Pathogenic Acinetobacter species have a functional type I secretion system and contact-dependent inhibition systems

Harding, CM; Pulido, MR; Di Venanzio, G; Kinsella, RL; Webb, AI; Scott, NE; Pachon, J; Feldman, MF

Author(s): Harding, CM; Pulido, MR; Di Venanzio, G; Kinsella, RL; Webb, AI; Scott, NE; Pachon, J; Feldman, MF;
Details: Publication Year 2017-04-03,Volume 292,Issue #22,Page 9075-9087
Journal Title: Journal of Biological Chemistry
Publication Type: Journal Article
Abstract: Pathogenic Acinetobacter species, including A. baumannii and A. nosocomialis, are opportunistic human pathogens of increasing relevance worldwide. Although their mechanisms of drug resistance are well studied, the virulence factors that govern Acinetobacter pathogenesis are incompletely characterized. Here we define the complete secretome of A. nosocomialis strain M2 in minimal media and demonstrate that pathogenic Acinetobacter species produce both a functional type I secretion system (T1SS) and a contact dependent inhibition (CDI) system. Using bioinformatics, quantitative proteomics, and mutational analyses we show that Acinetobacter uses its T1SS for exporting two putative T1SS effectors, an RTX-Serralysin-like toxin and the biofilm associated protein (Bap). Moreover, we found that mutation of any component of the T1SS system abrogated type VI secretion activity under nutrient-limited conditions, indicating a previously unrecognized crosstalk between these two systems. We also demonstrate that the Acinetobacter T1SS is required for biofilm formation. Lastly, we show that both A. nosocomialis and A. baumannii produce functioning CDI systems that mediate growth inhibition of sister cells lacking the cognate immunity protein. The Acinetobacter CDI systems are widely distributed across pathogenic Acinetobacter species, with many A. baumannii isolates harboring two distinct CDI systems. Collectively, these data demonstrate the power of differential, quantitative proteomics approaches to study secreted proteins, define the role of previously uncharacterized protein export systems, and observe crosstalk between secretion systems in the pathobiology of medically relevant Acinetobacter The data are available via ProteomeXchange with identifier PXD005881.
Publisher: ASBMB
Research Division(s): Systems Biology And Personalised Medicine
PubMed ID: 28373284
Publisher's Version: https://doi.org/10.1074/jbc.M117.781575
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2017-05-02 03:01:26

Last Modified: 2018-07-06 11:05:05