a legionella pneumophila effector protein encoded in a region of genomic plasticity binds to doticm-modified vacuoles嗜肺性军团菌效应蛋白质编码区域的基因组可塑性结合doticm-modified液泡.pdfVIP
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a legionella pneumophila effector protein encoded in a region of genomic plasticity binds to doticm-modified vacuoles嗜肺性军团菌效应蛋白质编码区域的基因组可塑性结合doticm-modified液泡
A Legionella pneumophila Effector Protein Encoded in a
Region of Genomic Plasticity Binds to Dot/Icm-Modified
Vacuoles
1 2 1
Shira Ninio , Jean Celli , Craig R. Roy *
1 Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, New Haven, Connecticut, United States of America,
2 Laboratory of Intracellular Parasites, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana,
United States of America
Abstract
Legionella pneumophila is an opportunistic pathogen that can cause a severe pneumonia called Legionnaires’ disease. In the
environment, L. pneumophila is found in fresh water reservoirs in a large spectrum of environmental conditions, where the
bacteria are able to replicate within a variety of protozoan hosts. To survive within eukaryotic cells, L. pneumophila require a
type IV secretion system, designated Dot/Icm, that delivers bacterial effector proteins into the host cell cytoplasm. In recent
years, a number of Dot/Icm substrate proteins have been identified; however, the function of most of these proteins
remains unknown, and it is unclear why the bacterium maintains such a large repertoire of effectors to promote its survival.
Here we investigate a region of the L. pneumophila chromosome that displays a high degree of plasticity among four
sequenced L. pneumophila strains. Analysis of GC content suggests that several genes encoded in this region were acquired
through horizontal gene transfer. Protein translocation studies establish that this region of genomic plasticity encodes for
multiple Dot/Icm effectors. Ectopic expression studies in mammalian cells indicate that one of these substrates, a protein
called PieA, has unique effecto
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