Abstract
The Bordetella genus is divided into two groups: classical and non-classical. Bordetella pertussis, Bordetella bronchiseptica and Bordetella parapertussis are known as classical bordetellae, a group of important human pathogens causing whooping cough or whooping cough-like disease and hypothesized to have evolved from environmental non-classical bordetellae. Bordetella infections have increased globally driving the need to better understand these pathogens for the development of new treatments and vaccines. One unexplored component in Bordetella is the role of serine, threonine and tyrosine phosphorylation. Therefore, this study characterized the phosphoproteome of classical bordetellae and examined its potential role in Bordetella biology and virulence. Applying strict identification of localization criteria, this study identified 70 unique phosphorylated proteins in the classical bordetellae group with a high degree of conservation. Phosphorylation was a key regulator of Bordetella metabolism with proteins involved in gluconeogenesis, TCA cycle, amino acid and nucleotide synthesis significantly enriched. Three key virulence pathways were also phosphorylated including type III secretion system, alcaligin synthesis and the BvgAS master transcriptional regulatory system for virulence genes in Bordetella. Seven new phosphosites were identified in BvgA with 6 located in the DNA binding domain. Of the 7, 4 were not present in non-classical bordetellae. This suggests that serine/threonine phosphorylation may play an important role in stabilizing/destabilizing BvgA binding to DNA for fine-tuning of virulence gene expression and that BvgA phosphorylation may be an important factor separating classical from non-classical bordetellae. This study provides the first insight into the phosphoproteome of classical Bordetella species and the role that Ser/Thr/Tyr phosphorylation may play in Bordetella biology and virulence.
Highlights
The genus Bordetella contains both environmental Gramnegative bacterial species and human pathogens (Gross et al, 2008)
Of the 54 phosphosites, 72% were located on serine residues, 17% were on threonine and 11% were on tyrosine
In B. parapertussis, we identified 50 phosphosites from 50 phosphopeptides and 42 proteins (1% of total proteins in the genome) with the distribution being 80% pSer, 12% pThr and 8% pTyr (Supplementary Table 2)
Summary
The genus Bordetella contains both environmental Gramnegative bacterial species and human pathogens (Gross et al, 2008). Bordetella pertussis together with Bordetella bronchiseptica and Bordetella parapertussis, make up the classical bordetellae group which causes respiratory disease in mammals while non-classical bordetellae species include environmental (Bordetella petrii), avian (Bordetella avium and Bordetella hinzii) and opportunistic human pathogens (Bordetella holmseii, Bordetella trematum and Bordetella ansorpii). Of the three classical species, B. bronchiseptica is the ancestral species to B. pertussis and B. parapertussis (Diavatopoulos et al, 2005). It can survive in the environment and infects a broad range of mammals including dogs, pigs, cats, rabbits and humans (Mattoo and Cherry, 2005). B. pertussis is responsible for whooping cough (pertussis), a severe, human respiratory disease while B. parapertussis contains a human specific lineage which causes pertussis-like disease and an ovine specific lineage which causes pneumonia in sheep (Diavatopoulos et al, 2005)
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