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Titolo:
Tyrosine phosphorylation patterns and size modification of the Helicobacter pylori CagA protein after translocation into gastric epithelial cells
Autore:
Backert, S; Muller, EC; Jungblut, PR; Meyer, TF;
Indirizzi:
Max Planck Inst Infekt Biol, Mol Biol Abt, D-10117 Berlin, Germany Max Planck Inst Infekt Biol Berlin Germany D-10117 10117 Berlin, Germany Max Delbruck Ctr, FG Prot Chem & Proteomforsch, Berlin, Germany Max Delbruck Ctr Berlin Germany t Chem & Proteomforsch, Berlin, Germany
Titolo Testata:
PROTEOMICS
fascicolo: 4, volume: 1, anno: 2001,
pagine: 608 - 617
SICI:
1615-9853(200104)1:4<608:TPPASM>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
2-DIMENSIONAL GEL-ELECTROPHORESIS; IONIZATION MASS-SPECTROMETRY; PATHOGENICITY ISLAND; IV SECRETION; HOST-CELLS; KAPPA-B; KINASE; IDENTIFICATION; VIRULENCE; CYTOTOXIN;
Keywords:
mass spectrometry; molecular pathogenesis; pathogenicity island; tyrosine phosphorylation; two-dimensional gel electrophoresis; virulence;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Meyer, TF Max Planck Inst Infekt Biol, Mol Biol Abt, Schumannstr 20-21, D-10117 Berlin, Germany Max Planck Inst Infekt Biol Schumannstr 20-21 BerlinGermany D-10117
Citazione:
S. Backert et al., "Tyrosine phosphorylation patterns and size modification of the Helicobacter pylori CagA protein after translocation into gastric epithelial cells", PROTEOMICS, 1(4), 2001, pp. 608-617

Abstract

Helicobacter pylori is one of the most common bacterial pathogens that causes a variety of gastric diseases. During infection, the immune-dominant H.pylori CagA protein is translocated and tyrosine-phosphorylated in gastricepithelial cells. We compared tyrosine phosphorylation patterns of five CagA variants by two-dimensional electrophoresis (2-DE) and immunoblotting studies. Tyrosine-phosphorylated CagA was detected as two distinct protein species in strains P12, P227, G27 and 26695 suggesting that two tyrosine residues of CagA can be phosphorylated both separately and simultanously. Prediction programs revealed the presence of three putative tyrosine phosphorylation motifs in the sequences of CagA. Mutations in these motifs were identified suggesting that only two putative phosphorylation-relevant tyrosines are present in each CagA variant. CagA of strain J99 was found to be unique because essential codons were mutated in each of the three motifs and, consequently, revealed no tyrosine phosphorylation signals at all. These findings support the view that CagA from different H. pylori strains can be tyrosine-phosphorylated at one or two out of three predicted positions. Additionally, truncated CagA protein species of about 100-105 kDa (p100(CagA)) havebeen detected after infection with some of the H. pylori strains. The isoelectric point determined by both 2-DE and sequence analysis suggested that p100(CagA) represents the amino (N)-terminal part of the protein. Translocation, tyrosine phosphorylation and size modification of CagA might be involved in host signal transduction and development of gastric disease.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 01:31:53