29 results about "Protein domain" patented technology

This invention provides a dengue / Zika virus genetically engineered vaccine and its application. The dengue / Zika virus vaccine comprises an open reading frame encoding envelope protein domain III (EDIII) and the non-structural protein NS1, and displays EDIII monomers in the delivery vector shell. Immunization with this vaccine primarily induces a type-specific antibody response, reducing the production of cross-antibodies and thus effectively avoiding or eliminating the risk of antibody-dependent enhancement of infection (ADE). This vaccine can be used to prevent dengue virus and Zika virus infection.

Disclosed herein are vaccine compositions, in particular, polyvalent icosahedral compositions for antigen presentation. The disclosed compositions may contain an S particle made up of recombinant fusion proteins. The recombinant fusion proteins may include a norovirus (NoV) S domain protein, a linker protein domain operatively connected to the norovirus S domain protein, and an antigen protein domain operatively connected to said linker.

The application provides a dengue virus protection and mosquito vector control antigen composition and application thereof. The antigen composition comprises a combination of dengue virus type 1-4 envelope protein domain III polypeptide and Aedes aegypti midgut mucin AaMuc1 antigen polypeptide; the amino acid sequences of the dengue virus type 1-4 envelope protein domain III polypeptide are respectively shown as SEQ ID NO. 1, SEQ ID NO. 2, SEQ ID NO. 3 and SEQ ID NO. 4; and the amino acid sequence of the Aedes aegypti midgut mucin AaMuc1 antigen polypeptide is shown as SEQ ID NO. 5. The prepared vaccine can induce the body to produce neutralizing antibodies against dengue virus type 1-4, achieve the protection of human body from dengue virus infection, induce the production of active antibodies targeting Aedes aegypti midgut mucin 1, inhibit and kill the dengue virus transmission vector Aedes aegypti, and achieve the dual prevention and control of dengue fever from two dimensions of infection prevention and transmission interruption.

The invention provides a preparation method of a genetically modified mouse capable of mediating Tbx1 inherent disorder protein structural domain deletion. The method comprises the following steps: (a) constructing a targeting vector; (b) preparing a gene editing compound; (c) microinjection; (d) embryo transplantation and screening; (e) breeding and establishing a stable strain. Sequencing verifies that the gene modified mouse can stably express the Tbx1 mutant protein which lacks IDR and carries an N-terminal 3xFlag tag, and a homozygote mutant mouse shows remarkable developmental defects such as ventricular septal defect and craniofacial deformity; and an important genetic tool is provided for researching the action mechanism of the phase separation characteristic of the Tbx1 protein in the heart, craniofacial development and congenital heart disease (such as DiGeorge syndrome).

Provided is an antibody for the treatment or prevention of autoimmune diseases, comprising a heavy chain variable region represented by SEQ ID NO: 1 or SEQ ID NO: 24, and a light chain variable region represented by SEQ ID NO: 6, SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, or SEQ ID NO: 25.

Provided herein are compositions comprising light-and-magnetoresponsive protein domain, such as engineered light-oxygen-voltage-sensing (LOV) domains, and methods of using the same. The light-and magnetoresponsive proteins domains may be used to form compositions such as fusion proteins comprising heterologous protein components and bioluminescent protein domains with activity that is dependent on the presence of light, e.g., light emitted by a reaction catalyzed by the bioluminescent protein domain, and on the presence of a magnetic field.

Methods of treating ocular diseases such as age-related macular degeneration may include the administration of peptides comprising complement factor H and factor H-like protein domains to reduce an amount of geographic atrophy in a subject in need thereof. These methods may be administered by intraocular, intervascular or subcutaneous injection.

