+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

A Burkholderia pseudomallei macrophage infectivity potentiator-like protein has rapamycin-inhibitable peptidylprolyl isomerase activity and pleiotropic effects on virulence



A Burkholderia pseudomallei macrophage infectivity potentiator-like protein has rapamycin-inhibitable peptidylprolyl isomerase activity and pleiotropic effects on virulence



Infection and Immunity 79(11): 4299-4307



Macrophage infectivity potentiators (Mips) are a group of virulence factors encoded by pathogenic bacteria such as Legionella, Chlamydia, and Neisseria species. Mips are part of the FK506-binding protein (FKBP) family, whose members typically exhibit peptidylprolyl cis-trans isomerase (PPIase) activity which is inhibitable by the immunosuppressants FK506 and rapamycin. Here we describe the identification and characterization of BPSS1823, a Mip-like protein in the intracellular pathogen Burkholderia pseudomallei. Recombinant BPSS1823 protein has rapamycin-inhibitable PPIase activity, indicating that it is a functional FKBP. A mutant strain generated by deletion of BPSS1823 in B. pseudomallei exhibited a reduced ability to survive within cells and significant attenuation in vivo, suggesting that BPSS1823 is important for B. pseudomallei virulence. In addition, pleiotropic effects were observed with a reduction in virulence mechanisms, including resistance to host killing mechanisms, swarming motility, and protease production.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 036231703

Download citation: RISBibTeXText

PMID: 21859853

DOI: 10.1128/iai.00134-11


Related references

Development, synthesis and structure-activity-relationships of inhibitors of the macrophage infectivity potentiator (Mip) proteins of Legionella pneumophila and Burkholderia pseudomallei. Bioorganic and Medicinal Chemistry 24(21): 5134-5147, 2016

A novel FK-506-binding-like protein that lacks peptidyl-prolyl isomerase activity is involved in intracellular infection and in vivo virulence of Burkholderia pseudomallei. Microbiology 157(Pt 9): 2629-2638, 2011

A novel FK-56-binding-like protein that lacks peptidyl-prolyl isomerase activity is involved in intracellular infection and in vivo virulence of Burkholderia pseudomallei. Microbiology 157(9): 2629-2638, 2011

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. 7(5): 777-783, 1993

Toxoplasma gondii expresses two cyclophilins cyps with cyclosporin a inhibitable peptidylprolyl isomerase ppiase activity. Program & Abstracts of the Interscience Conference on Antimicrobial Agents & Chemotherapy 32: 165, 1992

Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila. Infection and Immunity 71(8): 4389-4397, 2003

Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolyl cis/trans isomerase (PPIase) proteins. Expert Review of Vaccines 14(12): 1633-1649, 2015

In silico analysis of conformational changes induced by normal and mutation of macrophage infectivity potentiator catalytic residues and its interactions with Rapamycin. Interdisciplinary Sciences Computational Life Sciences 2015:, 2015

In Silico Analysis of Conformational Changes Induced by Normal and Mutation of Macrophage Infectivity Potentiator Catalytic Residues and its Interactions with Rapamycin. Interdisciplinary Sciences Computational Life Sciences 7(3): 326-333, 2015

Liposomes or traditional adjuvants: induction of bactericidal activity by the macrophage infectivity potentiator protein (Mip) of Neisseria meningitidis. Apmis 125(8): 725-731, 2017

Backbone chemical shift assignment of macrophage infectivity potentiator virulence factor of Trypanosoma cruzi. Biomolecular Nmr Assignments 13(1): 21-25, 2019

Trehalase plays a role in macrophage colonization and virulence of Burkholderia pseudomallei in insect and mammalian hosts. Virulence 8(1): 30-40, 2017

The Neisseria meningitidis macrophage infectivity potentiator protein induces cross-strain serum bactericidal activity and is a potential serogroup B vaccine candidate. Infection and Immunity 79(9): 3784-3791, 2011

Antibodies are generated during infection to Coxiella burnetii macrophage infectivity potentiator protein (Cb-Mip). Microbiology and Immunology 41(4): 371-376, 1997

Macrophage-lymphocyte interactions mediate anti-Burkholderia pseudomallei activity. Fems Immunology & Medical Microbiology. 21(4): 283-286,., 1998