Serine IgA1 proteases from Gramnegative bacteria are important virulence factors for a number of pathogens, including Neisseria meningitidis, Neisseria gonorrhoeae and Haemophilus influenzae. These highly specific enzymes catalyze the hydrolysis of ProSer or ProThr peptide bonds in the hinge region of secretory (sIgA1) and serum (IgA1) human immunoglobulin A1. By cleaving sIgA1 present on the host mucosa, IgA1 proteases facilitate the adhesion of pathogenic bacteria to the mucosal surface and the development of the inflammatory process. The prospect of using IgA1 proteases as the basis for a universal vaccine against N. meningitidis, N. gonorrhoeae and a significant part of H. influenzae strains is based on the high homology of the primary structures of these enzymes. Using the analysis of modern data by BLAST, we showed that the mature IgA1 protease (A28-P1004) from N. meningitidis serogroup B strain H44/76 has Top Identity above 85% in various strains of these pathogens. The aim of our research is to develop a broadspectrum vaccine candidate that would provide protection against all serogroups of N. meningitidis and against other pathogens that secrete homologous serinetype IgA1 proteases. We have created a number of recombinant proteins based on fragments of the IgA1 protease A28-P1004 and have shown that immunization of the host organism with these compounds leads to the formation of neutralizing antibodies that prevent the development of infection. As one of the possible methods of antigen delivery, the liposome method has been proposed. The conditions for obtaining two liposome preparations based on a recombinant protein with a molecular weight of 59.4 kDa and a DNA molecule in the vector encoding it in eukaryotic cells were screened. The resulting liposomal preparations can be used to create a vaccine against a number of pathogens that produce IgA1 protease. The work was supported by Project of Ministry of Science and Higher Education № 0751520211049.