Ng‐MIP, a surface‐exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl‐prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages
作者： Rosanna Leuzzi , Laura Serino , Maria Scarselli , Silvana Savino , Maria Rita Fontana
DOI: 10.1111/J.1365-2958.2005.04859.X
关键词:
摘要: Summary Macrophage infectivity potentiators (MIPs) are a family of surface-exposed virulence factors intracellular microorganisms such as Legionella , Chlamydia and Trypanosoma . These proteins display peptidylprolyl cis / trans isomerase (PPIase) activity that is inhibited by immunosuppressants FK506 rapamycin. Here we describe the identification characterization in Neisseria gonorrhoeae Ng-MIP, lipoprotein with high homology to MIPs. The protein an homodimer rapamycininhibited PPIase confirming it functional member MIP family. A knock-out strain, generated deletion mip gene N. F62 was evaluated for its role infection mouse human macrophages. We show Ng-MIP promotes survival macrophages, highlighting possible this promoting persistence gonococcal infection.
unirioja.es
core.ac.uk 
sci-hub.se 参考文章(28)
Angelika R. Kraft, Markus F. Templin, Joachim-Volker Höltje, Membrane-bound lytic endotransglycosylase in Escherichia coli. Journal of Bacteriology. ,vol. 180, pp. 3441- 3447 ,(1998) , 10.1128/JB.180.13.3441-3447.1998
Alan Riboldi-Tunnicliffe, Bettina König, Sven Jessen, Manfred S. Weiss, Jens Rahfeld, Jörg Hacker, Gunter Fischer, Rolf Hilgenfeld, Crystal structure of Mip, a prolylisomerase from Legionella pneumophila Nature Structural & Molecular Biology. ,vol. 8, pp. 779- 783 ,(2001) , 10.1038/NSB0901-779
B Knepper, I Heuer, T F Meyer, J P van Putten, Differential response of human monocytes to Neisseria gonorrhoeae variants expressing pili and opacity proteins Infection and Immunity. ,vol. 65, pp. 4122- 4129 ,(1997) , 10.1128/IAI.65.10.4122-4129.1997
Anker G. Lundemose, John E. Kay, John H. Pearce, Chlamydia trachomatis Mip-like protein has peptidylprolyl cis/trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection Molecular Microbiology. ,vol. 7, pp. 777- 783 ,(1993) , 10.1111/J.1365-2958.1993.TB01168.X
Jörg Hacker, Gunter Fischer, Immunophilins: structure-function relationship and possible role in microbial pathogenicity. Molecular Microbiology. ,vol. 10, pp. 445- 456 ,(1993) , 10.1111/J.1365-2958.1993.TB00917.X
N. P. Cianciotto, B. S. Fields, Legionella pneumophila mip gene potentiates intracellular infection of protozoa and human macrophages. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 89, pp. 5188- 5191 ,(1992) , 10.1073/PNAS.89.11.5188
S. Schreiber, Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science. ,vol. 251, pp. 283- 287 ,(1991) , 10.1126/SCIENCE.1702904
Nicholas P. Cianciotto, William O'Connell, Gregory A. Dasch, Louis P. Mallavia, Detection of mip -like sequences and mip-related proteins within the family Rickettsiaceae Current Microbiology. ,vol. 30, pp. 149- 153 ,(1995) , 10.1007/BF00296200
David E. Soper, Pelvic Inflammatory Disease (PID) Infectious Diseases in Obstetrics & Gynecology. ,vol. 4, pp. 62- 62 ,(1996) , 10.1155/S1064744996000130
Nicholas P. Cianciotto, Julie Kim Stamos, David W. Kamp, Infectivity of Legionella pneumophila mip mutant for alveolar epithelial cells Current Microbiology. ,vol. 30, pp. 247- 250 ,(1995) , 10.1007/BF00293641