Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Identification of a tyrosine-phosphorylated 35 kDa carboxy-terminal fragment (p35(CagA)) of the Helicobacter pylori CagA protein in phagocytic cells:Processing or breakage?
Autore:
Moese, S; Selbach, M; Zimny-Arndt, U; Jungblut, PR; Meyer, TF; Backert, S;
Indirizzi:
Max Planck Inst Infekt Biol, Abt Mol Biol, D-10117 Berlin, Germany Max Planck Inst Infekt Biol Berlin Germany D-10117 10117 Berlin, Germany
Titolo Testata:
PROTEOMICS
fascicolo: 4, volume: 1, anno: 2001,
pagine: 618 - 629
SICI:
1615-9853(200104)1:4<618:IOAT3K>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
GASTRIC EPITHELIAL-CELLS; IV SECRETION; 2-DIMENSIONAL ELECTROPHORESIS; PATHOGENICITY ISLAND; INHIBITS PHAGOCYTOSIS; PLANT-CELLS; HOST-CELLS; TRANSLOCATION; DIFFERENTIATION; ESTABLISHMENT;
Keywords:
mass spectrometry; molecular pathogenesis; pathogenicity island; tyrosine phosphorylation; two-dimensional gel electrophoresis; virulence;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Meyer, TF Max Planck Inst Infekt Biol, Abt Mol Biol, Schumannstr 20-21, D-10117 Berlin, Germany Max Planck Inst Infekt Biol Schumannstr 20-21 BerlinGermany D-10117
Citazione:
S. Moese et al., "Identification of a tyrosine-phosphorylated 35 kDa carboxy-terminal fragment (p35(CagA)) of the Helicobacter pylori CagA protein in phagocytic cells:Processing or breakage?", PROTEOMICS, 1(4), 2001, pp. 618-629

Abstract

Helicobacter pylori is a very common bacterial pathogen that causes gastric disease by inducing the infiltration of immune cells as an initial event. Virulent H. pylori strains express a type IV secretion system composed of several Virulence (Vir) proteins encoded by the cag pathogenicity island (cag PAI). During infection of phagocytic cells (U937, Josk-M and J774A.1) wehave detected a de novo tyrosine-phosphorylated protein (p35(p-Tyr) with sizes Of 30 kDa, 38 kDa or 40 kDa, depending on the H. pylori strain. p35(p-Tyr) occurrence required functional virB4, virB7, virB10, virB11, virD4 andcagA (cytotoxin-associated gene A) genes encoded by the cag PAI suggestingthat p35(p-Tyr) is a bacterial protein of variable size. We have biochemically purified p35(p-Tyr) from infected U937 cells. Tryptic peptides of p35p-Tyr determined by matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS) identified the carboxy (C)-terminal part of the H. pylori CagA protein. Subsequent analysis by two-dimensional electrophoresis (2-DE)and immunoblotting using anti-CagA antibodies revealed the presence of three stable CagA protein species in phagocytes: (i) 130-140 kDa full-length CagA (p135(CagA)), (ii) a 100-105 kDa fragment (p100(CagA)) and (iii) a 30-40 kDa fragment (p35(CagA)). Unlike p135(CagA), p35(CagA) and p100(CagA) were also detected in much lower amounts in H. pylori without host cell contact. Therefore, breakage or processing leads to the production of p35(CagA) and p100(CagA), a process that is enhanced after translocation into host cells. MALDI-MS data and the isoelectric point determined by both 2-DE and sequence analysis suggested that p35(CagA) represents the C-terminal part of CagA and p100(CagA) corresponds to the remaining amino (N)-terminal fragment. The possible function of CagA in host signal transduction and developmentof gastric disease is discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 13:01:05