
teresa.olczak@uwr.edu.pl
tel. +48 71 375 26 12
Interested
- porphyromonas gingivalis
- biochemistry molecular biology
- microbiology
- immunology
- dentistry
- general science technology
- chemical physics
- hmu system
- hus system
- periodontal diseases
Scientific discipline
- medical sciences
- biotechnology
Latest publications
- Hemophore-like proteins of the HmuY family in the oral and gut microbiome: unraveling the mystery of their evolution
- Production of interferon‐gamma, interleukin‐6, and interleukin‐1β by human peripheral blood mononuclear cells stimulated with novel lys‐gingipain synthetic peptides.
- Bacteroides fragilis expresses three proteins similar to Porphyromonas gingivalisHmuY: Hemophore‐like proteins differentially evolved to participate in heme acquisition in oral and gut microbiomes
- Glycation of host proteins increases pathogenic potential of Porphyromonas gingivalis.
- Unique properties of heme binding of the Porphyromonas gingivalis HmuY hemophore-like protein result from the evolutionary adaptation of the protein structure.
- SLC35A5 protein - a Golgi complex member with putative nucleotide sugar transport activity.
- Porphyromonas gingivalis HmuY and Streptococcus gordonii GAPDH—novel heme acquisition strategy in the oral microbiome.
- Porphyromonas gingivalis HmuY and Bacteroides vulgatus Bvu—A Novel Competitive Heme Acquisition Strategy
- Comparative analysis of Porphyromonas gingivalis A7436 and ATCC 33277 strains reveals differences in the expression of heme acquisition systems
- Interplay between Porphyromonas gingivalis hemophore-like protein HmuY and Kgp/RgpA gingipains plays a superior role in heme supply
- Prevotella intermedia produces two proteins homologous to Porphyromonas gingivalis HmuY but with different heme coordination mode.
- Novel synthetic peptide derived from Porphyromonas gingivalis Lys-gingipain detects IgG-mediated host response in periodontitis.
- Porphyromonas gingivalis PgFur is a member of a novel Fur subfamily with non-canonical function.
- Apoptosis transcriptional profile induced by Porphyromonas gingivalis HmuY.
- Porphyromonas endodontalis HmuY differentially participates in heme acquisition compared to the Porphyromonas gingivalis and Tannerella forsythia hemophore-like proteins
- Biosynthesis of GlcNAc-rich N- and O-glycans in the Golgi apparatus does not require the nucleotide sugar transporter SLC35A3
- Hemophore-like proteins produced by periodontopathogens are recognized by the host immune system and react differentially with IgG antibodies
- In silico analysis as a strategy to identify candidate epitopes with human IgG reactivity to study Porphyromonas gingivalis virulence factors.
- PgFur participates differentially in expression of virulence factors in more virulent A7436 and less virulent ATCC 33277 Porphyromonas gingivalis strains.
- Lysine at position 329 within a C-terminal dilysine motif is crucial for the ER localization of human SLC35B4.