A CRISPR-Cas system and applications thereof are provided, also related to a Cas protein, a fusion protein and a guide polynucleotide. The Cas protein has at least 50% sequence identity compared to the sequence set forth in any one of SEQ ID NOs: 1-184, 426-428. The fusion protein comprises the Cas protein fused to a protein domain and / or a polypeptide tag. The guide polynucleotide comprises a direct repeat sequence having at least 70% sequence identity to any one of SEQ ID NOs: 185-199, 245-247, 287-303, 369 and 370-373, and a guide sequence engineered to hybridize to a target nucleic acid. The CRISPR-Cas system comprises a Cas protein having at least 90% sequence identity compared to the sequence set forth in any one of SEQ ID NOs: 1-184, 426-428, or a nucleic acid encoding thereof, and a guide polynucleotide or a nucleic acid encoding thereof.

A thermally responsive nanosphere for binding to biofilms including a gold nanoparticle core functionalized with a polyethylene glycol; an R2ab fusion protein construct including an anchor that is a stable globular domain having a surface accessible cysteine residue, a linker, an S. epidermidis R2ab protein of SEQ ID NO. 1, and an elastin-like polypeptide. The linker may be a protein having SEQ ID NO. 7; and the anchor may be a modified third IgG binding domain from streptococcal protein G (GB3) having SEQ ID NO. 3, a ubiquitin protein having SEQ ID NO. 4, a Pin1 WW domain having SEQ ID NO. 5, and a fibronectin protein domain 3FN3 having SEQ ID NO. 6. A method for treating a biofilm containing S. epidermidis bacteria by binding a plurality of the nanospheres to the biofilm and exposing the biofilm to laser irradiation.

To provide compositions and methods for increasing efficiency of targeted genome / epigenetic modification in eukaryotic cells.SOLUTION: A fusion protein comprises at least one nucleosome interacting protein domain linked to a programmable DNA modification protein. A method for increasing efficiency of targeted genome or epigenetic modification in an eukaryotic cell comprises introducing, into the eukaryotic cell, the fusion protein or a nucleic acid encoding the fusion protein.SELECTED DRAWING: None

Provided are a method, an apparatus, and a computer program for predicting interaction between a compound and a protein. A method for predicting interaction between a compound and a protein according to some embodiments of the present disclosure may comprises the steps of: acquiring learning data composed of compound data for learning, protein data for learning, and interaction scores; constructing a deep-learning model by using the acquired learning data; and predicting interaction of a given compound and protein through the constructed deep-learning model. Through the learning of the deep-learning mode with the exclusion of amino acid sequences associated with protein domains having a negative influence on interactions from amino acid sequences of proteins for learning, the interaction between a given compound and protein in the in vivo environment can be accurately predicted.

The invention discloses a protein structural domain function prediction method and device based on a long short-term memory network, terminal equipment and a storage medium, and the method comprises the steps: obtaining a to-be-detected protein amino acid sequence, and coding the to-be-detected protein amino acid sequence to obtain a coded sequence; the coded sequence is input into a bidirectional long short-term memory network, the bidirectional long short-term memory network extracts a forward hidden state from the N end to the C end of the coded sequence through a forward LSTM, extracts a reverse hidden state from the C end to the N end of the coded sequence through the forward LSTM, and the forward hidden state and the reverse hidden state are spliced to obtain a bidirectional hidden state; performing global pooling operation on the bidirectional hidden states of all the time steps to generate a global feature vector; and carrying out linear transformation on the global feature vector, and predicting to obtain the protein structural domain function of the amino acid sequence of the to-be-detected protein. By implementing the method, the efficiency of protein structure domain function analysis can be improved.

The present invention relates to the field of genetic engineering. In particular, the present invention relates to a genome editing fusion protein comprising a CRISPR effector protein domain and a deaminase domain, as well as a bifunctional genome editing system comprising said genome editing fusion protein and uses thereof.

The application discloses a novel coronavirus vaccine for promoting specific IgA antibody secretion and a construction method and application thereof, belongs to the field of immunology and the field of genetic engineering, and is an immunogen developed by taking S protein as the vaccine (the same is true for other structural proteins of the novel coronavirus, such as N protein or E protein or M protein), aims to improve the mucosal IgA expression level after immunization of the vaccine, and constructs a novel coronavirus vaccine which can significantly promote human B lymphocytes to secrete specific anti-S protein IgA antibodies in the process of stimulating the immune response of the body by the S protein, and further enhance the mucosal protection and defense function, and provides a construction technology, method and application thereof. By introducing a specific protein domain, IL-5 (referred to as 'adjuvant protein'), into the S protein of the novel coronavirus, a novel coronavirus vaccine modified by the 'adjuvant protein' is formed.

