期刊
EXPERT REVIEW OF VACCINES
卷 14, 期 12, 页码 1633-1649出版社
TAYLOR & FRANCIS LTD
DOI: 10.1586/14760584.2015.1095638
关键词
macrophage infectivity potentiator protein; Neisseria; peptidyl prolyl cis; trans isomerase; structural vaccinology; virulence
类别
资金
- University of Southampton
- GlaxoSmithKline
- Medical Research Council, UK [MR/K027131/1]
- MRC [MR/K027131/1] Funding Source: UKRI
- Medical Research Council [MR/K027131/1] Funding Source: researchfish
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.
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