PXD022419-1

PXD022419 is an original dataset announced via ProteomeXchange.

Title	Dissecting the molecular diversity and commonality of bovine and human treponemes identifies key survival and adhesion mechanisms
Description	Here, we report the first complete genomes of three cultivable treponeme species from bovine digital dermatitis (DD) skin lesions, two comparative human treponemes and a bovine gastrointestinal (GI) isolate. Key genomic differences between bovine and human treponemes implicate microbial mechanisms that enhance knowledge of how DD, a severe disease of ruminants, has emerged into a prolific and endemic disease in countries worldwide. Bovine DD treponemes have additional oxidative stress genes compared to nearest human-isolated relatives, suggesting better toleration of oxidative stress, and thus potentially explaining the ability of bovine strains to colonize skin surfaces. Comparison of bovine DD and GI treponemes as well as bovine pathogenic and human non-pathogenic saprophyte Treponema phagedenis strains indicates genes encoding a five-enzyme biosynthetic pathway for the production of 2,3-diacetamido-2,3-dideoxy-d-mannuronic acid, a rare di-N-acetylated mannuronic acid sugar with potential immunomodulatory activity, as important for pathogenesis. The bovine T. phagedenis strains further differed from human strains by having a larger number of unique genetic features including components of a type IV secretion system and a phosphate utilisation system including phoU, a gene associated with enhanced osmotic stress survival. Proteomic analyses confirmed bovine derived T. phagedenis exhibits expression of PhoU but not the putative secretion system whilst the novel mannuronic acid pathway was expressed in near entirety across the DD treponemes. Analysis of osmotic stress response in water identified a difference between bovine and human T. phagedenis with bovine strains surviving better. This novel mechanism could enable a selective advantage, allowing environmental persistence and transmission of bovine T. phagedenis. Finally, we investigated a range of treponeme genes encoding ortholog families across the DD treponemes representing putative outer membrane proteins (OMPs) and identified several families as multi-specific adhesins capable of binding extra cellular matrix (ECM) components. Human saprophytic T. phagedenis could not be differentiated from bovine pathogenic strains by these adhesins and only two of ten characterised ortholog OMP families were absent from commensal bovine treponemes. One of these bovine pathogen specific adhesin ortholog families showed considerable diagnostic potential with the Treponema medium representative demonstrating the greatest disease specificity (91.6%). This work has shed light on treponeme host adaptation and has identified candidate molecules for future diagnostics, vaccination and therapeutic intervention.
HostingRepository	PRIDE
AnnounceDate	2021-03-16
AnnouncementXML	Submission_2021-03-16_03:00:43.444.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD022419
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Stuart Armstrong
SpeciesList	scientific name: Treponema ruminis; NCBI TaxID: 744515; scientific name: Treponema pedis; NCBI TaxID: 409322; scientific name: Treponema sp. T19; NCBI TaxID: 744517; scientific name: Treponema phagedenis; NCBI TaxID: 162; scientific name: Treponema sp. T320A; NCBI TaxID: 744518; scientific name: Treponema medium; NCBI TaxID: 58231;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2020-11-09 03:23:48	ID requested
⏵ 1	2021-03-16 03:00:43	announced

Dataset with its publication pending

submitter keyword: Treponemes, bovine digital dermatitis, shotgun LC MSMS

Nicholas Evans
contact affiliation	Senior Lecturer Department of Infection Biology and Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool,
contact email	evansnj@liverpool.ac.uk
lab head
Stuart Armstrong
contact affiliation	Infection Biology
contact email	sarmstro@liv.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD022419
     1. Label: PRIDE project
     2. Name: Dissecting the molecular diversity and commonality of bovine and human treponemes identifies key survival and adhesion mechanisms