FINE STRUCTURE OF PLASMODIOPHORA BRASSICAE IN SPOROGENESIS

1967 ◽  
Vol 45 (9) ◽  
pp. 1665-1669 ◽  
Author(s):  
P. H. Williams ◽  
Sharon S. McNabola
Keyword(s):  
Endoplasmic Reticulum ◽  
Fine Structure ◽  
Host Cell ◽  
Outer Membrane ◽  
Lipid Droplets ◽  
Plasmodiophora Brassicae ◽  
Cell Cytoplasm ◽  
Host Cell Cytoplasm ◽  
Vacuolar Membranes ◽  
Sporangial Wall

The vegetative Plasmodium of Plasmodiophora brassicae is contained within host cell cytoplasm. The multinucleate Plasmodium contains numerous large lipid droplets and is replete with mitochondria, dictyosomes, endoplasmic reticulum, and ribosomes. A 250 Å thick osmiophilic plasmodial envelope is characteristic of the vegetative Plasmodium. This envelope is composed of two closely appressed membranes each consisting of a pair of electron-dense layers. As sporogenesis is initiated, the outer membrane of the plasmodial envelope disintegrates, leaving the Plasmodium surrounded by the plasmodial membrane. Nucleoli disappear and numerous vacuoles and vesicles appear in the cytoplasm of the parasite. Vacuoles appear to be formed from invaginations of the plasmodial membrane. These vacuoles become aligned in planes of cleavage around each nucleus, forming the boundaries of each future sporangium. As these vacuoles coalesce, the nucleus of each young resting sporangium becomes surrounded with cytoplasm and is enveloped by the vacuolar membranes. Spines form on the sporangial membrane as aggregates of residual vacuolar material. The sporangial wall is then deposited between the sporangial membrane and the spines. Intact host nuclei, mitochondria, and plastids can be found dispersed among the mature resting sporangia. The host plasmalemma is the only membrane surrounding the mass of resting sporangia. The uninucleate resting sporangium is rich in lipid and contains those organelles found in the vegetative Plasmodium.

scholarly journals Cardiolipin Synthesis and Outer Membrane Localization Are Required forShigella flexneriVirulence

mBio ◽  
2017 ◽  
Vol 8 (4) ◽  
Author(s):  
Rachael M. Rossi ◽  
Lauren Yum ◽  
Hervé Agaisse ◽  
Shelley M. Payne
Keyword(s):  
Cell Division ◽  
Epithelial Cells ◽  
Host Cell ◽  
Outer Membrane ◽  
Shigella Flexneri ◽  
Cell Cytoplasm ◽  
Inner Membrane ◽  
Bacterial Surface ◽  
Host Cell Cytoplasm ◽  
Cultured Epithelial Cells

ABSTRACTCardiolipin, an anionic phospholipid that resides at the poles of the inner and outer membranes, is synthesized primarily by the putative cardiolipin synthase ClsA inShigella flexneri. AnS. flexneri clsAmutant had no cardiolipin detected within its membrane, grew normallyin vitro, and invaded cultured epithelial cells, but it failed to form plaques in epithelial cell monolayers, indicating that cardiolipin is required for virulence. TheclsAmutant was initially motile within the host cell cytoplasm but formed filaments and lost motility during replication and failed to spread efficiently to neighboring cells. Mutation ofpbgA, which encodes the transporter for cardiolipin from the inner membrane to the outer membrane, also resulted in loss of plaque formation. TheS. flexneri pbgAmutant had normal levels of cardiolipin in the inner membrane, but no cardiolipin was detected in the outer membrane. ThepbgAmutant invaded and replicated normally within cultured epithelial cells but failed to localize the actin polymerization protein IcsA properly on the bacterial surface and was unable to spread to neighboring cells. TheclsAmutant, but not thepbgAmutant, had increased phosphatidylglycerol in the outer membrane. This appeared to compensate partially for the loss of cardiolipin in the outer membrane, allowing some IcsA localization in the outer membrane of theclsAmutant. We propose a dual function for cardiolipin inS. flexneripathogenesis. In the inner membrane, cardiolipin is essential for proper cell division during intracellular growth. In the outer membrane, cardiolipin facilitates proper presentation of IcsA on the bacterial surface.IMPORTANCEThe human pathogenShigella flexnericauses bacterial dysentery by invading colonic epithelial cells, rapidly multiplying within their cytoplasm, and then spreading intercellularly to neighboring cells. Worldwide,Shigellaspp. infect hundreds of millions of people annually, with fatality rates up to 15%. Antibiotic treatment ofShigellainfections is compromised by increasing antibiotic resistance, and there is no approved vaccine to prevent future infections. This has created a growing need to understandShigellapathogenesis and identify new targets for antimicrobial therapeutics. Here we show a previously unknown role of phospholipids inS. flexneripathogenesis. We demonstrate that cardiolipin is required in the outer membrane for proper surface localization of IcsA and in the inner membrane for cell division during growth in the host cell cytoplasm.

scholarly journals FINE STRUCTURE OF THE ASEXUAL STAGES OF PLASMODIUM ELONGATUM

1967 ◽  
Vol 34 (1) ◽  
pp. 229-249 ◽  
Author(s):  
Masamichi Aikawa ◽  
Clay G. Huff ◽  
Helmuth Sprinz
Keyword(s):  
Fine Structure ◽  
Host Cell ◽  
Malarial Parasite ◽  
Red Cell ◽  
Digestive Vacuole ◽  
Cell Cytoplasm ◽  
Erythrocytic Stage ◽  
New Host ◽  
Feeding Mechanism ◽  
Host Cell Cytoplasm

Plasmodium elongatum, an avian malarial parasite, differs from other such parasites by infecting both the circulating red blood cells and the hematopoietic cells. The exoerythrocytic development of P. elongatum occurs mainly in these red cell precursors. The fine structure of the asexual stages of P. elongatum has been studied in the bone marrow and peripheral blood of canaries and compared with that of the asexual stages of other avian malarial parasites. With minor differences, the merozoites of P. elongatum possess the same organelles as those in the exoerythrocytic merozoites of P. fallax and the erythrocytic stages of P. cathemerium, P. lophurae, P. fallax, and P. gallinaceum. The developmental sequence is also essentially similar to that of other avian malarial parasites, in that upon entry into a new host cell, the dedifferentiation, growth, and redifferentiation phases take place. However, we have found some important differences in the feeding mechanism of P. elongatum. The cytostome is involved in the ingestion of host cell cytoplasm in both exoerythrocytic and erythrocytic stages, in contrast to P. fallax, in which the cytostome is inactive in the exoerythrocytic stages. In P. elongatum, host cell cytoplasm is ingested through the cytostome, and "boluses" are formed and incorporated into a large digestive vacuole. Subsequently, the digestion of the boluses takes place in this digestive vacuole. Thus, in regard to the function of the cytostome, the exoerythrocytic stages of P. elongatum appear to be closely related to the erythrocytic stage which has a feeding mechanism similar to that of the erythrocytic stage of other avian malarial parasites.

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.

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

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.

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
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