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The Mutation of Conservative Asp268 Residue in the Peptidoglycan-Associated Domain of the OmpA Protein Affects Multiple Acinetobacter baumannii Virulence Characteristics

1
Institute of Biosciences, Life Sciences Center, Vilnius University, Saulėtekio ave. 7, LT-10257 Vilnius, Lithuania
2
Micalis Institute, INRA, AgroParisTech, Université Paris-Saclay, 78350 Jouy-en-Josas, France
*
Author to whom correspondence should be addressed.
Molecules 2019, 24(10), 1972; https://doi.org/10.3390/molecules24101972
Received: 16 April 2019 / Revised: 7 May 2019 / Accepted: 20 May 2019 / Published: 22 May 2019
(This article belongs to the Section Chemical Biology)
Acinetobacter baumannii is a nosocomial human pathogen of increasing concern due to its multidrug resistance profile. The outer membrane protein A (OmpA) is an abundant bacterial cell surface component involved in A. baumannii pathogenesis. It has been shown that the C-terminal domain of OmpA is located in the periplasm and non-covalently associates with the peptidoglycan layer via two conserved amino acids, thereby anchoring OmpA to the cell wall. Here, we investigated the role of one of the respective residues, D268 in OmpA of A. baumannii clinical strain Ab169, on its virulence characteristics by complementing the ΔompA mutant with the plasmid-borne ompAD268A allele. We show that while restoring the impaired biofilm formation of the ΔompA strain, the Ab169ompAD268A mutant tended to form bacterial filaments, indicating the abnormalities in cell division. Moreover, the Ab169 OmpA D268-mediated association to peptidoglycan was required for the manifestation of twitching motility, desiccation resistance, serum-induced killing, adhesion to epithelial cells and virulence in a nematode infection model, although it was dispensable for the uptake of β-lactam antibiotics by outer membrane vesicles. Overall, the results of this study demonstrate that the OmpA C-terminal domain-mediated association to peptidoglycan is critical for a number of virulent properties displayed by A. baumannii outside and within the host. View Full-Text
Keywords: Acinetobacter baumannii; OmpA; peptidoglycan; virulence; outer membrane vesicles; β-lactams Acinetobacter baumannii; OmpA; peptidoglycan; virulence; outer membrane vesicles; β-lactams
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Skerniškytė, J.; Karazijaitė, E.; Deschamps, J.; Krasauskas, R.; Briandet, R.; Sužiedėlienė, E. The Mutation of Conservative Asp268 Residue in the Peptidoglycan-Associated Domain of the OmpA Protein Affects Multiple Acinetobacter baumannii Virulence Characteristics. Molecules 2019, 24, 1972.

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