The present invention provides a Mitrecin A polypeptide useful in prevention and treatment of one or more bacteria. Also provided is a method to kill or prevent growth of one or more bacteria comprising contacting the one or more bacteria with a Mitrecin A polypeptide. The target bacteria can be selected from the group consisting of a Gram-positive bacterium, a Gram-negative bacterium, or both. In one embodiment, the present invention is drawn to a polynucleotide encoding a Mitrecin A polypeptide, a vector comprising the polynucleotide, a host cell comprising the polynucleotide, or a composition comprising the Mitrecin A polypeptide, the polynucleotide, the vector, or the host cell.

The present invention provides a Mitrecin A polypeptide useful in prevention and treatment of one or more bacteria. Also provided is a method to kill or prevent growth of one or more bacteria comprising contacting the one or more bacteria with a Mitrecin A polypeptide. The target bacteria can be selected from the group consisting of a Gram-positive bacterium, a Gram-negative bacterium, or both. In one embodiment, the present invention is drawn to a polynucleotide encoding a Mitrecin A polypeptide, a vector comprising the polynucleotide, a host cell comprising the polynucleotide, or a composition comprising the Mitrecin A polypeptide, the polynucleotide, the vector, or the host cell.

Described are methods and means for metabolic engineering and improved product formation by a filamentous micro-organism or a low G+C gram-positive bacterium. Disclosed is that DasR and DasR binding sites play an important and universal role in the control of gene expression in micro-organisms. Based on this finding, provided are multiple useful applications, such as a method for regulating the expression of a gene of interest, a method for controlling metabolism, a method for decreasing undesired expression and many more. Moreover, provided are means that can be used to establish said methods: for example a micro-organism in which the DasR binding site in operable linkage with a particular gene has been modified to obtain increased or decreased expression of a protein (being a desired or undesired protein) encoded by said gene.

Described are methods and means for metabolic engineering and improved product formation by a filamentous micro-organism or a low G+C gram-positive bacterium. Disclosed is that DasR and DasR binding sites play an important and universal role in the control of gene expression in micro-organisms. Based on this finding, provided are multiple useful applications, such as a method for regulating the expression of a gene of interest, a method for controlling metabolism, a method for decreasing undesired expression and many more. Moreover, provided are means that can be used to establish said methods: for example a micro-organism in which the DasR binding site in operable linkage with a particular gene has been modified to obtain increased or decreased expression of a protein (being a desired or undesired protein) encoded by said gene.

Polypeptides are provided that include an actinohivin variant polypeptide. The actinohivin variant polypeptide can be operably connected to an antibody fragment, such as a fragment crystallizable (Fc) region of immunoglobulin (Ig) G. Nucleic acid sequences, expression vectors, and transformed plant cells useful for producing the polypeptides are also provided. Further provided are methods for treating a viral infection or a cancer in a subject and include the step of administering the actinohivin variant polypeptide to the subject.

Polypeptides are provided that include an actinohivin variant polypeptide. The actinohivin variant polypeptide can be operably connected to an antibody fragment, such as a fragment crystallizable (Fc) region of immunoglobulin (Ig) G. Nucleic acid sequences, expression vectors, and transformed plant cells useful for producing the polypeptides are also provided. Further provided are methods for treating a viral infection or a cancer in a subject and include the step of administering the actinohivin variant polypeptide to the subject.

The invention concerns novel streptavidin muteins and methods of determining, immobilizing, isolating or purifying proteins under denaturing conditions. In one embodiment such a mutein has an Cys residue at sequence position 127 of the wild-type sequence of streptavidin and comprises at least one mutation in the region of the amino acid positions 117 to 121 with reference to the amino acid sequence of wild type streptavidin.

The invention concerns novel streptavidin muteins and methods of determining, immobilizing, isolating or purifying proteins under denaturing conditions. In one embodiment such a mutein has an Cys residue at sequence position 127 of the wild-type sequence of streptavidin and comprises at least one mutation in the region of the amino acid positions 117 to 121 with reference to the amino acid sequence of wild type streptavidin.

In accordance with the purpose(s) of the present disclosure, as embodied and broadly described herein, embodiments of the present disclosure, in some aspects, relate to genetically modified Streptomyces bacteria capable of increased thaxtomin production, genetically modified Streptomyces bacteria with reduced activity of a CebR protein encoded by a cebR gene and/or reduced activity of a β-glucosidase enzyme encoded by the bglC gene, genetically modified Streptomyces bacteria including a mutation of a native cebR gene and/or a native bglC gene, methods of increasing thaxtomin production in Streptomyces bacteria, methods of suppressing CebR and/or BglC activity, methods of producing thaxtomin, and thaxtomin produced by the methods of the present disclosure.

The invention concerns novel streptavidin muteins. In one embodiment such a the mutein (a) contains at least two cysteine residues in the region of the amino acid positions 44 to 53 with reference to the amino acid sequence of wild type streptavidin as set forth at SEQ ID NO: 212 and (b) has a higher binding affinity than (i) a streptavidin mutein “1” (SEQ ID NO: 112) that comprises the amino acid sequence Val.sup.44-Thr.sup.45-Ala.sup.46-Arg.sup.47 (SEQ ID NO: 98), or (ii) wild type-streptavidin of which amino acid residues 14 to 139 are shown as SEQ ID NO: 212 for peptide ligands comprising the amino acid sequence Trp-Ser-His-Pro-Gln-Phe-Glu-Lys (SEQ ID NO: 100).