Markus B. Tomek

ORCID: 0000-0003-0492-975X
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Research Areas
  • Oral microbiology and periodontitis research
  • Probiotics and Fermented Foods
  • HIV/AIDS oral health manifestations
  • Glycosylation and Glycoproteins Research
  • Genomics and Phylogenetic Studies
  • Receptor Mechanisms and Signaling
  • Immune Cell Function and Interaction
  • Microbial Metabolites in Food Biotechnology
  • Enzyme Production and Characterization
  • Cleft Lip and Palate Research
  • Bacterial Genetics and Biotechnology
  • Biochemical and Structural Characterization
  • T-cell and B-cell Immunology
  • Streptococcal Infections and Treatments
  • Bacteriophages and microbial interactions
  • Salivary Gland Disorders and Functions
  • Monoclonal and Polyclonal Antibodies Research
  • Spectroscopy and Quantum Chemical Studies
  • Lipid Membrane Structure and Behavior
  • Infant Nutrition and Health

BOKU University
2014-2024

University of Vienna
2024

Vienna Biocenter
2021

ETH Zurich
2019

Karolinska University Hospital
2012

Karolinska Institutet
2012

Summary Conserved C‐terminal domains ( CTD ) have been shown to act as a signal for the translocation of certain proteins across outer membrane Bacteroidetes via type IX secretion system (T9 SS ). The genome sequence periodontal pathogen T annerella forsythia predicts presence components T9 in conjunction with suite proteins. . is covered two‐dimensional crystalline surface (S‐) layer composed glycosylated TfsA and TfsB. To investigate, if functional , ‐deficient mutants were generated by...

10.1111/omi.12062 article EN Molecular Oral Microbiology 2014-06-18

Glycosylation of proteins profoundly impacts their physical and biological properties. Yet our ability to engineer novel glycoprotein structures remains limited. Established bacterial glycoengineering platforms require secretion the acceptor protein periplasmic space preassembly oligosaccharide substrate as a lipid-linked precursor, limiting access glycan substrates respectively. Here, we circumvent these bottlenecks by developing facile platform that operates in cytoplasm. The Glycoli...

10.1038/s41467-019-13283-2 article EN cc-by Nature Communications 2019-11-27

The occurrence of nonulosonic acids in bacteria is wide-spread and linked to pathogenicity. However, the knowledge cognate acid transferases scarce. In periodontopathogen Tannerella forsythia, several proposed virulence factors carry strain-specifically either a pseudaminic or legionaminic derivative as terminal sugar on an otherwise structurally identical, protein-bound oligosaccharide. This study aims shed light transfer proximal N-acetylmannosaminuronic residue within O-glycan structure,...

10.1093/glycob/cwx019 article EN cc-by-nc Glycobiology 2017-02-15

The cell surface of the oral pathogen Tannerella forsythia is heavily glycosylated with a unique, complex decasaccharide that O-glycosidically linked to bacterium's abundant (S-) layer, as well other proteins. S-layer glycoproteins are virulence factors T. and there evidence protein O-glycosylation underpins pathogenicity. To elucidate pathway, genes suspected encoding pathway components were first identified in genome sequence ATCC 43037 type strain, revealing 27-kb gene cluster was shown...

10.3389/fmicb.2018.02008 article EN cc-by Frontiers in Microbiology 2018-08-28

Tannerella forsythia is an anaerobic, Gram-negative oral pathogen that thrives in multispecies biofilms associated with periodontitis. The bacterium auxotrophic for the commonly essential bacterial cell wall sugar N‑acetylmuramic acid (MurNAc) and, thus, strictly depends on exogenous supply of MurNAc growth and maintenance morphology. A transporter (Tf_MurT; Tanf_08375) ortholog Escherichia coli etherase MurQ (Tf_MurQ; Tanf_08385) converting MurNAc-6-phosphate to GlcNAc-6-phosphate were...

10.3389/fmicb.2018.00019 article EN cc-by Frontiers in Microbiology 2018-01-26

Tannerella forsythia and Porphyromonas gingivalis target distinct virulence factors bearing a structurally conserved C-terminal domain (CTD) to the type IX protein secretion system (T9SS). The T9SS comprises an outer membrane translocation complex which works in concert with signal peptidase for CTD cleavage. Among prominent cargo linked periodontal diseases are TfsA TfsB components of T. forsythia's cell surface (S-) layer, bacterium's BspA antigen set cysteine proteinases (gingipains) from...

10.3389/fcimb.2022.835509 article EN cc-by Frontiers in Cellular and Infection Microbiology 2022-02-10

The molecular basis underlying T-cell recognition of MHC molecules presenting altered peptide ligands is still not well-established. A hierarchy activation by class I-restricted has been defined using the receptor P14 specific for H-2D(b) in complex with immunodominant lymphocytic choriomeningitis virus gp33 (KAVYNFATM). While substitution tyrosine to phenylalanine (Y4F) or serine (Y4S) abolished P14, TCR unexpectedly recognized alanine-substituted semiagonist Y4A, which displayed most...

10.1002/eji.201242588 article EN European Journal of Immunology 2012-07-26

Abstract Background The Gram-negative oral pathogen Tannerella forsythia strictly depends on the external supply of essential bacterial cell wall sugar N -acetylmuramic acid (MurNAc) for survival because lack common MurNAc biosynthesis enzymes MurA/MurB. bacterium thrives in a polymicrobial biofilm consortium and, thus, it is plausible that procures from MurNAc-containing peptidoglycan (PGN) fragments (muropeptides) released cohabiting bacteria during natural PGN turnover or death. There...

10.1186/s12866-020-02006-z article EN cc-by BMC Microbiology 2020-11-17

Introduction Degradation of host proteins by bacterial proteases leads to the subversion response and disruption oral epithelial integrity, which is considered an essential factor in progression periodontitis. High-temperature requirement A (HtrA) protease, critical for survival environmental adaptation, found several bacteria, including periodontal pathogen Tannerella forsythia . This study investigated proteolytic activity HtrA from T. its ability modulate response. Methods was identified...

10.3389/froh.2024.1425937 article EN cc-by Frontiers in Oral Health 2024-07-05
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