Jurnecka David D

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Proteomics (3)

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Alphavirus (3)
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Betaherpesvirinae (3)
Borrelia (3)
Botrytis cinerea (3)
Clostridium perfringens (3)
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Severe acute respiratory syndrome coronavirus 2 (3)
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Viruses (3)

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pride (3)

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Prokaryotic cell (2)
Bronchial epithelial cell (1)
Bronchial epithelium (1)
Cell culture (1)

Disease

Pertussis (2)

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Mass Spectrometry (3)
Shotgun proteomics (3)

Publication Date

2020 (2)
2018 (1)

Lab affiliation

Institute of Microbiology of the CAS, v. v. i. (2)
Laboratory of Molecular Biology of Bacterial Pathogens, Institute of Microbiology, Czech Academy of Sciences (1)

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The Bordetella pertussis and Bordetella bronchiseptica filamentous hemagglutinins are processed at different sites

Mapping of the C-terminal residues of FHA from Bordetellae utilizing differential 16O/18O labelling

ORGANISM(S): Bordetella pertussis Bordetella bronchiseptica RB50

2018-10-22 | PXD008664 | Pride

Retargeting from CR3 to the LFA-1 receptor uncovers the adenylyl cyclase enzymetranslocating segment of Bordetella adenylate cyclase toxin

The Bordetella adenylate cyclase toxinhemolysin (CyaA) and the α-hemolysin (HlyA) of Escherichia coli both belong to the family of cytolytic pore-forming Repeats in ToXin (RTX) cytotoxins. HlyA preferentially binds the αLβ2 integrin LFA-1 (CD11a/CD18) of leukocytes and can promiscuously bind and per...

ORGANISM(S): Escherichia coli Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)

2020-05-11 | PXD018789 | Pride

Ac domain translocation Fatty acyl Rtx toxin Acylation Acyltransferase Integrin

Selection of the length of fatty acyl chain and of the acylation site by the acyltransferase governs activation of RTX toxins

Numerous proteins synthesized in cells ranging from bacteria to humans have to be posttranslationally acylated to become biologically active. Bacterial Repeats in ToXin (RTX) cytolysins form a prominent group of proteins that are synthesized as inactive protoxins and undergo a posttranslational acyl...