The invention concerns a trans-splicing RNA (tsRNA) molecule comprising one or multiple unstructured binding domains; a cell or vector comprising said tsRNA; and a method for killing cells or treating a disease using said tsRNA.

Methods of eliciting and/or modulating immune responses, therapeutic methods, and antigen delivery methods that include the step of administering a protein particle derived from a cell, the protein particle comprising a diphtheria toxin Cross Reacting Material (CRM) amino acid sequence are disclosed. Included are diagnostic methods using the protein particle derived from a cell, the protein particle comprising a diphtheria toxin CRM amino acid sequence. The methods disclosed herein may be useful as an antigen carrier delivery system.

Methods of eliciting and/or modulating immune responses, therapeutic methods, and antigen delivery methods that include the step of administering a protein particle derived from a cell, the protein particle comprising a diphtheria toxin Cross Reacting Material (CRM) amino acid sequence are disclosed. Included are diagnostic methods using the protein particle derived from a cell, the protein particle comprising a diphtheria toxin CRM amino acid sequence. The methods disclosed herein may be useful as an antigen carrier delivery system.

The present disclosure is the first to identify a host cell protein and its function with which MPT63 and MPT64, secreted antigens of Mycobacterium tuberculosis, interact, and to construct a recombinant MPT protein including each domain of MPT63 and MPT64 interacting with the host cell protein, and the recombinant MPT protein may be applied to a use for the prevention and treatment of tuberculosis by confirming that the recombinant MPT protein targets the Mycobacterium tuberculosis-infected macrophages and increases the ROS level and inflammatory cytokine expression in macrophages, thereby inducing the death of Mycobacterium tuberculosis. And MPT protein of the present disclosure can improve the vaccine effect by the BCG vaccine so that it can be used as a tuberculosis vaccine and/or vaccine adjuvant either alone or together with known tuberculosis vaccines.

The present disclosure is the first to identify a host cell protein and its function with which MPT63 and MPT64, secreted antigens of Mycobacterium tuberculosis, interact, and to construct a recombinant MPT protein including each domain of MPT63 and MPT64 interacting with the host cell protein, and the recombinant MPT protein may be applied to a use for the prevention and treatment of tuberculosis by confirming that the recombinant MPT protein targets the Mycobacterium tuberculosis-infected macrophages and increases the ROS level and inflammatory cytokine expression in macrophages, thereby inducing the death of Mycobacterium tuberculosis. And MPT protein of the present disclosure can improve the vaccine effect by the BCG vaccine so that it can be used as a tuberculosis vaccine and/or vaccine adjuvant either alone or together with known tuberculosis vaccines.

Provided is a recombinant BCG employing a pMyong2 vector system to express HIV-1 p24 and a use thereof as a HIV-1 vaccine. rBCG-pMyong2-p24, which is a pMyong2 vector system, was found to induce the upregulation of HIV-1 p24 gag expression in rBCG and infected antigen-presenting cells (APC) and to induce improved p24-specific immune responses in vaccinated mice, compared to rBCG-pAL-p24 in a pAL5000 derived vector system. rBCG-pMyong2-p24 was identified to exhibit a higher p24-specific Ab production level than rSmeg-pMyong2-p24 in the same pMyong2 vector system. Therefore, the recombinant BCG employing rBCG-pMyong2-p24 to express HIV-1 p24 according to the present invention is identified to elicit enhanced immune responses to HIV-1 infection in mouse model systems and thus can be expected to be used as a prime vaccine in the heterologous prime-boost vaccination strategy against HIV-1 infection.

Provided is a recombinant BCG employing a pMyong2 vector system to express HIV-1 p24 and a use thereof as a HIV-1 vaccine. rBCG-pMyong2-p24, which is a pMyong2 vector system, was found to induce the upregulation of HIV-1 p24 gag expression in rBCG and infected antigen-presenting cells (APC) and to induce improved p24-specific immune responses in vaccinated mice, compared to rBCG-pAL-p24 in a pAL5000 derived vector system. rBCG-pMyong2-p24 was identified to exhibit a higher p24-specific Ab production level than rSmeg-pMyong2-p24 in the same pMyong2 vector system. Therefore, the recombinant BCG employing rBCG-pMyong2-p24 to express HIV-1 p24 according to the present invention is identified to elicit enhanced immune responses to HIV-1 infection in mouse model systems and thus can be expected to be used as a prime vaccine in the heterologous prime-boost vaccination strategy against HIV-1 infection.

The present invention relates to the following compounds (I) wherein the integers are as defined in the description, and where the compounds may be useful as medicaments, for instance for use in the treatment of tuberculosis (e.g. in combination).

##STR00001##

The present invention discloses a preparation method for a disubstituted PEGylated interleukin 2, which comprises the steps of: (1) PEGylating IL-2 to obtain a crude product of a PEGylated interleukin; (2) performing gel chromatography filtration to remove free interleukin 2 from the crude product; (3) performing affinity chromatography on the product in the step (2) by means of an α receptor column, and collecting a flow-through peak component and an elution peak component; (4) performing ion exchange separation on the flow-through peak component and the elution peak component in the step (3); and (5) collecting components of the disubstituted PEGylated interleukin 2.

Biochemically active PASTA kinase inhibitors which exploit subtle structural differences between human kinases and bacterial PASTA kinases to improve specificity and inhibitor activity. The disclosed kinase inhibitors have the general formula:

##STR00001##

wherein: R.sub.1=Me, Et, n-Pr, —CH.sub.2CH.sub.2OH, —CH.sub.2CH.sub.2OP(O)(OH).sub.2, —CH.sub.2CH.sub.2NMe.sub.2; R.sub.2=H, Me, Et, o-Pr, i-Pr, CF.sub.3, Cl, OMe; R.sub.3=H, Me, NHMe, NHBn, Cl, NO.sub.2OMe, F, CN; and Ar=

##STR00002##