| Literature DB >> 25156738 |
Carlos Rumbo1, María Tomás2, Esteban Fernández Moreira1, Nelson Cruz Soares1, Micaela Carvajal3, Elena Santillana4, Alejandro Beceiro1, Antonio Romero4, Germán Bou2.
Abstract
Acinetobacter baumannii is an extracellular opportunistic human pathogen that is becoming increasingly problematic in hospitals. In the present study, we demonstrate that the A. baumannii Omp 33- to 36-kDa protein (Omp33-36) is a porin that acts as a channel for the passage of water. The protein is found on the cell surface and is released along with other porins in the outer membrane vesicles (OMVs). In immune and connective cell tissue, this protein induced apoptosis by activation of caspases and modulation of autophagy, with the consequent accumulation of p62/SQSTM1 (sequestosome 1) and LC3B-II (confirmed by use of autophagy inhibitors). Blockage of autophagy enables the bacterium to persist intracellularly (inside autophagosomes), with the subsequent development of cytotoxicity. Finally, we used macrophages and a mouse model of systemic infection to confirm that Omp33-36 is a virulence factor in A. baumannii. Overall, the study findings show that Omp33-36 plays an important role in the pathogenesis of A. baumannii infections.Entities:
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Year: 2014 PMID: 25156738 PMCID: PMC4249306 DOI: 10.1128/IAI.02034-14
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441