title: Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolyl cis/trans isomerase (PPIase) proteins.
abstract: Peptidyl prolyl cis/trans isomerases (PPIases) are a superfamily of proteins ubiquitously distributed among living organisms, which function primarily to assist the folding and structuring of unfolded and partially folded polypeptide chains and proteins. In this review, we focus specifically on the Macrophage Infectivity Potentiator (MIP)-like PPIases, which are members of the immunophilin family of FK506-binding proteins (FKBP). MIP-like PPIases have accessory roles in virulence and are candidates for inclusion in vaccines protective against both animal and human bacterial pathogens. A structural vaccinology approach obviates any issues over molecular mimicry and potential cross-reactivity with human FKBP proteins and studies with a representative antigen, the Neisseria meningitidis-MIP, support this strategy. Moreover, a dual approach of vaccination and drug targeting could be considered for controlling bacterial infectious diseases of humans and animals.
authors.affiliation: a Neisseria Research, Molecular Microbiology, Academic Unit of Clinical and Experimental Sciences, Sir Henry Wellcome Laboratories , University of Southampton Faculty of Medicine , Southampton , UK.
authors.forename: María Victoria
authors.initials: MV
authors.lastname: Humbert
authors.affiliation: a Neisseria Research, Molecular Microbiology, Academic Unit of Clinical and Experimental Sciences, Sir Henry Wellcome Laboratories , University of Southampton Faculty of Medicine , Southampton , UK.
authors.forename: Hannia L
authors.initials: HL
authors.lastname: Almonacid Mendoza
authors.affiliation: a Neisseria Research, Molecular Microbiology, Academic Unit of Clinical and Experimental Sciences, Sir Henry Wellcome Laboratories , University of Southampton Faculty of Medicine , Southampton , UK.
authors.forename: Alexandra C
authors.initials: AC
authors.lastname: Jackson
authors.affiliation: a Neisseria Research, Molecular Microbiology, Academic Unit of Clinical and Experimental Sciences, Sir Henry Wellcome Laboratories , University of Southampton Faculty of Medicine , Southampton , UK.
authors.forename: Miao-Chiu
authors.initials: MC
authors.lastname: Hung
authors.affiliation: a Neisseria Research, Molecular Microbiology, Academic Unit of Clinical and Experimental Sciences, Sir Henry Wellcome Laboratories , University of Southampton Faculty of Medicine , Southampton , UK.
authors.forename: Magdalena K
authors.initials: MK
authors.lastname: Bielecka
authors.affiliation: a Neisseria Research, Molecular Microbiology, Academic Unit of Clinical and Experimental Sciences, Sir Henry Wellcome Laboratories , University of Southampton Faculty of Medicine , Southampton , UK.
authors.forename: John E
authors.initials: JE
authors.lastname: Heckels
authors.affiliation: a Neisseria Research, Molecular Microbiology, Academic Unit of Clinical and Experimental Sciences, Sir Henry Wellcome Laboratories , University of Southampton Faculty of Medicine , Southampton , UK.
authors.forename: Myron
authors.initials: M
authors.lastname: Christodoulides
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001424:Bacterial Infections / Q000276:immunology / Q000517:prevention & control; D001426:Bacterial Proteins / Q000276:immunology*; D001428:Bacterial Vaccines / Q000276:immunology*; D015195:Drug Design; D006801:Humans; D016952:Legionella pneumophila / Q000276:immunology; D008264:Macrophages / Q000276:immunology*; D008585:Meningitis, Meningococcal / Q000276:immunology / Q000382:microbiology / Q000517:prevention & control; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000276:immunology / Q000472:pathogenicity; D019696:Peptidylprolyl Isomerase / Q000276:immunology*; D022021:Tacrolimus Binding Proteins / Q000276:immunology*; D022223:Vaccines, Subunit / Q000276:immunology*
chemical_list: D001426:Bacterial Proteins; D001428:Bacterial Vaccines; D022223:Vaccines, Subunit; D022021:Tacrolimus Binding Proteins; C512922:Mip protein, Legionella pneumophila; D019696:Peptidylprolyl Isomerase
keywords: Neisseria; macrophage infectivity potentiator protein; peptidyl prolyl cis/trans isomerase; structural vaccinology; virulence