the intein is mutated. The elastin-like polypeptides (ELPs) are ELP-IN and precursor protein ELP-IC-PrxI. The protein Prx is purified in a non-chromatography way by use of the elasticity function of the elastin-like polypeptides; no chromatographic column is required for separation, and the target protein precipitates by virtue of incubation at a certain temperature; besides, the precipitate can be re-dissolved in a buffer solution, and consequently, the protein can be purified more efficiently and quickly.