The application provides a coordination nanometer assembly of a chiral cyclic peptide and a manganese ion, a preparation method and application thereof, the method of the application combines a manganese superoxide dismutase protein domain with a unique tumor microenvironment of a melanoma high tyrosinase, and first designs polypeptide sequences with different chirality L‑ Y D‑ h L‑ D D‑ h、 L‑ Y L‑ H L‑ D L‑ H and D‑ y D‑ h D‑ d D‑ h, regulates polypeptide chirality, improves in-vivo circulation stability and cell entry efficiency of the nanometer assembly, coordinates self-assembly of manganese and the chiral cyclic peptide, simulates in-situ oxidation of the tumor microenvironment for photothermal therapy, and coats cell membranes. The method of the application is simple, the experimental conditions are mild, and the method is easy to operate, the cell membrane coated nanometer assembly prepared by the method not only has long circulation stability and high cell entry efficiency, but also can realize mild photothermal therapy through in-situ oxidation, release manganese ions to activate the CGAS-STING pathway for tumor immunotherapy, and has potential application value in the field of tumor combination therapy.

The invention discloses a vaccine for preventing and treating swine Japanese encephalitis virus and application, and belongs to the field of biological pharmacy for livestock. The CHO stable expression cell line expressing the E protein Domain III is constructed, transcription and protein expression levels are remarkably improved, the cell line grows under the glutamine-free condition, accumulation of metabolites such as ammonia is reduced, and cell activity and long-term culture stability are improved. The FC fusion protein is added after the ED3 gene sequence through the flexible Linker, so that the affinity chromatography purification process is simplified, the recovery rate and the purity are improved, and the production cost is reduced; meanwhile, the high-efficiency expression of CHO cells is combined, so that the purified protein yield is higher than 2g / L, which is far better than that of a traditional method, and the large-scale requirement of veterinary vaccines is met. The vaccine provided by the invention has no pathogen residual risk, the safety is higher than that of the traditional inactivated or attenuated live vaccine, and the vaccine which is safe, reliable and good in immunogenicity is provided for preventing and treating infection of the swine Japanese encephalitis virus.

A method and apparatus for generating a main chain structure of a protein, and a device and a storage medium. The method comprises: on the basis of distance information between atoms in a plurality of protein domains, generating a plurality of feature maps corresponding to the plurality of protein domains; by means of combining the plurality of feature maps, generating a fused feature map; and generating a main chain structure of a protein by means of using a first model to process the fused feature map, thereby improving the quality and stability of long-chain protein design.

To provide compositions and methods for treating diseases or disorders associated with pathological calcification or pathological ossification.SOLUTION: Provided are a compound having a structure of protein-Z-domain-X-Y, wherein the protein is a specific sequence derived from ectonucleotide pyrophosphate / phosphodiesterase-1 or a mutant thereof, the domain is a human IgGFc domain or a human serum albumin protein and a fragment thereof, X and Z are polypeptides having a specific amino acid sequence of 20 or less, and Y is a compound consisting of a specific amino acid sequence, and a composition and a treatment method for treating systemic arterial calcification of infancy (GACI), idiopathic arterial calcification of infancy (IIAC), and the like.SELECTED DRAWING: None

One objective is to provide a CD3 antibody that can bind to primate CD3, possesses appropriate CD3-binding ability, and has a stable single-chain scFv structure. [Solution] The present invention discloses an antibody targeting CD3, a bispecific antibody, and its use. The CD3-targeting antibody comprises a light chain variable region (VL) and a heavy chain variable region (VH), wherein the VL is the amino acid sequence shown in SEQ ID NO: 56 or a variant thereof, and the VH is a mutation in the amino acid sequence shown in SEQ ID NO: 42, wherein the mutation is selected from one or more amino acid residues at positions 30, 73, 76, 78, 93, and 94. The bispecific antibody comprises a first protein domain and a second protein domain, wherein the first protein domain contains the CD3-targeting antibody. The CD3-targeting antibody of the present invention reduces the toxicity caused by cytokine release syndrome, and the bispecific antibody produced using it is stable, has T cell binding ability, and is easier to produce.

