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Infection and Immunity, April 2009, p. 1285-1292, Vol. 77, No. 4
0019-9567/09/$08.00+0 doi:10.1128/IAI.01062-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

L. Farah Sogo,1,
Ming Tan,2 and
Christine Sütterlin1*
Department of Developmental and Cell Biology,1 Departments of Microbiology & Molecular Genetics and Medicine, University of California, Irvine, Irvine, California 92697-23002
Received 26 August 2008/ Returned for modification 30 September 2008/ Accepted 13 January 2009
Chlamydia is an obligate intracellular bacterium that grows and replicates inside a cytoplasmic inclusion. We report that a host protein, CD59, which regulates complement function at the surfaces of uninfected cells, can be detected at the membrane of the chlamydial inclusion. This localization to the inclusion membrane was specific for CD59 and not a general feature of other glycosylphosphatidylinositol (GPI)-anchored proteins or representative cell surface proteins. Using differential permeabilization studies, we showed that CD59 is localized to the luminal but not the cytoplasmic face of the inclusion membrane, consistent with membrane association via its GPI anchor. Furthermore, CD59 was present at the inclusion even when we prevented it from associating with membrane microdomains via the GPI anchor or when we inhibited general protein transport to the cell surface, indicating that a conventional Golgi apparatus-dependent trafficking mechanism was not involved. Based on these findings, we propose that selected host proteins are trafficked to the inclusion by a Golgi apparatus-independent pathway during a Chlamydia infection.
Published ahead of print on 21 January 2009.
A.H. and L.F.S. contributed equally to this work.
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