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.

Keywords:

• macrophage infectivity potentiator protein
• Neisseria
• peptidyl prolyl cis/trans isomerase
• structural vaccinology
• virulence

Acknowledgements

This article made use of the Neisseria Multi Locus Sequence Typing Website (http://pubmlst.org/Neisseria) to update the allelic information on Nm- and Ng-MIP. The website was developed by Keith Jolley and is sited at the University of Oxford: development of this site has been funded by the Wellcome Trust and the European Union.