Comparative Phosphoproteomics of Classical Bordetellae Elucidates the Potential Role of Serine, Threonine and Tyrosine Phosphorylation in Bordetella Biology and Virulence

Frontiers in Cellular and Infection Microbiology

Ling Zhong¹  Mark J. Raftery¹  Laurence Don Wai Luu²  Sandeep Kaur²  Ruiting Lan² 

[1] Bioanalytical Mass Spectrometry Facility, University of New South Wales, Sydney, NSW, Australia;School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW, Australia;

关键词: Bordetella pertussis;    Bordetella;    phosphoproteomics;    BvgA;    protein phosphorylation;    Bordetella parapertussis;    Bordetella bronchiseptica;    serine/threonine/tyrosine kinase;   

DOI  :  10.3389/fcimb.2021.660280

来源: Frontiers

【 摘 要 】

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.

【 授权许可】

CC BY