Allelic variation of Escherichia coli outer membrane protein A: Impact on cell surface properties, stress tolerance and allele distribution

• Published in: PloS one 2022-10, Vol.17 (10), p.e0276046-e0276046
• Main Authors: Liao, Chunyu, Santoscoy, Miguel C, Craft, Julia, Anderson, Chiron, Soupir, Michelle L, Jarboe, Laura R
• Format: Article
• Language: English
• Subjects: Acetic acid; Alleles; Amino acids; Analysis; Bacteria; Biofilms; Biology and Life Sciences; Cell surface; Dimerization; E coli; Elastase; Escherichia coli; Gram-negative bacteria; Growth rate; Hydrophobicity; Leukocytes (neutrophilic); Medicine and Health Sciences; Membrane proteins; Membranes; Outer membrane proteins; Peptides; Phenotypes; Physical Sciences; Properties; Protein A; Proteins; Relative abundance; Research and Analysis Methods; Surface charge; Surface properties; Variation; Zeta potential
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0276046

Outer membrane protein A (OmpA) is one of the most abundant outer membrane proteins of Gram-negative bacteria and is known to have patterns of sequence variations at certain amino acids-allelic variation-in Escherichia coli. Here we subjected seven exemplar OmpA alleles expressed in a K-12 (MG1655) [DELTA]ompA background to further characterization. These alleles were observed to significantly impact cell surface charge (zeta potential), cell surface hydrophobicity, biofilm formation, sensitivity to killing by neutrophil elastase, and specific growth rate at 42°C and in the presence of acetate, demonstrating that OmpA is an attractive target for engineering cell surface properties and industrial phenotypes. It was also observed that cell surface charge and biofilm formation both significantly correlate with cell surface hydrophobicity, a cell property that is increasingly intriguing for bioproduction. While there was poor alignment between the observed experimental values relative to the known sequence variation, differences in hydrophobicity and biofilm formation did correspond to the identity of residue 203 (N vs T), located within the proposed dimerization domain. The relative abundance of the (I, [delta]) allele was increased in extraintestinal pathogenic E. coli (ExPEC) isolates relative to environmental isolates, with a corresponding decrease in (I, [alpha]) alleles in ExPEC relative to environmental isolates. The (I, [alpha]) and (I, [delta]) alleles differ at positions 203 and 251. Variations in distribution were also observed among ExPEC types and phylotypes. Thus, OmpA allelic variation and its influence on OmpA function warrant further investigation.