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71 results about "Primary sequence" patented technology

The primary structure (or sequence) of a peptide or protein is always written starting with the amino terminus on the left and progressing towards the carboxy terminus.

Moving image encoding method, moving image decoding method, moving image encoding device, moving image decoding device, program, and integrated circuit

An encoding method includes: a conversion step wherein the pixel values for an image are converted to a two-dimensional matrix formed with n coefficients which indicate the frequency; a quantization step wherein each of the n coefficients is quantized to generate n quantized coefficients; a sequence generation step wherein a one-dimensional sequence is generated based on tree structure information which defines a binary tree and on the two-dimensional matrix; and an encoding step wherein the primary sequence and at least a portion of the n quantized coefficients are encoded. The sequence generation step includes: a referent determination step (S31) wherein referent information, which indicates a position in the two-dimensional matrix which is referenced by each of n leaf nodes, is generated based on the two-dimensional matrix; a value assignment step (S32) wherein either a first or a second value is assigned to each node of the binary tree based on the two-dimensional matrix and the referent information; and a traversal step (S33) wherein the values assigned to each of the nodes are laid out in preorder to generate a one-dimensional sequence.
Owner:PANASONIC CORP

Modified tobacco mosaic virus particles as scaffolds for display of protein antigens for vaccine applications

Display of peptides or proteins in an ordered, repetitive array, such as on the surface of a virus-like particle, is known to induce an enhanced immune response relative to vaccination with the “free” protein antigen. The 2100 coat proteins comprising the rod-shaped capsid of Tobacco mosaic virus (TMV) can accommodate short peptide insertions into the primary sequence, but the display of larger protein moieties on the virion surface by genetic fusions to the capsid protein has not been possible. Since TMV lacks surface exposed residues compatible with commonly available linker chemistries, we employed a randomized library approach to introduce a reactive lysine at the externally located at the amino-terminus of the coat protein. We found that we could easily control the extent of virion conjugation and demonstrated stoichiometric biotinylation of the introduced lysine. To characterize this modular platform for the display of heterologous proteins, we bound a model antigen (streptavidin (SA)-green fluorescent protein (GFP), expressed and purified from plants) to the surface of TMV, creating a GFP-SA decorated virus particle. Rapid and quantitative determination of the level of TMV capsid decoration was accomplished by subjecting the complex to amino acid analysis and solving the family of linear equations relating the pmoles of each residue to the known amino acid composition of the complex components. We obtained a GFP-SA tetramer loading of 26%, which corresponds to display of approximately 2200 GFP moieties per intact virion. We evaluated the immunogenicity of GFP decorated virions in both mice and guinea pigs, and found augmented humoral IgG titers in both species, relative to unbound GFP-SA tetramer. In mice, we observed a detectable humoral immune response after only a single immunization with the TMV-protein complex. By demonstrating the presentation of whole proteins, this study expands the utility of TMV as a vaccine scaffold beyond that which is possible by genetic manipulation.
Owner:KENTUCKY BIOPROCESSING
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