Fungal development and host cell responses to the rust fungus Puccinia substriata var. indica in seedling and mature leaves of susceptible and resistant pearl millet

1991 ◽  
Vol 69 (6) ◽  
pp. 1207-1219 ◽  
Author(s):  
J. Taylor ◽  
C. W. Mims
Keyword(s):  
Host Cell ◽  
Pearl Millet ◽  
Rust Fungus ◽  
Plant Cells ◽  
Host Cells ◽  
Resistant Cultivar ◽  
Fungal Colonization ◽  
Mature Leaves ◽  
Before And After ◽  
Mother Cells

The rust fungus Puccinia substriata var. indica established a compatible relationship with host cells, characterized by large numbers of haustoria and an extensive system of intercellular hyphae, in seedling leaves of the susceptible pearl millet cultivar Tift 23DB. At some infection sites, however, necrotic host cells and papillae formed by plant cells adjacent to infection hyphae or haustorial mother cells were noted. In seedling leaves of the moderately resistant cultivar 86-8770, the initial interaction between host cells and the pathogen was quite variable and included successful haustorium formation as well as papilla deposition. Necrosis of host cells apparently developed as a gradual disorganization of the cytoplasm of invaded and surrounding host cells and occurred at all infection sites by 2 days postinoculation. In seedling leaves of the highly resistant cultivar Tift 85DB, haustoria were established at early stages of development, followed by a rapid necrosis response at 1 day postinoculation. Host cell disintegration was noted both before and after abnormalities in haustoria were observed. In mature leaves of all three cultivars, wall deposits were quite extensive at 12 h postinoculation. In addition, necrotic plant cells appeared rapidly in both susceptible and resistant cultivars. Both of these factors may have contributed to the increased resistance to fungal colonization observed in mature leaves. Key words: Puccinia substriata var. indica, pearl millet rust, host resistance, ultrastructure.

scholarly journals Perturbation of host autophagy by the Irish potato famine pathogen

2014 ◽  
Vol 70 (a1) ◽  
pp. C826-C826
Author(s):  
Abbas Maqbool ◽  
Richard Richard ◽  
Tolga Bozkurt ◽  
Yasin Dagdas ◽  
Khaoula Belhai ◽  
...  
Keyword(s):  
Host Cell ◽  
Plant Cells ◽  
Irish Potato ◽  
Effector Proteins ◽  
Host Cells ◽  
Cell Physiology ◽  
Biochemical Basis ◽  
The Impact ◽  
Potato Famine ◽  
Irish Potato Famine

Autophagy is a catabolic process involving degradation of dysfunctional cytoplasmic components to ensure cellular survival under starvation conditions. The process involves formation of double-membrane vesicles called autophagosomes and delivery of the inner constituents to lytic compartments. It can also target invading pathogens, such as intracellular bacteria, for destruction and is thus implicated in innate immune pathways [1]. In response, certain mammalian pathogens deliver effector proteins into host cells that inhibit autophagy and contribute to enabling parasitic infection [2]. Pyhtophthora infestans, the Irish potato famine pathogen, is a causative agent of late blight disease in potato and tomato crops. It delivers a plethora of modular effector proteins into plant cells to promote infection. Once inside the cell, RXLR-type effector proteins engage with host cell proteins, to manipulate host cell physiology for the benefit of the pathogen. As plants lack an adaptive immune system, this provides a robust mechanism for pathogens to circumvent host defense. PexRD54 is an intracellular RXLR-type effector protein produced by P. infestans. PexRD54 interacts with potato homologues of autophagy protein ATG8 in plant cells. We have been investigating the structural and biochemical basis of the PexRD54/ATG8 interaction in vitro. We have purified PexRD54 and ATG8 independently and in complex from E. coli. Using protein/protein interaction studies we have shown that PexRD54 binds ATG8 with sub-micromolar affinity. We have also determined the structure of PexRD54 in the presence of ATG8. This crystal structure provides key insights into how the previously reported WY-fold of oomycete RXLR-type effectors [3] can be organized in multiple repeats. The structural data also provides insights into the interaction between PexRD54 and ATG8, suggesting further experiments to understand the impact of this interaction on host cell physiology and how this benefits the pathogen.

