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Nucleic Acids Research, 2003, Vol. 31, No. 3 886-892
© 2003 Oxford University Press

Infection by Mycoplasma hyorhinis strongly enhances uptake of antisense oligonucleotides: a reassessment of receptor-mediated endocytosis in the HepG2 cell line

Philippe de Diesbach*, Francisca N’Kuli, Michel Delmée1 and Pierre J. Courtoy

Cell Biology Unit, Christian de Duve Institute of Cellular Pathology and Université catholique de Louvain, UCL 7541, 75 avenue Hippocrate, B-1200 Brussels, Belgium and 1 Bacteriology Unit, Université catholique de Louvain, UCL 5490, 54 avenue Hippocrate, B-1200 Brussels, Belgium

*To whom correspondence should be addressed. Tel: +32 2 764 7541; Fax: +32 2 764 7543; Email: diesbach{at}cell.ucl.ac.be

This paper shows that the ~66 kDa band, previously isolated from the HepG2 cell line as an oligonucleotide (ON) plasma membrane ‘receptor’, is induced by Mycoplasma infection. Moreover, this band has been identified as the invariant membrane protein of Mycoplasma hyorhinis, p70, based on ribosomal DNA sequencing combined with ON ligand blotting after p70 immunoprecipitation by a monoclonal antibody. Whereas antibiotic treatment of infected HepG2 cells strongly decreased ON capture, as measured by a biochemical assay, conversely, deliberate infection of HeLa cells with M.hyorhinis dramatically promoted ON uptake but did not affect receptor-mediated endocytosis of transferrin. This was confirmed by confocal microscopy of infected HepG2 cells, which also showed an indistinguishable labelling pattern after exposure of living cells to fluorescent ON and after p70 immunolabelling in permeabilised fixed cells. We propose that ON binds to p70 on M.hyorhinis attached at the cell surface, after which the complex is internalised by ‘piggy-back’ endocytosis.


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