The invention relates to the technical field of genetic engineering and bioinformatics, in particular to a method for creating a new gene in a living body on the premise of no artificial DNA template and application. The method is characterized in that DNA fractures are simultaneously generated at at least two different specific positions in the genome of an organism, the specific positions are genomic sites capable of segmenting different gene elements or different protein structural domains, and the DNA fractures are connected with one another by means of non-homologous end connection (NHEJ) or homologous repair. And generating a new combination of the different gene elements or different protein structural domains, which is different from the original genome sequence, so as to form a new gene. The new gene provided by the invention can change the growth, development, resistance, yield and other characters of organisms, and has important application value.

The application discloses a molecular recruitment co-localization system, comprising: a spatially targeted visualization module for recruiting target proteins to a specific site and generating a fluorescence co-localization signal in living cells based on the target proteins recruited to the specific site; a multi-protein interaction verification module for observing protein interactions in a multi-protein complex based on different pairs of proteins recruited to the specific site at a specified genetic locus; a protein binding capacity evaluation module for quantitatively analyzing the binding capacity between proteins based on the co-localization percentage and signal-to-noise ratio of the proteins; a protein phase separation capacity evaluation module for rapidly evaluating whether different proteins or protein domains have phase separation capacity based on the recruitment of the different proteins or protein domains to a specific location; and a dynamic observation and quantitative evaluation module for observing the dynamic changes of proteins in the phase separation process in real time by combining multi-channel fluorescence and quantum dot probes and providing preliminary quantitative data for the physical properties of the condensate.

The present application relates to the technical field of genetic engineering, and particularly relates to a maize ZmBARK1 sequence and application of a protein coded by the ZmBARK1 sequence in regulating low-temperature tolerance of maize in a germination stage. The present application finds a connection between the ZmBARK1 gene and the low-temperature tolerance of maize in the germination stage. After verification, it is found that the low-temperature tolerance of maize in the germination stage is significantly improved after the coding protein domain of the ZmBARK1 gene is deleted in the maize, which has important significance in the field of cultivating low-temperature tolerant maize varieties. The present application provides a new way for exploring new low-temperature tolerant materials of maize in the germination stage, lays a genetic material foundation for subsequent research, and provides a good information platform for low-temperature tolerant gene resources of maize in the germination stage. The present application is helpful for analyzing the genetic mechanism of low-temperature tolerance of plants in the germination stage and the research of molecular breeding, and lays a theoretical foundation for breeding and improving the genetic quality of low-temperature tolerant varieties of maize and other plants in the germination stage.

The present invention features thermostable protein binding scaffolds containing framework regions and variable loop regions that can be mutagenized to bind a desired target. The scaffolds are derived from the Carbohydrate Binding Module Family 32 (CBM32) protein domain of Clostridium perfringens hyaluronidase (NagH). The robust framework of the scaffolds described herein allows for the development of custom, high performance affinity chromatography resins compatible with the harsh conditions of process-scale applications that can be adaptable to a wide diversity of target substrates.

The present invention relates to protein bacteriocins (PBs) as therapeutic agents, specifically protein complexes comprising two or more PB molecules associated with a protein scaffold, wherein the protein scaffold comprises a cognate immunity protein domain for each PB effector moiety. In particular, the present invention provides an antibacterial protein complex comprising: (a) a first PB molecule and a second PB molecule; and (b) an immunity protein scaffold comprising a first immunity protein domain and a second immunity protein domain, wherein the first and second immunity protein domains are non-covalently bound to the first and second PB molecules, respectively.

