scholarly journals Localization of Chlamydia trachomatis hypothetical protein CT311 in host cell cytoplasm

2011 ◽  
Vol 51 (3) ◽  
pp. 101-109 ◽  
Author(s):  
Lei Lei ◽  
Manli Qi ◽  
Nicole Budrys ◽  
Robert Schenken ◽  
Guangming Zhong
Keyword(s):  
Chlamydia Trachomatis ◽  
Host Cell ◽  
Hypothetical Protein ◽  
Cell Cytoplasm ◽  
Host Cell Cytoplasm

scholarly journals Chlamydia trachomatis Secretion of an Immunodominant Hypothetical Protein (CT795) into Host Cell Cytoplasm

2011 ◽  
Vol 193 (10) ◽  
pp. 2498-2509 ◽  
Author(s):  
M. Qi ◽  
L. Lei ◽  
S. Gong ◽  
Q. Liu ◽  
M. P. DeLisa ◽  
...  
Keyword(s):  
Chlamydia Trachomatis ◽  
Host Cell ◽  
Hypothetical Protein ◽  
Cell Cytoplasm ◽  
Host Cell Cytoplasm

scholarly journals Chlamydia trachomatis GlgA Is Secreted into Host Cell Cytoplasm

PLoS ONE ◽  
2013 ◽  
Vol 8 (7) ◽  
pp. e68764 ◽  
Author(s):  
Chunxue Lu ◽  
Lei Lei ◽  
Bo Peng ◽  
Lingli Tang ◽  
Honglei Ding ◽  
...  
Keyword(s):  
Chlamydia Trachomatis ◽  
Host Cell ◽  
Cell Cytoplasm ◽  
Host Cell Cytoplasm

scholarly journals Chlamydia trachomatis secretion of hypothetical protein CT622 into host cell cytoplasm via a secretion pathway that can be inhibited by the type III secretion system inhibitor compound 1

Microbiology ◽  
2011 ◽  
Vol 157 (4) ◽  
pp. 1134-1144 ◽  
Author(s):  
Siqi Gong ◽  
Lei Lei ◽  
Xiaotong Chang ◽  
Robert Belland ◽  
Guangming Zhong
Keyword(s):  
Host Cell ◽  
Type Iii Secretion ◽  
Fusion Proteins ◽  
Hypothetical Protein ◽  
Secretion System ◽  
Cell Cytoplasm ◽  
Host Cell Cytoplasm ◽  
Cell Cytosol ◽  
H Protein ◽  
Host Cell Cytosol

Using antibodies raised with C. trachomatis fusion proteins, we localized a hypothetical protein encoded by the ORF ct622 in the cytoplasm of C. trachomatis-infected mammalian cells. The detection was specific since the antibody labelling of CT622 protein was removed by preabsorption with CT622 but not other fusion proteins. We similarly confirmed that CT621, a known secretion protein encoded by a hypothetical ORF downstream of ct622, was secreted into host cell cytosol. Proteins CT622 and CT621 displayed a similar secretion pattern, with both intra-inclusion and host cell cytosol localization, that was distinct from that of CPAF (chlamydial protease/proteasome-like activity factor). However, the expression and secretion kinetics differed significantly between CT622 and CT621: CT622 mRNA was detected at 2 h, protein at 6 h and secretion of protein into host cell cytoplasm at 36 h post-infection, while CT621 mRNA was detected at 8 h, protein at 16 h and secretion at 24 h. The secretion of both CT622 and CT621 was blocked by N′-(3,5-dibromo-2-hydroxybenzylidene)-4-nitrobenzohydrazide (compound 1), an inhibitor known to target the type III secretion system of bacteria. These results suggest that CT621 and CT622 may fulfil different functions during chlamydial intracellular growth. Further characterization of these proteins may generate important information for understanding chlamydial pathogenesis.

scholarly journals Fusion of Chlamydia trachomatis-Containing Inclusions Is Inhibited at Low Temperatures and Requires Bacterial Protein Synthesis

1998 ◽  
Vol 66 (11) ◽  
pp. 5364-5371 ◽  
Author(s):  
Christiaan Van Ooij ◽  
Ellen Homola ◽  
Eleanor Kincaid ◽  
Joanne Engel
Keyword(s):  
Protein Synthesis ◽  
Chlamydia Trachomatis ◽  
Host Cell ◽  
Host Cells ◽  
Bacterial Protein ◽  
Cell Cytoplasm ◽  
Mammalian Cell Lines ◽  
Host Cell Cytoplasm ◽  
Early Endosomes ◽  
Bacterial Protein Synthesis

ABSTRACT The human pathogen Chlamydia trachomatis is an obligate intracellular bacterium with a unique developmental cycle. Within the host cell cytoplasm, it resides within a membrane-bound compartment, the inclusion. A distinguishing characteristic of the C. trachomatis life cycle is the fusion of the chlamydia-containing inclusions with each other in the host cell cytoplasm. We report that fusion of inclusions does not occur at 32°C in multiple mammalian cell lines and with three different serovars of C. trachomatis. The inhibition of fusion was inclusion specific; the fusion with sphingolipid-containing secretory vesicles and the interaction with early endosomes were unaffected by incubation at 32°C. The inhibition of fusion of the inclusions was not primarily the result of delayed maturation of the inclusion, as infectious progeny was produced in host cells incubated at 32°C, and the unfused inclusions remained competent to fuse up to 48 h postinfection. The ability to reverse the inhibition of fusion by shifting the infected cells from 32 to 37°C allowed the measurement of the rate and the time of fusion of the inclusions after entry of the bacteria. Most significantly, we demonstrate that fusion of inclusions with each other requires bacterial protein synthesis and that the required bacterial protein(s) is present, but inactive or not secreted, at 32°C.

