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The outer membrane protein X from Escherichia coli exhibits immune properties.
- Source :
-
Vaccine [Vaccine] 2003 Sep 08; Vol. 21 (25-26), pp. 3765-74. - Publication Year :
- 2003
-
Abstract
- Outer membrane proteins (OMP) are expressed in Gram-negative bacterial cell wall. OmpA from Klebsiella pneumoniae (KpOmpA) has been shown to bind and to activate selectively antigen presenting cells (APCs), eliciting protective CTL responses. In this study, we investigated whether OmpX, another member of the OMP family and structurally related to OmpA, exhibits the same immune properties. Using recombinant OmpX from Escherichia coli (EcOmpX), we report that EcOmpX binds to and is internalized by human APCs. However, EcOmpX does not activate APCs. EcOmpX acts as an efficient carrier protein as it induces a potent and Th1/Th2 mixed anti-TNP humoral response. However, adjuvant is required to generate a protective anti-tumoral immune response in mice injected with a tumor model antigen coupled to EcOmpX. Collectively, these data show that EcOmpX is recognized by innate cells but does not activate them, suggesting that EcOmpX does not provide a signal danger to APCs. In conclusion, this study provides information on the molecular mechanisms involved in the recognition and activation of innate cells by bacterial outer membrane proteins.
- Subjects :
- Animals
Antibodies, Neoplasm biosynthesis
Antibody Formation immunology
Antigens, Bacterial immunology
Bacterial Outer Membrane Proteins biosynthesis
Biotin
DNA, Complementary biosynthesis
DNA, Complementary genetics
Escherichia coli metabolism
Escherichia coli Proteins biosynthesis
Flow Cytometry
Fluorescein-5-isothiocyanate
Fluorescent Dyes
Haptens immunology
Humans
Immunity, Cellular immunology
Macrophage Activation
Mice
Mice, Inbred C57BL
Microscopy, Confocal
Monocytes immunology
Neoplasm Transplantation
Recombinant Proteins biosynthesis
Recombinant Proteins immunology
Tetanus Toxoid immunology
Bacterial Outer Membrane Proteins immunology
Escherichia coli immunology
Escherichia coli Proteins immunology
Hydrolases
Subjects
Details
- Language :
- English
- ISSN :
- 0264-410X
- Volume :
- 21
- Issue :
- 25-26
- Database :
- MEDLINE
- Journal :
- Vaccine
- Publication Type :
- Academic Journal
- Accession number :
- 12922110
- Full Text :
- https://doi.org/10.1016/s0264-410x(03)00316-5