A glimpse into the modulation of post-translational modifications of human-colonizing bacteria

Bastos, Paulo; Costa, João Pinto da; Vitorino, Rui

doi:10.1016/j.jprot.2016.11.005

Cited by 20 publications

(24 citation statements)

References 281 publications

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“…While 146 examples of protein glycosylation were cited for Francisella and only 111 for Helicobacter pylori (Bastos et al, 2017), the importance of these PTM, observed in Francisella and those induced in the host, is still largely unknown, notably on the outcome of the infectious cycle. Indeed, a large correlation between glycosylation and bacterial pathogenicity has already been proven for various species e.g., Campylobacter jejuni, Legionella and enteropathogenic Escherichia coli (EPEC) (Lu et al, 2015).…”

Section: Resultsmentioning

confidence: 99%

“…This study included the major classes of prokaryotic (i.e., bacterial and archaeal) glycoconjugates without any example on Francisella . Furthermore, in a very recent publication (Bastos et al, 2017), while F. tularensis was shown to exhibit the largest number of glycoproteins in common with M. tuberculosis ( Mtb ), by sharing 16% of its glycoproteome, none of the glycosylated proteins of Francisella , as well as none of the enzymes involved in glycosylation pathway, have been found to play a specific role in pathogenesis. At the opposite, in M. tuberculosis , glycosylation of HbN, a truncated hemoglobin protein, was demonstrated to be necessary for its maintainance at the bacterial membrane and wall (Arya et al, 2013).…”

Section: Role Of Post-translational Modifications (Ptm) On Bacteria/hmentioning

confidence: 99%

“…Of note, Francisella did not belong to the list of prokaryotes that catalyzed glycosylation of host cell proteins (Bastos et al, 2017). In contrast, Legionella was cited as targeting eEF1A through effect of the glucosyl transferase Lgt1, with as result, the killing of eukaryotic cells (Belyi et al, 2008).…”

Section: Role Of Post-translational Modifications (Ptm) On Bacteria/hmentioning

confidence: 99%

“…For example, they may allow interaction of bacterial proteins with host-derived proteins or they may modulate bacteria- and/or host-related events (Bastos et al, 2017). All these events may be essential for bacterial colonization, its survival and the subsequent infection.…”

Section: Introductionmentioning

confidence: 99%

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Role of Glycosylation/Deglycolysation Processes in Francisella tularensis Pathogenesis

Barel

Charbit

2017

Front. Cell. Infect. Microbiol.

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Francisella tularensis is able to invade, survive and replicate inside a variety of cell types. However, in vivo F. tularensis preferentially enters host macrophages where it rapidly escapes to the cytosol to avoid phagosomal stresses and to multiply to high numbers. We previously showed that human monocyte infection by F. tularensis LVS triggered deglycosylation of the glutamine transporter SLC1A5. However, this deglycosylation, specifically induced by Francisella infection, was not restricted to SLC1A5, suggesting that host protein deglycosylation processes in general might contribute to intracellular bacterial adaptation. Indeed, we later found that Francisella infection modulated the transcription of numerous glycosidase and glycosyltransferase genes in human macrophages and analysis of cell extracts revealed an important increase of N and O-protein glycosylation. In eukaryotic cells, glycosylation has significant effects on protein folding, conformation, distribution, stability, and activity and dysfunction of protein glycosylation may lead to development of diseases like cancer and pathogenesis of infectious diseases. Pathogenic bacteria have also evolved dedicated glycosylation machineries and have notably been shown to use these glycoconjugates as ligands to specifically interact with the host. In this review, we will focus on Francisella and summarize our current understanding of the importance of these post-translational modifications on its intracellular niche adaptation.

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Section: Resultsmentioning

confidence: 99%

Section: Role Of Post-translational Modifications (Ptm) On Bacteria/hmentioning

confidence: 99%

Section: Role Of Post-translational Modifications (Ptm) On Bacteria/hmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Role of Glycosylation/Deglycolysation Processes in Francisella tularensis Pathogenesis

Barel

Charbit

2017

Front. Cell. Infect. Microbiol.

