期刊论文

Wu, Yimou

英文

PLOS ONE

1932-6203

2013

8

7

e68764

10.1371/journal.pone.0068764

US NIHUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [R01AI47997, R01AI64537]; NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [R01AI047997, R01AI047997, R01AI047997, R01AI064537, R01AI064537, R01AI047997, R01AI047997, R01AI064537, R01AI047997, R01AI047997, R01AI064537, R01AI047997, R01AI064537, R01AI064537, R01AI047997, R01AI047997, R01AI047997, R01AI064537, R01AI047997, R01AI064537, R01AI047997, R01AI064537, R01AI064537, R01AI047997, R01AI047997, R01AI047997] Funding Source: NIH RePORTER

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Glycogen has been localized both inside and outside Chlamydia trachomatis organisms. We now report that C. trachomatis glycogen synthase (GlgA) was detected in both chlamydial organism-associated and -free forms. The organism-free GlgA molecules were localized both in the lumen of chlamydial inclusions and in the cytosol of host cells. The cytosolic GlgA displayed a distribution pattern similar to that of a known C. trachomatis-secreted protease, CPAF. The detection of GlgA was specific since the anti-GlgA antibody labeling was only removed by preabsorption with GlgA but not CPAF fusion protei...