The RhopH complex is transferred to the host cell cytoplasm following red blood cell invasion by Plasmodium falciparum

2008 ◽  
Vol 160 (2) ◽  
pp. 81-89 ◽  
Author(s):  
Laetitia Vincensini ◽  
Gamou Fall ◽  
Laurence Berry ◽  
Thierry Blisnick ◽  
Catherine Braun Breton
Keyword(s):  
Plasmodium Falciparum ◽  
Blood Cell ◽  
Host Cell ◽  
Cell Invasion ◽  
Red Blood Cell ◽  
Cell Cytoplasm ◽  
Host Cell Cytoplasm

scholarly journals Brefeldin A inhibits transport of the glycophorin-binding protein from Plasmodium falciparum into the host erythrocyte

1994 ◽  
Vol 300 (3) ◽  
pp. 821-826 ◽  
Author(s):  
J Benting ◽  
D Mattei ◽  
K Lingelbach
Keyword(s):  
Plasmodium Falciparum ◽  
Golgi Apparatus ◽  
Host Cell ◽  
Protein Secretion ◽  
Secretory Pathway ◽  
Binding Protein ◽  
Brefeldin A ◽  
Cell Cytoplasm ◽  
Parasite Cell ◽  
Host Cell Cytoplasm

Plasmodium falciparum, a protozoan parasite of the human erythrocyte, causes the most severe form of malaria. During its intraerythrocytic development, the parasite synthesizes proteins which are exported into the host cell. The compartments involved in the secretory pathway of P. falciparum are still poorly characterized. A Golgi apparatus has not been identified, owing to the lack of specific protein markers and Golgi-specific post-translational modifications in the parasite. The fungal metabolite brefeldin A (BFA) is known to inhibit protein secretion in higher eukaryotes by disrupting the integrity of the Golgi apparatus. We have used the parasite-encoded glycophorin-binding protein (GBP), a soluble protein found in the host cell cytoplasm, as a marker to investigate the effects of BFA on protein secretion in the intracellular parasite. In the presence of BFA, GBP was not transported into the erythrocyte, but remained inside the parasite cell. The effect caused by BFA was reversible, and the protein could be chased into the host cell cytoplasm within 30 min. Transport of GBP from the BFA-sensitive site into the host cell did not require protein synthesis. Similar observations were made when infected erythrocytes were incubated at 15 degrees C. Incubation at 20 degrees C resulted in a reduction rather than a complete block of protein export. The relevance of our findings to the identification of compartments involved in protein secretion from the parasite cell is discussed.

Eimeria canadensis (Protozoa, Sporozoea): ultrastructure of the host–parasite interface during development of first-generation schizonts in vitro

1980 ◽  
Vol 58 (11) ◽  
pp. 2018-2025 ◽  
Author(s):  
Bodo E. G. Mueller
Keyword(s):  
Host Cell ◽  
Parasitophorous Vacuole ◽  
Eimeria Species ◽  
Outer Zone ◽  
Ultrastructural Observation ◽  
Cell Cytoplasm ◽  
Cell Organelles ◽  
Host Cell Cytoplasm ◽  
Host Parasite

Eimeria canadensis sporozoites were inoculated into monolayer cultures of Madin–Darby bovine kidney and primary bovine embryonic kidney cells. Sporozoites retained their shape for at least 9 days. At that time, the nucleus was enlarged and contained a prominent nucleolus, and amylopectin granules were no longer apparent. The width of the parasitophorous vacuole (pv) between host cell cytoplasm and parasite pellicle widened during transformation of sporozoites into multinucleate schizonts. Areas of altered host cell cytoplasm immediately adjacent to the pv membrane increased in size and became confluent, resulting in the formation of two distinct layers of cytoplasm. The outer zone contained the host cell nucleus, mitochondria, Golgi stacks, and ER, whereas the inner layer appeared granular and was void of all cell organelles except structures resembling ribosomes. Microfilaments were abundant at the border between inner and outer zone. In the most advanced stages observed, host cell organelles persisted only in the perinuclear region. The remaining, attenuated cytoplasm resembled the former inner zone.The novel ultrastructural observation of a bilayered cytoplasm of cells harbouring E. canadensis schizonts is compared with light microscope reports of similar effects caused by other Eimeria species of ruminants and with electron microscope findings of altered intestinal and abomasal cells of sheep harbouring "globidial" schizonts.

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