Glycosylation of the Enterobacter cloacae outer membrane protein OmpX in eukaryotic cells.
FEMS Microbiol Lett
; 177(2): 305-11, 1999 Aug 15.
Article
em En
| MEDLINE
| ID: mdl-10474197
ABSTRACT
The topological model of the Enterobacter cloacae outer membrane protein OmpX showed three putative glycosylation sites. When OmpX was expressed in bacteria that were cultured under aerated conditions, no glycosylation was observed. The coupling of carbohydrate chains to the ompX gene product was also investigated in the eukaryotic baculovirus expression system. For this purpose, a recombinant ompX gene-containing baculovirus was made. Infection of insect cells with this recombinant virus resulted in the production of sufficient amounts of OmpX to study glycosylation. In this system, all potential N-glycosylation sites of OmpX were utilized. Furthermore, it became clear that glycosylated OmpX was retained in the insect cells and was not secreted in the medium. Given the fact that OmpX plays a role in the invasion of E. cloacae in rabbit enterocytes, glycosylation of this protein occurring only under specific conditions may be involved in this process.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas da Membrana Bacteriana Externa
/
Processamento de Proteína Pós-Traducional
/
Enterobacter cloacae
/
Proteínas de Escherichia coli
/
Hidrolases
Limite:
Animals
Idioma:
En
Revista:
FEMS Microbiol Lett
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Holanda