Dataset Information


Thioredoxin Modulates Cell Surface Hydrophobicity in Acinetobacter baumannii.

ABSTRACT: Acinetobacter baumannii, a Gram-negative coccobacillus, has become a prevalent nosocomial health threat affecting the majority of hospitals both in the U.S. and around the globe. Microbial cell surface hydrophobicity (CSH) has previously been correlated with virulence, uptake by immune cells, and attachment to epithelial cells. A mutant strain of A. baumannii (?trxA) lacking the redox protein thioredoxin A was found to be more hydrophobic than its wild type (WT) and complemented counterparts, as measured by both Microbial Adhesion to Hydrocarbon (MATH) and salt aggregation. The hydrophobicity of the mutant could be abrogated through treatment with sodium cyanoborohydride (SCBH). This modulation correlated with reduction of disulfide bonds, as SCBH was able to reduce 5,5'-dithio-bis-[2-nitrobenzoic acid] and treatment with the known disulfide reducer, ?-mercaptoethanol, also decreased ?trxA CSH. Additionally, the ?trxA mutant was more readily taken up than WT by J774 macrophages and this differential uptake could be abrogated though SCBH treatment. When partitioned into aqueous and hydrophobic phases, ?trxA recovered from the hydrophobic partition was phagocytosed more readily than from the aqueous phase further supporting the contribution of CSH to A. baumannii uptake by phagocytes. A second Gram-negative bacterium, Francisella novicida, also showed the association of TrxA deficiency (Fn?trxA) with increased hydrophobicity and uptake by J774 cells. We previously have demonstrated that modification of the type IV pilus system (T4P) was associated with the A. baumannii ?trxA phenotype, and the Francisella Fn?trxA mutant also was found to have a marked T4P deficiency. Interestingly, a F. novicida mutant lacking pilT also showed increased hydrophobicity over FnWT. Collective evidence presented in this study suggests that Gram-negative bacterial thioredoxin mediates CSH through multiple mechanisms including disulfide-bond reduction and T4P modulation.


PROVIDER: S-EPMC6927278 | BioStudies | 2019-01-01

REPOSITORIES: biostudies

Similar Datasets

2018-01-01 | S-EPMC6050963 | BioStudies
2010-01-01 | S-EPMC2912274 | BioStudies
2019-01-01 | S-EPMC6605650 | BioStudies
2008-01-01 | S-EPMC2896474 | BioStudies
2017-01-01 | S-EPMC5487381 | BioStudies
2005-01-01 | S-EPMC1087808 | BioStudies
2019-01-01 | S-EPMC6436345 | BioStudies
2004-01-01 | S-EPMC305758 | BioStudies
2013-01-01 | S-EPMC3658162 | BioStudies
2016-01-01 | S-EPMC4938169 | BioStudies