Histopathologic characterization of the process of Marssonina brunnea infection in poplar leaves

2018 ◽  
Vol 48 (11) ◽  
pp. 1302-1310 ◽  
Author(s):  
Yanfeng Zhang ◽  
Wei He ◽  
Dong-Hui Yan
Keyword(s):  
Plasma Membranes ◽  
Leaf Surface ◽  
Host Cells ◽  
Post Inoculation ◽  
Ultrastructural Evidence ◽  
Black Spots ◽  
Marssonina Brunnea ◽  
Germ Tubes ◽  
Poplar Leaves

Marssonina brunnea (Ellis & Everh.) Magnus, the causative pathogen of Marssonina leaf spot of poplars (MLSP), can lead to complete defoliation and tree death. Although MLSP has been studied for over 30 years, its precise process of infection is currently unclear. In this study, we present the process of M. brunnea infection in detail using several types of microscopy. When the conidia came into contact with the poplar leaves, they developed germ tubes to attach to the leaf surface. During the first 2 days post inoculation (dpi), infection vesicles (IV) and primary hyphae (PH) formed within host cells. The plasma membranes of the host cells penetrated by IV remained unbroken and intact organelles were visible, indicating that the IV did not kill the host cell. At 3 dpi, secondary hyphae (SH) began to appear within and outside the host cells. The ultrastructural evidence indicated that the SH could kill the host cells rapidly, producing black spots on the surfaces of the leaves. These results collectively suggested that M. brunnea is a typical hemibiotrophic fungus. In addition, M. brunnea could develop intercellular infective hyphae (IH) for expansion. Our findings also confirmed that the germ tubes, IV, and SH are crucial structures for the disease interactions and showed that the two formae speciales of M. brunnea share the same infection histopathological features. This provides important insight for further research into M. brunnea.

scholarly journals Characterization of cobalamin receptor sites in brush-border plasma membranes of the tapeworm Spirometra mansonoides.

1983 ◽  
Vol 258 (7) ◽  
pp. 4261-4265
Author(s):  
P A Friedman ◽  
P P Weinstein ◽  
J F Mueller ◽  
R H Allen
Keyword(s):  
Brush Border ◽  
Plasma Membranes ◽  
Receptor Sites

scholarly journals Characterization of calcium binding to adipocyte plasma membranes.

1976 ◽  
Vol 251 (17) ◽  
pp. 5345-5351
Author(s):  
J M McDonald ◽  
D E Bruns ◽  
L Jarett
Keyword(s):  
Calcium Binding ◽  
Plasma Membranes ◽  
Adipocyte Plasma Membranes

scholarly journals Functional Characterization of a Redundant Plasmodium TRAP Family Invasin, TRAP-Like Protein, by Aldolase Binding and a Genetic Complementation Test

2008 ◽  
Vol 7 (6) ◽  
pp. 1062-1070 ◽  
Author(s):  
Kirsten Heiss ◽  
Hui Nie ◽  
Sumit Kumar ◽  
Thomas M. Daly ◽  
Lawrence W. Bergman ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Cell Entry ◽  
Host Cells ◽  
Complementation Test ◽  
Type I ◽  
Cycle Progression ◽  
Targeted Gene Disruption ◽  
Specific Host ◽  
Host Cell Entry

ABSTRACT Efficient and specific host cell entry is of exquisite importance for intracellular pathogens. Parasites of the phylum Apicomplexa are highly motile and actively enter host cells. These functions are mediated by type I transmembrane invasins of the TRAP family that link an extracellular recognition event to the parasite actin-myosin motor machinery. We systematically tested potential parasite invasins for binding to the actin bridging molecule aldolase and complementation of the vital cytoplasmic domain of the sporozoite invasin TRAP. We show that the ookinete invasin CTRP and a novel, structurally related protein, termed TRAP-like protein (TLP), are functional members of the TRAP family. Although TLP is expressed in invasive stages, targeted gene disruption revealed a nonvital role during life cycle progression. This is the first genetic analysis of TLP, encoding a redundant TRAP family invasin, in the malaria parasite.

scholarly journals Purification and characterization of a major glycoprotein in rat hepatoma plasma membranes. One of the membrane proteins released by phosphatidylinositol-specific phospholipase C

