Abstract: Minimal Motifs of linear B-cell epitopes in L1 structure protein from human papillomavirus type 58 (HPV 58) and their applications are disclosed. Eighteen linear epitope motifs and their extended 8-mer peptides in the L1 protein from HPV 58 are described, which can be used as antigens separately or in combination to specifically detect the serum from subjects with HPV 58 infection, or to develop preventive or therapeutic multi-epitope peptide vaccines against HPV 58 by inducing humoral immunity. Of the eighteen B-cell epitope motifs, ten of them are 100% conservative and one is highly conservative among many homologous proteins of high-risk HPVs. They can be used as candidate “universal” epitopes to develop preventive or therapeutic HPV vaccines. The amino acid sequences of the epitope motifs and the 8-mer peptide formula of the invention are shown below in SEQ ID No. 1-2, 2B, 3, 3B, 4-18, 18B, 19, 19B, and 20-32.

Abstract: Minimal Motifs of linear B-cell epitopes in L1 structure protein from human papillomavirus type 58 (HPV 58) and their applications are disclosed. Eighteen linear epitope motifs and their extended 8-mer peptides in the L1 protein from HPV 58 are described, which can be used as antigens separately or in combination to specifically detect the serum from subjects with HPV 58 infection, or to develop preventive or therapeutic multi-epitope peptide vaccines against HPV 58 by inducing humoral immunity. Of the eighteen B-cell epitope motifs, ten of them are 100% conservative and one is highly conservative among many homologous proteins of high-risk HPVs. They can be used as candidate “universal” epitopes to develop preventive or therapeutic HPV vaccines. The amino acid sequences of the epitope motifs and the 8-mer peptide formula of the invention are shown below in SEQ ID No. 1-2, 2B, 3, 3B, 4-18, 18B, 19, 19B, and 20-32.

Abstract: The invention belongs to the field of biological engineering techniques and relates to a thermophilic alkaline phosphoesterase. The invention provides an amino acid sequence of a thermophilic alkaline phosphoesterase of the invention, as well as a DNA fragment encoding the amino acid sequence. The present invention also includes methods for cloning an expression vector containing the DNA fragment or a portion thereof and for producing the recombinant enzyme. The invention also relates to a method for tagging biological macromolecules utilizing the enzyme.