We describe novel Staphylococcal Protein A ligands that enable milder elution pH for use in affinity chromatography. The change in elution pH is the result of point mutations to the protein sequence. Two novel ligands are investigated in this study. The first, designated Z(H18S)4, represents a histidine to serine substitution single mutation. The second, designated Z(H18S, N28A)4, is a double mutant comprising histidine to serine and asparagine to alanine mutations. Both are compared against the unmutated sequence, designated Z4, which is currently utilized in a commercially available Protein A stationary phase for the purification of molecules containing Fc domains. The ligands are coupled to a chromatography support matrix and tested against a panel of antibodies and an Fc fusion protein for elution pH, dynamic binding capacity, step-wise elution, and capture from clarified culture media. Results demonstrate that the novel ligands result in milder elution pH, on average >0.5 pH units, when tested in a pH gradient. For step-wise elution at pH 4.0, the Z(H18S, N28A)4 ligand showed on average a greater than 30% increase in yield compared to Z4. Importantly, for the antibodies tested the mutations did not result in a decrease in dynamic binding capacity or other desirable attributes such as selectivity. A potential application of the novel ligands is shown with a pH sensitive molecule prone to aggregation under acidic conditions.

An ontologized knowledge semantic annotation method for a protein domain and an online analysis engine system. By integrating differently defined protein domain data types, a protein domain semantic annotation map is provided for a user. The proposed semantic annotation method comprises: using protein domain information and protein ontology annotations to construct a mapping matrix between domains / superdomains and ontology terms; respectively performing overall statistical inference and relative statistical inference on the mapping matrix to retain the most relevant ontology terms; and obtaining domain-centric ontology annotations according to a real path rule, and for each domain / superdomain, screening for an association relationship between terms according to the obtained overall statistical inference result and relative statistical inference result, so as to form an ontology annotation configuration file. A user is supported to perform semantic annotation on a corresponding protein domain, and enrichment analysis of ontologized knowledge is also supported, thereby providing a strong support for exploration in the field of protein domain semantic annotation.

To provide antibodies for treating or preventing autoimmune diseases.SOLUTION: Provided is an in vivo or in vitro method including: administering a cell including an antibody or antigen-binding fragment thereof, an antibody conjugate, a multispecific antibody, a fusion protein, or a pharmaceutical composition that specifically binds to human IL-12 / IL-23p40, the antibody or antigen-binding fragment thereof blocking the function of an interleukin IL-12 / IL-23p40 protein domain and including heavy and light chain variable regions that include specific amino acid sequences; and administering to a subject in need thereof an effective amount of any one of the disclosed antibodies or antigen-binding fragments thereof, antibody conjugates, multispecific antibodies, fusion proteins, or pharmaceutical compositions.SELECTED DRAWING: None

The application provides a recombinant Protein L protein and a preparation method and application thereof. The recombinant Protein L protein is a mutant of a Protein L protein domain B5, and is characterized in that the mutant is 1-6 repeat units, each repeat unit is obtained by mutation of an amino acid sequence of the B5 domain, and the mutation position is one or multiple positions of 18, 53 and 68 of the B5 domain. The application selects a strong alkali-resistant domain, the B5 domain of the Protein L protein as a template, and through mutation of amino acids, the protein has strong alkali resistance in a protein purification process, and the purification efficiency is improved.

A method, a device, and a computer program for predicting the interaction between a compound and a protein are provided. A method for predicting the interaction between a compound and a protein, according to some embodiments of the present disclosure, may include: acquiring compound data for training, protein data for training, and training data including interaction scores; constructing a deep-learning model by using the acquired training data; and predicting the interaction between the given compound and protein by using the constructed deep-learning model. The interaction between the given compound and protein in an in vivo environment can be accurately predicted by training the deep-learning model, while excluding, from an amino acid sequence of the protein for training, amino acid sequences associated with a protein domain having a negative influence on the interaction.