C07K14/375

NOVEL MUTANT OF RECOMBINANT GANODERMA LUCIDUM IMMUNOMODULATORY PROTEIN AND USE THEREOF
20240424071 · 2024-12-26 ·

The present application relates to a recombinant protein comprising a spacer peptide and a recombinant Ganoderma lucidum immunomodulatory protein mutant (rLZ-8 mutant), wherein said rLZ-8 mutant comprises an amino acid sequence as shown in any one of SEQ ID NOS: 13 and 19-21, wherein said spacer peptide comprises 2 EAs (Glu Ala Glu Ala).

NOVEL MUTANT OF RECOMBINANT GANODERMA LUCIDUM IMMUNOMODULATORY PROTEIN AND USE THEREOF
20240424071 · 2024-12-26 ·

The present application relates to a recombinant protein comprising a spacer peptide and a recombinant Ganoderma lucidum immunomodulatory protein mutant (rLZ-8 mutant), wherein said rLZ-8 mutant comprises an amino acid sequence as shown in any one of SEQ ID NOS: 13 and 19-21, wherein said spacer peptide comprises 2 EAs (Glu Ala Glu Ala).

USE OF GALERINA MARGINATA GENES AND PROTEINS FOR PEPTIDE PRODUCTION

The present invention relates to compositions and methods comprising genes and peptides associated with cyclic peptides and cyclic peptide production in mushrooms. In particular, the present invention relates to using genes and proteins from Galerina species encoding peptides specifically relating to amatoxins in addition to proteins involved with processing cyclic peptide toxins. In a preferred embodiment, the present invention also relates to methods for making small peptides and small cyclic peptides including peptides similar to amanitin. Further, the present inventions relate to providing kits for making small peptides.

USE OF GALERINA MARGINATA GENES AND PROTEINS FOR PEPTIDE PRODUCTION

The present invention relates to compositions and methods comprising genes and peptides associated with cyclic peptides and cyclic peptide production in mushrooms. In particular, the present invention relates to using genes and proteins from Galerina species encoding peptides specifically relating to amatoxins in addition to proteins involved with processing cyclic peptide toxins. In a preferred embodiment, the present invention also relates to methods for making small peptides and small cyclic peptides including peptides similar to amanitin. Further, the present inventions relate to providing kits for making small peptides.

Histamine releaser contained in human sweat

Provided are a sweat allergy antigen, an antibody capable of binding to the antigen specifically, and others, which are produced utilizing a microorganism-originated protein that exists in sweat allergy patient in a dissolved state or a partial peptide of the protein.

Histamine releaser contained in human sweat

Provided are a sweat allergy antigen, an antibody capable of binding to the antigen specifically, and others, which are produced utilizing a microorganism-originated protein that exists in sweat allergy patient in a dissolved state or a partial peptide of the protein.

Isolation and application of BAD-1 for diagnosing infections with Blastomyces dermatitidis

Methods for obtaining highly pure native, recombinant or modified BAD-1 protein include the steps of culturing a population of microbes expressing BAD-1 protein in a culture medium, collecting the population of microbes from the culture medium, obtaining a BAD-1 protein-containing solution, and purifying the BAD-1 protein from the solution by combining the BAD-1 protein-containing solution with a nickel-chelating resin, washing the nickel-chelating resin to remove unbound matter, and eluting the BAD-1 protein from the nickel-chelating resin. Highly pure native BAD-1 protein may be used in diagnostic kits for detecting Blastomyces dermatitidis infections in animals.

Modified biotin-binding protein

The present invention provides a modified biotin-binding protein comprising an amino acid sequence represented by SEQ ID NO: 2 or its modified sequence and having a biotin-binding activity and replacement selected from the group consisting of: 1) replacement of the 36th serine residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond; 2) replacement of the 80th tryptophan residue of SEQ ID NO: 2 with a hydrophilic amino acid residue; 3) replacement of the 116th aspartic acid residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond; 4) replacement of the 46th proline residue of SEQ ID NO: 2 with a threonine, serine, or tyrosine residue and replacement of the 78th threonine residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond; 5) replacement of the 46th proline residue of SEQ ID NO: 2 with a threonine, serine, or tyrosine residue and replacement of the 116th aspartic acid residue of SEQ ID NO: 2 with an amino acid that does not form a hydrogen bond; and 6) replacement of the 46th proline residue of SEQ ID NO: 2 with a threonine, serine, or tyrosine residue, replacement of the 78th threonine residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond, and replacement of the 116th aspartic acid residue of SEQ ID NO: 2 with an amino acid that does not form a hydrogen bond.

Modified biotin-binding protein

The present invention provides a modified biotin-binding protein comprising an amino acid sequence represented by SEQ ID NO: 2 or its modified sequence and having a biotin-binding activity and replacement selected from the group consisting of: 1) replacement of the 36th serine residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond; 2) replacement of the 80th tryptophan residue of SEQ ID NO: 2 with a hydrophilic amino acid residue; 3) replacement of the 116th aspartic acid residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond; 4) replacement of the 46th proline residue of SEQ ID NO: 2 with a threonine, serine, or tyrosine residue and replacement of the 78th threonine residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond; 5) replacement of the 46th proline residue of SEQ ID NO: 2 with a threonine, serine, or tyrosine residue and replacement of the 116th aspartic acid residue of SEQ ID NO: 2 with an amino acid that does not form a hydrogen bond; and 6) replacement of the 46th proline residue of SEQ ID NO: 2 with a threonine, serine, or tyrosine residue, replacement of the 78th threonine residue of SEQ ID NO: 2 with an amino acid residue that does not form a hydrogen bond, and replacement of the 116th aspartic acid residue of SEQ ID NO: 2 with an amino acid that does not form a hydrogen bond.

Use of Galerina marginata genes and proteins for peptide production

The present invention relates to compositions and methods comprising genes and peptides associated with cyclic peptides and cyclic peptide production in mushrooms. In particular, the present invention relates to using genes and proteins from Galerina species encoding peptides specifically relating to amatoxins in addition to proteins involved with processing cyclic peptide toxins. In a preferred embodiment, the present invention also relates to methods for making small peptides and small cyclic peptides including peptides similar to amanitin. Further, the present inventions relate to providing kits for making small peptides.