InterPro : IPR008104

Name  Macrophage infectivity potentiator Short Name  INFPOTNTIATR
Type  Family Description  Legionella pneumophila, the causative agent of Legionnaire's disease, is a facultative intracellular microbe that commonly infects human lung monocytes and macrophages and causes pneumonia []. It is water-borne and highly virulent, relying on several specific pathogenic factors to invade and infect the alveolar tissue. However, once grown to stationary phase in culture, the pathogen spontaneously converts to an avirulent state []. The major virulence factor expressed by Legionella pneumophilais the macrophage infectivity potentiator (Mip) []. Site-directed mutagenesis studies of this protein in vitro severely impaired the intracellular infection of human macrophages by L. pneumophila, causing it to lose its potent antigenic activity []. Further studies into the enzymatic activity of Mip have revealed that it plays a similar role to eukaryotic FK506-binding proteins. In vivo, it acts as a peptidyl-prolyl-cis/trans- isomerase (PPIase) on oligopeptides [], although it is unclear whether this forms part of the virulence process. Substitution of Asp142 of the mature protein by Leu severely reduces the PPIase activity of Mip []. The structure of Mip has been resolved to 2.41A by X-ray crystallography [], revealing the virulence factor to exist as a homodimer. Each monomer consists of an N-terminal dimerisation module, a long central connecting alpha-helix and a conserved PPIase domain at the C terminus.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR000774 Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal PPIase_FKBP_N Domain

0 Found In

1 Parent Features

Id Name Short Name Type
IPR023566 Peptidyl-prolyl cis-trans isomerase, FKBP-type PPIase_FKBP Family

5 Publications

First Author Title Year Journal Volume Pages
Fischer G Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity. 1992 Mol Microbiol 6 1375-83
Engleberg NC DNA sequence of mip, a Legionella pneumophila gene associated with macrophage infectivity. 1989 Infect Immun 57 1263-70
Ludwig B Characterization of Mip proteins of Legionella pneumophila. 1994 FEMS Microbiol Lett 118 23-30
Hacker J Analysis of virulence factors of Legionella pneumophila. 1993 Zentralbl Bakteriol 278 348-58
Riboldi-Tunnicliffe A Crystal structure of Mip, a prolylisomerase from Legionella pneumophila. 2001 Nat Struct Biol 8 779-83



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)