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

Publisher: MDPI Country of Publication: Switzerland NLM ID: 100964009 Publication Model: Electronic Cited Medium: Internet ISSN: 1420-3049 (Electronic) Linking ISSN: 14203049 NLM ISO Abbreviation: Molecules Subsets: MEDLINE

Original Publication: Basel, Switzerland : MDPI, c1995-

Mutation*; Acinetobacter baumannii/*pathogenicity ; Bacterial Outer Membrane Proteins/*metabolism ; Peptidoglycan/*metabolism; Acinetobacter baumannii/genetics ; Asparagine/genetics ; Bacterial Adhesion ; Bacterial Outer Membrane Proteins/chemistry ; Bacterial Outer Membrane Proteins/genetics ; Biofilms ; Protein Domains ; Virulence

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 Ab 169 , on its virulence characteristics by complementing the Δ ompA mutant with the plasmid-borne ompA D268A allele. We show that while restoring the impaired biofilm formation of the Δ ompA strain, the Ab 169 ompA D268A mutant tended to form bacterial filaments, indicating the abnormalities in cell division. Moreover, the Ab 169 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.

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09.3.3.-LMT-K-712-10-0095 Lietuvos Mokslo Taryba

Keywords: Acinetobacter baumannii; OmpA; outer membrane vesicles; peptidoglycan; virulence; β-lactams

0 (Bacterial Outer Membrane Proteins)
0 (Peptidoglycan)
149024-69-1 (OMPA outer membrane proteins)
7006-34-0 (Asparagine)

Date Created: 20190525 Date Completed: 20191125 Latest Revision: 20200225

20250114

PMC6572160

10.3390/molecules24101972

31121924