Dataset Information

Human plasma proteins detected by HPLC-MS/MS after blood incubation with E. coli treated/not treated with mucin

ABSTRACT: Whole human blood incubated with E. coli isolate with or without bound mucin. Plasma was obtained and the effect of mucin bound to E. coli on plasma proteins content was analysed by HPLC-MS-MS.

INSTRUMENT(S): maXis

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Daria Rakitina

LAB HEAD: Gleb Yurievich Fisunov

PROVIDER: PXD010496 | Pride | 2019-12-16

REPOSITORIES: pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	PLASMAfileslist.txt	Txt
	a466-468-F032394.mzid.gz	Mzid
	a466-468-F032394.pride.mztab.gz	Mztab
	a466-468-mascot_daemon_merge.mgf	Mgf
	a466-468-mascot_daemon_merge.mgf.export.F032394.csv	Mgf

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Publications

Mucin adsorbed by E. coli can affect neutrophil activation in vitro.

Mikhalchik Elena E Balabushevich Nadezhda N Vakhrusheva Tatiana T Sokolov Alexey A Baykova Julia J Rakitina Daria D Scherbakov Petr P Gusev Sergey S Gusev Alexander A Kharaeva Zaira Z Bukato Olga O Pobeguts Olga O

FEBS open bio 20191219 2

Bacteria colonizing human intestine adhere to the gut mucosa and avoid the innate immune system. We previously demonstrated that Escherichia coli isolates can adsorb mucin from a diluted solution in vitro. Here, we evaluated the effect of mucin adsorption by E. coli cells on neutrophil activation in vitro. Activation was evaluated based on the detection of reactive oxygen species production by a chemiluminescent reaction (ChL), observation of morphological alterations in neutrophils and detectio ...[more]

PMID: 31785127

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Project description:In actinomycetes, antibiotic production is often associated with a morpho-physiological differentiation program that is regulated by complex molecular and metabolic networks. Many aspects of these regulatory circuits have been already elucidated and many others still deserve further investigations. In this regard, the possible role of many small open-reading frames(smORFs) in actinomycete morpho-physiological differentiation is still elusive. In Streptomyces coelicolor, inactivation of the smORF trpM (SCO2038) - whose product modulates L-tryptophan metabolism - impairs production of antibiotics and morphological differentiation. Indeed, it was demonstrated that TrpM is able to interact with PepA (SCO2179), a putative cytosol aminopeptidase playing a key role in antibiotic production and sporulation. In this work, a S. coelicolor trpM knock-in (Sco-trpMKI) mutant strain was generated by cloning trpM into overexpressing vector to further investigate the role of trpM in actinomycete growth and morpho-physiological differentiation. Results highlighted that trpM: i) stimulates growth and actinorhodin production; ii) decreases calcium-dependent antibiotic production; iii) has no effect on undecylprodigiosin production. Metabolic pathways influenced by trpM knock-in were investigated by combining two-difference in gel electrophoresis/nanoliquid chromatography coupled to electrospray linear ion trap tandem mass spectrometry (2D-DIGE/nanoLC-ESI-LIT- MS/MS) and by LC-ESI-MS/MS procedures, respectively. These analyses demonstrated that over-expression of trpM causes an over-representation of factors involved in protein synthesis and nucleotide metabolism as well as a down-representation of proteins involved in central carbon and amino acid metabolism. At the metabolic level, this corresponded to a differential accumulation pattern of different amino acids - including aromatic ones but tryptophan – and central carbon intermediates. PepA was also down-represented in Sco-trpMKI. The latter was produced as recombinant His- tagged protein and was originally proven having the predicted aminopeptidase activity. Altogether, these results highlight the stimulatory effect of trpM in S. coelicolor growth and actinorhodin biosynthesis, which are elicited through the modulation of various metabolic pathways and PepA representation, further confirming the complexity of regulatory networks that control antibiotic production in actinomycetes.