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Infection and Immunity, September 2008, p. 3940-3950, Vol. 76, No. 9
0019-9567/08/$08.00+0     doi:10.1128/IAI.00632-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Pmp-Like Proteins Pls1 and Pls2 Are Secreted into the Lumen of the Chlamydia trachomatis Inclusion{triangledown}

Ine Jorgensen and Raphael H. Valdivia*

Department of Molecular Genetics and Microbiology and Center for Microbial Pathogenesis, Duke University Medical Center, Durham, North Carolina 27710

Received 22 May 2008/ Returned for modification 13 June 2008/ Accepted 23 June 2008

The obligate intracellular pathogen Chlamydia trachomatis secretes effector proteins across the membrane of the pathogen-containing vacuole (inclusion) to modulate host cellular functions. In an immunological screen for secreted chlamydial proteins, we identified CT049 and CT050 as potential inclusion membrane-associated proteins. These acidic, nonglobular proteins are paralogously related to the passenger domain of the polymorphic membrane protein PmpC and, like other Pmp proteins, are highly polymorphic among C. trachomatis ocular and urogenital strains. We generated antibodies to these Pmp-like secreted (Pls) proteins and determined by immunofluorescence microscopy that Pls1 (CT049) and Pls2 (CT050) localized to globular structures within the inclusion lumen and at the inclusion membrane. Fractionation of membranes and cytoplasmic components from infected cells by differential and density gradient centrifugation further indicated that Pls1 and Pls2 associated with membranes distinct from the bulk of bacterial and inclusion membranes. The accumulation of Pls1 and, to a lesser extent, Pls2 in the inclusion lumen was insensitive to the type III secretion inhibitor C1, suggesting that this translocation system is not essential for Pls protein secretion. In contrast, Pls secretion and stability were sensitive to low levels of β-lactam antibiotics, suggesting that a functional cell wall is required for Pls secretion from the bacterial cell. Finally, we tested the requirement for these proteins in Chlamydia infection by microinjecting anti-Pls1 and anti-Pls2 antibodies into infected cells. Coinjection of anti-Pls1 and -Pls2 antibodies partially inhibited expansion of the inclusion. Because Pls proteins lack classical sec-dependent secretion signals, we propose that Pls proteins are secreted into the inclusion lumen by a novel mechanism to regulate events important for chlamydial replication and inclusion expansion.

* Corresponding author. Mailing address: Duke University Medical Center, 272 Jones Bldg., Box 3580, Durham, NC 27710. Phone: (919) 668-3831. Fax: (919) 681-9193. E-mail: valdi001{at}mc.duke.edu

{triangledown} Published ahead of print on 30 June 2008.

Editor: R. P. Morrison

Infection and Immunity, September 2008, p. 3940-3950, Vol. 76, No. 9
0019-9567/08/$08.00+0     doi:10.1128/IAI.00632-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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