5 results about "Superantigen" patented technology

The application discloses a targeting superantigen fusion protein based on an improved SE(3)-Transformer and an implementation method. In an offline stage, amino acid sequences are first converted into one-hot encoding or language model embedding (such as ESM-2), and are spliced with multiple sequence alignment (MSA) features for geometric initialization. A neural network (improved SE(3)-Transformer) combined with multiple sequence alignment (MSA) and an attention mechanism is constructed to predict the coordinates of C alpha, C, N and O atoms for main chain prediction, and the neural network is trained through a gradient descent method based on a physical heuristic potential item. In a verification stage, the improved SE(3)-Transformer after training is used to generate a predicted structure, conformational stability is verified through a simplified force field, and fine tuning is performed based on a confidence score. The application can accurately predict the structure of a target antigen epitope and an antibody variable region, optimize a superantigen functional domain in combination with a graph neural network, and dynamically design a flexible connecting peptide to realize modular fusion.

Provided herein are methods of immunizing against, treating or preventing streptococcal toxic shock syndrome in a subject, by administration of a group A streptococcus M protein, inclusive of fragments, variants or derivatives thereof, or an antibody that binds, or is raised against the M protein and optionally a group A streptococcus superantigen protein, inclusive of fragments, variants or derivatives thereof, or an antibody or antibody fragment that binds, or is raised against, the superantigen protein.

This invention relates to the fields of biomedicine and immunology, and particularly to the preparation and application of an anti-Staphylococcal enterotoxin B antibody. The antibody provided by this invention has a SEB-A8 heavy chain variable region containing CDR sequences as shown in SEQ ID NO:1-3, and a light chain variable region containing CDR sequences as shown in SEQ ID NO:9-11. It has significant application value in the treatment, prevention, and diagnosis of Staphylococcus aureus infections. Experimental data show that this antibody can effectively neutralize the superantigen activity of SEB, significantly improve the survival rate of MRSA-infected mice, and exhibit a dose-dependent protective effect. It can be used as a "non-antibiotic" treatment strategy for the treatment of methicillin-resistant Staphylococcus aureus infections, which is of great significance in controlling the development of bacterial resistance and provides a new research direction for clinical anti-infective therapy.

The present disclosure relates to pharmaceutical compounds and compositions and methods for treating an allergy and Crohn's disease. Methods for treating an allergy can include (a) predicting potential epitopes based proteomes of microbiome and that of an allergen, (b) filtering the potential epitopes obtained in step a) to result in a list of epitopes; and (c) reengineering the list of epitopes obtained in step b) to result in the new epitope. Methods for treating Crohn's disease can include (a), identifying one or more binding regions of an HLA class II protein and / or hemagglutinin to I2 superantigen; (b) determining a first peptide sequence corresponding to the one or more binding regions, and (c) producing a peptide inhibitor having a second peptide sequence that is a mutation of the first peptide sequence, wherein the second peptide sequence has a stronger binding affinity to the I2 superantigen than the first peptide sequence.

The present invention relates to a method of purifying a recombinant polypeptide from Host Cell Proteins (HCP), the method comprising: (a) applying a solution comprising the recombinant polypeptide and HCP to a superantigen chromatography solid support, (b) washing the superantigen chromatography solid support with a wash buffer comprising caprylate and arginine; and (c) eluting the recombinant polypeptide from the superantigen chromatography solid support.