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Characterization of Chlamydia trachomatis L2‐induced tyrosine‐phosphorylated HeLa cell proteins by two‐dimensional gel electrophoresis
Author(s) -
Birkelund Svend,
Bini Luca,
Pallini Vitaliano,
SanchezCampillo Maria,
Liberatori Sabrina,
Clausen Johannes D.,
Østergaard Søren,
Holm Arne,
Christiansen Gunna
Publication year - 1997
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150180338
Subject(s) - chlamydia trachomatis , tyrosine phosphorylation , tyrosine , phagocytosis , gel electrophoresis , biology , phosphorylation , hela , intracellular , microbiology and biotechnology , polyacrylamide gel electrophoresis , protein phosphorylation , biochemistry , cell , virology , enzyme , protein kinase a
Chlamydia trachomatis is an obligate intracellular bacteria, inducing its own uptake in nonprofessional phagocytes either by phagocytosis or pinocytosis. We have previously shown that C. trachomatis L2 induces tyrosine phosphorylation of eukaryotic proteins upon their entry by phagocytosis. In this paper we characterize the tyrosine‐phosphorylated proteins by two‐dimensional gel electrophoresis. In immunoblotting with anti‐phosphotyrosine antibodies of C. trachomatis L2‐infected HeLa cells, but not with uninfected cells, two rows of spots were observed with a molecular mass of 69 and 71 kDa and p I from 5.0 to 5.2. In addition, a single spot of 100 kDa and p I 6.2 was observed.