Publication Details

Category Text Publication
Reference Category Journals
DOI 10.1128/mSystems.01175-20
Licence creative commons licence
Title (Primary) New provisional function of OmpA from Acinetobacter sp. strain SA01 based on environmental challenges
Author Shahryari, S.; Talaee, M.; Haghbeen, K.; Adrian, L.; Vali, H.; Shahbani Zahiri, H.; Noghabi, K.A.
Journal mSystems
Year 2021
Department UBT
Volume 6
Issue 1
Page From e01175-20
Language englisch
Topic T7 Bioeconomy
Keywords Acinetobacter sp. SA01 phenol OmpA emulsifying ability porin oxidative stress outer membrane vesicle (OMV)
UFZ wide themes ProVIS;
Abstract An outer membrane protein A (OmpA) from Acinetobacter sp. strain SA01 was identified and characterized in-depth based on the structural and functional characteristics already known of its homologues. In silico structural studies showed that this protein can be a slow porin, binds to peptidoglycan, and exhibits emulsifying properties. Characterization of the recombinant SA01-OmpA, based on its emulsifying properties, represented its promising potentials in biotechnology. Also, the presence of SA01-OmpA in outer membrane vesicles (OMV) and biofilm showed that this protein, like its homologues in Acinetobacter baumannii, can be secreted into the extracellular environment through OMVs and play a role in the formation of biofilm. After ensuring the correct selection of the protein of interest, the role of oxidative stress induced by cell nutritional parameters (utilization of specific carbon sources) on the expression level of OmpA was carefully studied. For this purpose, the oxidative stress level of SA01 cell cultures in the presence of three nonrelevant carbon sources (sodium acetate, ethanol, and phenol) was examined under each condition. High expression of SA01-OmpA in ethanol- and phenol-fed cells with higher levels of oxidative stress than acetate suggested that oxidative stress could be a substantial factor in the regulation of SA01-OmpA expression. The significant association of SA01-OmpA expression with the levels of oxidative stress induced by cadmium and H2O2, with oxidative stress-inducing properties and lack of nutritional value, confirmed that the cells tend to harness their capacities with a possible increase in OmpA production. Collectively, this study suggests a homeostasis role for OmpA in Acinetobacter sp. SA01 under oxidative stress besides assuming many other roles hitherto attributed to this protein.
Persistent UFZ Identifier
Shahryari, S., Talaee, M., Haghbeen, K., Adrian, L., Vali, H., Shahbani Zahiri, H., Noghabi, K.A. (2021):
New provisional function of OmpA from Acinetobacter sp. strain SA01 based on environmental challenges
mSystems 6 (1), e01175-20