1987 ◽  
Vol 241 (1) ◽  
pp. 63-70 ◽  
Author(s):  
Y Ikehara ◽  
Y Hayashi ◽  
S Ogata ◽  
A Miki ◽  
T Kominami
Keyword(s):  
Alkaline Phosphatase ◽  
Phospholipase C ◽  
Plasma Membranes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Soluble Form ◽  
Microsomal Membranes ◽  
Hydrophobic Nature ◽  
Rat Hepatoma

A major glycoprotein of rat hepatoma plasma membranes was selectively released as a soluble form by incubating the membrane with phosphatidylinositol-specific phospholipase C. The soluble form corresponding to the glycoprotein was also prepared by butan-1-ol extraction of microsomal membranes at pH 5.5, whereas extraction at pH 8.5 yielded an electrophoretically different form with a hydrophobic nature. The soluble glycoprotein extracted at pH 5.5 was purified by sequential chromatography on concanavalin A-Sepharose, Sephacryl S-300 and anti-(alkaline phosphatase) IgG-Sepharose, the last step being used to remove a contaminating alkaline phosphatase. The glycoprotein thus purified was a single protein with Mr 130,000 in SDS/polyacrylamide-gel electrophoresis, although it behaved as a dimer in gel filtration on Sephacryl S-300. The glycoprotein was analysed for amino acid and carbohydrate composition. The composition of the carbohydrate moiety, which amounted to 64% by weight, suggested that the glycoprotein contained much larger numbers of N-linked oligosaccharide chains than those with O-linkage. It was confirmed that the purified glycoprotein was immunologically identical not only with that released by the phospholipase C but also with the hydrophobic form extracted with butan-1-ol at pH 8.5. The results indicate that the glycoprotein of rat hepatoma plasma membranes, which has an unusually high content of carbohydrate, is another membrane protein released by phosphatidylinositol-specific phospholipase C, as documented for alkaline phosphatase, acetylcholinesterase and Thy-1 antigen.

Impact of fluoroquinolones and aminoglycosides on P. aeruginosa virulence factor production and cytotoxicity

2021 ◽  
Author(s):  
Daniel Morgan Foulkes ◽  
Keri McLean ◽  
Marta Sloniecka ◽  
Dominic Byrne ◽  
Atikah S Haneef ◽  
...  
Keyword(s):  
Plasma Membranes ◽  
Opportunistic Pathogen ◽  
World Health Organisation ◽  
Host Cells ◽  
World Health ◽  
Corneal Epithelial Cell ◽  
Cell Infection ◽  
Minimal Inhibitory Concentrations ◽  
Line Of Therapy

Infection from the opportunistic pathogen Pseudomonas aeruginosa is one of leading causes of disability and mortality worldwide and the world health organisation has listed it with the highest priority for the need of new antimicrobial therapies. P. aeruginosa strains responsible for the poorest clinical outcomes express either ExoS or ExoU, which are injected into target host cells via the type III secretion system (T3SS). ExoS is a bifunctional cytotoxin that promotes intracellular survival of invasive P. aeruginosa by preventing targeting of the bacteria to acidified intracellular compartments and lysosomal degradation. ExoU is a potent phospholipase which causes rapid destruction of host cell plasma membranes, leading to acute tissue damage and bacterial dissemination. Fluoroquinolones are usually employed as a first line of therapy as they have been shown to be more active against P. aeruginosa in vitro than other antimicrobial classes. However, their overuse over the past decade has caused alarming rates of antibiotic resistance to emerge. In certain clinical situations, aminoglycosides have been shown to be more effective then fluoroquinolones, despite their reduced potency towards P. aeruginosa in vitro. In this study, we evaluated the effects of fluoroquinolones (moxifloxacin and ciprofloxacin) and aminoglycosides (tobramycin and gentamycin) on T3SS expression and toxicity, in corneal epithelial cell infection models. We discovered tobramycin disrupted T3SS expression and inhibited both ExoS and ExoU mediated cytotoxicity, protecting infected HCE-T cells even at concentrations below the minimal inhibitory concentrations (MIC). Fluoroquinolones moxifloxacin and ciprofloxacin, however, upregulated the T3SS and in particular did not subvert the cytotoxic effects of ExoS and ExoU.

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