in silico analysis and modeling of acp-mip–pilq chimeric antigen from neisseria meningitidis serogroup b

background: neisseria meningitidis, a life-threatening human pathogen with the potential to cause large epidemics, can be isolated from the nasopharynx of 5–15% of adults. the aim of the current study was to evaluate biophysical and biochemical properties and immunological aspects of chimeric acyl-carrier protein-macrophage infectivity potentiator protein-type iv pilus biogenesis protein antigen (acp-mip-pilq) from n. meningitidis serogroup b strain. methods: biochemical properties and multiple alignments were predicted by appropriate web servers. secondary molecular structures were predicted based on chou and fasman, garnier-osguthorpe-robson, and neural network methods. tertiary modeling elucidated conformational properties of the chimeric protein. proteasome cleavage and transporter associated with antigen processing (tap) binding sites, and t- and b-cell antigenic epitopes, were predicted using bioinformatic web servers. results: based on our in silico and immunoinformatics analyses, the acp-mip-pilq protein (amp) can induce high-level cross-strain bactericidal activity. in addition, several immune proteasomal cleavage sites were detected. the 22 epitopes associated with mhc class i and class ii (dr) alleles were confirmed in the amp. thirty linear b-cell epitopes as antigenic regions were predicted from the full-length protein. conclusion: all predicted properties of the amp indicate it could be a good candidate for further immunological in vitro and in vivo studies.