6sb5

Structural highlights

Function

[MPEG1_MOUSE] Plays a key role in the innate immune response following bacterial infection by polymerizing and inserting into the bacterial surface to form pores (PubMed:26402460). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (PubMed:30249808). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23257510, PubMed:23753625, PubMed:26402460). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (PubMed:26831467). Required for the antibacterial activity of reactive oxygen species and nitric oxide (PubMed:26402460).^{[1] [2] [3] [4] [5]}

References

1. ↑ McCormack R, de Armas LR, Shiratsuchi M, Ramos JE, Podack ER. Inhibition of intracellular bacterial replication in fibroblasts is dependent on the perforin-like protein (perforin-2) encoded by macrophage-expressed gene 1. J Innate Immun. 2013;5(2):185-94. doi: 10.1159/000345249. Epub 2012 Dec 15. PMID:23257510 doi:http://dx.doi.org/10.1159/000345249
2. ↑ Fields KA, McCormack R, de Armas LR, Podack ER. Perforin-2 restricts growth of Chlamydia trachomatis in macrophages. Infect Immun. 2013 Aug;81(8):3045-54. doi: 10.1128/IAI.00497-13. Epub 2013 Jun, 10. PMID:23753625 doi:http://dx.doi.org/10.1128/IAI.00497-13
3. ↑ McCormack RM, de Armas LR, Shiratsuchi M, Fiorentino DG, Olsson ML, Lichtenheld MG, Morales A, Lyapichev K, Gonzalez LE, Strbo N, Sukumar N, Stojadinovic O, Plano GV, Munson GP, Tomic-Canic M, Kirsner RS, Russell DG, Podack ER. Perforin-2 is essential for intracellular defense of parenchymal cells and phagocytes against pathogenic bacteria. Elife. 2015 Sep 24;4. doi: 10.7554/eLife.06508. PMID:26402460 doi:http://dx.doi.org/10.7554/eLife.06508
4. ↑ McCormack R, Bahnan W, Shrestha N, Boucher J, Barreto M, Barrera CM, Dauer EA, Freitag NE, Khan WN, Podack ER, Schesser K. Perforin-2 Protects Host Cells and Mice by Restricting the Vacuole to Cytosol Transitioning of a Bacterial Pathogen. Infect Immun. 2016 Mar 24;84(4):1083-1091. doi: 10.1128/IAI.01434-15. Print 2016 , Apr. PMID:26831467 doi:http://dx.doi.org/10.1128/IAI.01434-15
5. ↑ Bai F, McCormack RM, Hower S, Plano GV, Lichtenheld MG, Munson GP. Perforin-2 Breaches the Envelope of Phagocytosed Bacteria Allowing Antimicrobial Effectors Access to Intracellular Targets. J Immunol. 2018 Nov 1;201(9):2710-2720. doi: 10.4049/jimmunol.1800365. Epub 2018 , Sep 24. PMID:30249808 doi:http://dx.doi.org/10.4049/jimmunol.1800365