Disclosed herein are bacterial proteins that increase pancreatic beta (β) cell number and/or proliferation, methods of increasing β cell number and/or proliferation using such proteins, and methods of treating or inhibiting diabetes in a subject by administering such proteins to the subject. In some embodiments, the protein has at least 80% sequence identity to the amino acid sequence set forth as any one of SEQ ID NOs: 1-7, or fragments thereof. Recombinant vectors including a nucleic acid encoding the protein (such as a nucleic acid encoding a protein with at least 80% sequence identity to any one of SEQ ID NOs: 1-7 or fragments thereof) operably linked to a heterologous promoter are also disclosed. Also disclosed are methods of identifying compounds that increase β cell number and/or proliferation by determining the effect of test compounds on β cell number or proliferation in zebrafish pancreas.

The present disclosure relates to immunogenic polypeptides, immunogenic compositions and vaccine compositions and use thereof for immunization of mammals susceptible to Streptococcus suis infection. The disclosure also relates to methods for preparing, formulating and administrating such compositions.

The present disclosure relates to immunogenic polypeptides, immunogenic compositions and vaccine compositions and use thereof for immunization of mammals susceptible to Streptococcus suis infection. The disclosure also relates to methods for preparing, formulating and administrating such compositions.

The disclosure provides a method of separation of at least one ABD-containing molecule present in a liquid from other constituents in the liquid, comprising a step of affinity separation, in which step is used, as affinity ligand, an ABD binding polypeptide comprising an ABD binding motif BM, which motif consists of an amino acid sequence selected from TABLE-US-00001 (SEQ ID NO: 166) EX.sub.2X.sub.3X.sub.4AX.sub.6X.sub.7EIX.sub.10X.sub.11LPNLX.sub.16X.sub.17X.sub.18QX.sub.20X.sub.21AFIX.sub.25X.sub.26LX.sub.28D
and amino acid sequences with at least 89% identity thereto.

The disclosure provides a method of separation of at least one ABD-containing molecule present in a liquid from other constituents in the liquid, comprising a step of affinity separation, in which step is used, as affinity ligand, an ABD binding polypeptide comprising an ABD binding motif BM, which motif consists of an amino acid sequence selected from TABLE-US-00001 (SEQ ID NO: 166) EX.sub.2X.sub.3X.sub.4AX.sub.6X.sub.7EIX.sub.10X.sub.11LPNLX.sub.16X.sub.17X.sub.18QX.sub.20X.sub.21AFIX.sub.25X.sub.26LX.sub.28D
and amino acid sequences with at least 89% identity thereto.

An isolated nucleic acid that includes an open reading frame encoding a lanthipeptide protease polypeptide for scarless tag removal from a polypeptide is presented. Reagents, expression constructs and methods are also provided for preparing a scarless tag polypeptide product from a tagged polypeptide precursor containing a lanthipeptide protease cleavage site. The reagents are directed to novel lanthipeptide proteases and expression constructs and polypeptide precursors that include highly specific lanthipeptide protease substrate recognition sequence. Methods are provided that enable scarless tag removal from a cognate lanthipeptide, a non-cognate lanthipeptide or a heterologous polypeptide that includes extraneous amino acid sequences, such as leader peptides and tags.

An isolated nucleic acid that includes an open reading frame encoding a lanthipeptide protease polypeptide for scarless tag removal from a polypeptide is presented. Reagents, expression constructs and methods are also provided for preparing a scarless tag polypeptide product from a tagged polypeptide precursor containing a lanthipeptide protease cleavage site. The reagents are directed to novel lanthipeptide proteases and expression constructs and polypeptide precursors that include highly specific lanthipeptide protease substrate recognition sequence. Methods are provided that enable scarless tag removal from a cognate lanthipeptide, a non-cognate lanthipeptide or a heterologous polypeptide that includes extraneous amino acid sequences, such as leader peptides and tags.

The invention provides proteins from group B streptococcus (Streptococcus agalactiae) and group A streptococcus (Streptococcus pyogenes), including amino acid sequences and the corresponding nucleotide sequences. Data are given to show that the proteins are useful antigens for vaccines, immunogenic compositions, and/or diagnostics. The proteins are also targets for antibiotics.

The invention provides proteins from group B streptococcus (Streptococcus agalactiae) and group A streptococcus (Streptococcus pyogenes), including amino acid sequences and the corresponding nucleotide sequences. Data are given to show that the proteins are useful antigens for vaccines, immunogenic compositions, and/or diagnostics. The proteins are also targets for antibiotics.

Pre-conditioning a vaccine site with a potent recall antigen such as tetanus/diphtheria (Td) toxoid can significantly improve the lymph node homing and efficacy of tumor antigen-specific DC vaccines. Patients given Td had enhanced DC migration bilaterally and significantly improved survival. In mice, Td pre-conditioning also enhanced bilateral DC migration and suppressed tumor growth in a manner dependent on the chemokines CCL3 and CCL21 and Td-activated CD4.sup.+ T cells. Interference with any component of this axis markedly reduced Td-mediated DC migration and antitumor responses. Our clinical studies and corroborating investigations in mice suggest that pre-conditioning with a potent recall antigen represents a viable strategy to increase DC homing to lymph nodes and improve antitumor immunotherapy.