Abstract
Cytochrome P450s are b-heme-containing enzymes that are able to introduce oxygen atoms into a wide variety of organic substrates. They are extremely widespread in nature having diverse functions at both biochemical and physiological level. The genome of C. jejuni 81-176 encodes a single cytochrome P450 (Cj1411c) that has no close homologues. Cj1411c is unusual in its genomic location within a cluster involved in the biosynthesis of outer surface structures. Here we show that E. coli expressed and affinity-purified C. jejuni cytochrome P450 is lipophilic, containing one equivalent Cys-ligated heme. Immunoblotting confirmed the association of cytochrome P450 with membrane fractions. A Cj1411c deletion mutant had significantly reduced ability to infect human cells and was less able to survive following exposure to human serum when compared to the wild type strain. Phenotypically following staining with Alcian blue, we show that a Cj1411c deletion mutant produces significantly less capsular polysaccharide. This study describes the first known membrane-bound bacterial cytochrome P450 and its involvement in Campylobacter virulence.
Highlights
During the past few decades Campylobacter has been identified as the most common cause of bacterial diarrheal illness in the European Union and worldwide [1]
Escherichia. coli, for example, has no cytochrome P450 encoded in its genome, whereas Mycobacterium tuberculosis contains twenty and Streptococcus coelicolor eighteen P450 cytochromes [7]
In this study we show that CYP1411c is a membranebound cytochrome P450, that when mutated significantly impairs C. jejuni 81-176 pathogenicity
Summary
During the past few decades Campylobacter has been identified as the most common cause of bacterial diarrheal illness in the European Union and worldwide [1] This pathogen is responsible, in some patients, for severe neurological diseases including Guillain-Barré syndrome [2]. Cytochromes P450s are a superfamily of proteins with a maximum absorption at 450 nm and are characterized by the presence of a conserved Cys residue [5]. This cysteine distinguishes cytochrome P450s from other oxygen activating enzymes such as globins and peroxidases that utilize histidine during the reaction with hydroperoxide [6]. The genome of C. jejuni 81-176 encodes a single cytochrome P450, Cj1411c (CYP1411c)
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