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“…These posttranslational modifications can alter mucin peptide charge and conformation, thereby modulating proteolytic degradation, and more extensive alterations in glycan patterns are associated with more severe disease presentation and progression, and therefore with a worse prognosis . Note that, as recently reviewed, human‐colonizing bacteria use and exploit an extraordinary plethora of posttranslational modifications on both bacterial and host proteins, which are in turn involved in immune system modulation and evasion. It is thus very tempting to speculate about how bacteria may modulate posttranslational modifications of host proteins in GI tract diseases as well.…”

Section: The Gastrointestinal Barriermentioning

confidence: 99%

How are the expression patterns of gut antimicrobial peptides modulated by human gastrointestinal diseases? A bridge between infectious, inflammatory, and malignant diseases

Bastos

Santos

Vitorino

2018

Journal of Peptide Science

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The human gut barrier is the tissue exposed to the highest load of microorganisms, harbouring 100 trillion bacteria. In addition, the gut's renewal rate outruns that of any other human tissue. Antimicrobial peptides (AMPs) are highly optimized defense molecules in the intestinal barrier optimized to maintain gastrointestinal homeostasis. Alterations in AMPs activity can lead to or result from human gastrointestinal diseases. In this review, unique, conserved, or otherwise regular alterations in the expression patterns of human AMPs across gastrointestinal inflammatory and infectious diseases were analyzed for pattern elucidation. Human gastrointestinal diseases are associated with alterations in gut AMPs' expression patterns in a peptide-specific, disease-specific, and pathogen-specific way, modulating human gastrointestinal functioning. Across diseases, there is a (i) marked reduction in otherwise constitutively expressed AMPs, leading to increased disease susceptibility, and a (ii) significant increase in the expression of inducible AMPs, leading to tissue damage and disease severity. Infections and inflammatory conditions are associated with altered gene expression in the gut, whose patterns may favour cellular metaplasia, mucosal dysfunction, and disease states. Altered expression of AMPs can thus thrive disease severity and evolution since its early stages. Nevertheless, the modulation of AMP expression patterns unveils promising therapeutic targets.

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Differential Abundance of Protein Acylation in Mycobacterium tuberculosis Under Exposure to Nitrosative Stress

Birhanu,

Riaz,

Støen

et al. 2024

Proteomics Clinical Apps

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Background: Human macrophages generate antimicrobial reactive nitrogen species in response to infection by Mycobacterium tuberculosis (Mtb). Exposure to these redox‐reactive compounds induces stress response in Mtb, which can affect posttranslational modifications (PTM). Methods: Here, we present the global analysis of the PTM acylation of Mtb proteins in response to a sublethal dose of nitrosative stress in the form of nitric oxide (NO) using label free quantification. Results: A total of 6437 acylation events were identified on 1496 Mtb proteins, and O‐acylation accounted for 92.2% of the events identified, while 7.8% were N‐acylation events. About 22% of the sites identified were found to be acylated by more than one acyl‐group. Furthermore, the abundance of each acyl‐group decreased as their molecular weight increased. Quantitative PTM analysis revealed differential abundance of acylation in proteins involved in stress response, iron ion homeostasis, growth, energy metabolism, and antimicrobial resistance (AMR) induced by nitrosative stress over time. Conclusions: The results reveal a potential role of Mtb protein acylation in the bacterial stress responses and AMR. To our knowledge, this is the first report on global O‐acylation profile of Mtb in response to NO. This will significantly improve our understanding of the changes in Mtb acylation under nitrosative stress, highly relevant for global health.

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A glimpse into the modulation of post-translational modifications of human-colonizing bacteria

Cited by 20 publications

References 281 publications

Role of Glycosylation/Deglycolysation Processes in Francisella tularensis Pathogenesis

Role of Glycosylation/Deglycolysation Processes in Francisella tularensis Pathogenesis

How are the expression patterns of gut antimicrobial peptides modulated by human gastrointestinal diseases? A bridge between infectious, inflammatory, and malignant diseases

Differential Abundance of Protein Acylation in Mycobacterium tuberculosis Under Exposure to Nitrosative Stress

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