Cj1388 Is a RidA Homolog and Is Required for Flagella Biosynthesis and/or Function in Campylobacter jejuni.

Jessica Irons,Christine M Szymanski,Diana M Downs,Jessica C Sacher

doi:10.3389/fmicb.2019.02058

Jessica Irons, Christine M Szymanski + Show 2 more

Open Access

https://doi.org/10.3389/fmicb.2019.02058

Copy DOI

Abstract

Campylobacter jejuni is the leading bacterial cause of acute gastroenteritis worldwide and thus significant to public health. C. jejuni primarily lives in the gastrointestinal tracts of poultry and can contaminate meat during processing. Despite a small genome, the metabolic plasticity of C. jejuni allows proliferation in chicken ceca and mammalian host intestines, and survival in environments with a variety of temperatures, pH, osmotic conditions, and nutrient availabilities. The exact mechanism of C. jejuni infection is unknown, however, virulence requires motility. Our data suggest the C. jejuni RidA homolog, Cj1388, plays a role in flagellar biosynthesis, regulation, structure, and/or function and, as such is expected to influence virulence of the organism. Mutants lacking cj1388 have defects in motility, autoagglutination, and phage infectivity under the conditions tested. Comparison to the RidA paradigm from Salmonella enterica indicates the phenotypes of the C. jejuni cj1388 mutant are likely due to the inhibition of one or more pyridoxal 5′-phosphate-dependent enzymes by the reactive enamine 2-aminoacrylate.

Highlights

IntroductionThe Rid/YER057c/UK114 protein superfamily (COG0251) is broadly conserved throughout all domains of life (Kim et al, 2001; Leitner-Dagan et al, 2006; Lambrecht et al, 2012, 2013; Downs and Ernst, 2015; Niehaus et al, 2015; ElRamlawy et al, 2016)
A S. enterica ridA mutant fails to grow on minimal medium with serine due to the accumulation of 2AA that is generated by the biosynthetic serine/threonine dehydratase encoded by ilvA (EC 4.3.1.19) (Schmitz and Downs, 2004; Lambrecht et al, 2013)
A S. enterica ridA mutant was transformed with pBAD24 constructs harboring a gene encoding Rid proteins from C. jejuni, the S. enterica ridA under the control of an arabinose promoter, or an empty vector control

Summary

Introduction

The Rid/YER057c/UK114 protein superfamily (COG0251) is broadly conserved throughout all domains of life (Kim et al, 2001; Leitner-Dagan et al, 2006; Lambrecht et al, 2012, 2013; Downs and Ernst, 2015; Niehaus et al, 2015; ElRamlawy et al, 2016). The RidA, reactive intermediate deaminase A, of S. enterica was found to be an enamine deaminase, and multiple homologs from the three domains of life have similar activity (Lambrecht et al, 2010; Lambrecht et al, 2012; Niehaus et al, 2015; ElRamlawy et al, 2016; Ernst and Downs, 2018). A cellular role for RidA involves quenching the reactive metabolite 2-aminoacrylate (2AA) to prevent damage to specific pyridoxal 5 -phosphate (PLP)-dependent enzymes

Methods

Results

Conclusion