scholarly journals Identification of a Protein from Rust Fungi Transferred from Haustoria into Infected Plant Cells

2005 ◽  
Vol 18 (11) ◽  
pp. 1130-1139 ◽  
Author(s):  
Eric Kemen ◽  
Ariane C. Kemen ◽  
Maryam Rafiqi ◽  
Uta Hempel ◽  
Kurt Mendgen ◽  
...  
Keyword(s):  
Fluorescent Protein ◽  
Polyclonal Antibodies ◽  
Rust Fungus ◽  
Infected Plant ◽  
Plant Cells ◽  
Host Cells ◽  
Nuclear Localization Signals ◽  
Uromyces Fabae ◽  
Host Cytoplasm ◽  
Functional Efficiency

The formation of haustoria is one of the hallmarks of the interaction of obligate biotrophic fungi with their host plants. In addition to their role in nutrient uptake, it is hypothesized that haustoria are actively involved in establishing and maintaining the biotrophic relationship. We have identified a 24.3-kDa protein that exhibited a very unusual allocation. Rust transferred protein 1 from Uromyces fabae (Uf-RTP1p) was not only detected in the host parasite interface, the extrahaustorial matrix, but also inside infected plant cells by immunofluorescence and electron microscopy. Uf-RTP1p does not exhibit any similarity to sequences currently listed in the public databases. However, we identified a homolog of Uf-RTP1p in the related rust fungus Uromyces striatus (Us-RTP1p). The localization of Uf-RTP1p and Us-RTP1p inside infected plant cells was confirmed, using four independently raised polyclonal antibodies. Depending on the developmental stage of haustoria, Uf-RTP1p was found in increasing amounts in host cells, including the host nucleus. Putative nuclear localization signals (NLS) were found in the predicted RTP1p sequences. However, functional efficiency could only be verified for the Uf-RTP1p NLS by means of green fluorescent protein fusions in transformed tobacco protoplasts. Western blot analysis indicated that Uf-RTP1p and Us-RTP1p most likely enter the host cell as N-glycosylated proteins. However, the mechanism by which they cross the extrahaustorial membrane and accumulate in the host cytoplasm is unknown. The localization of RTP1p suggests that it might play an important role in the maintenance of the biotrophic interaction.

Ultrastructure of the early stages of infection of peanut leaves by the rust fungus Puccinia arachidis

1989 ◽  
Vol 67 (12) ◽  
pp. 3570-3579 ◽  
Author(s):  
C. W. Mims ◽  
J. Taylor ◽  
E. A. Richardson
Keyword(s):  
Host Cell ◽  
Mother Cell ◽  
Primary Infection ◽  
Rust Fungus ◽  
Mitotic Division ◽  
Infection Process ◽  
Rust Disease ◽  
Puccinia Arachidis ◽  
Mother Cells ◽  
Infection Hypha

Peanut rust disease proved to be an excellent system for ultrastructural study of development of infection structures by the fungus Puccinia arachidis. Fungal structures were clearly visible by light microscopy in fixed and embedded samples and could be located either on leaf surfaces or within the large substomatal chambers of peanut leaves. Samples could easily be oriented for thin sectioning. The infection process was a highly orchestrated process involving precisely timed events and highly specialized structures. Infection pegs developed from appressoria over stomata and entered the leaf by growing into the openings between guard cells. Once past the rim formed by the guard cell walls, the infection peg expanded to form a substomatal vesicle in which a synchronous mitotic division of the four nuclei occurred. A primary infection hypha then developed from the vesicle and grew into the mesophyll of the leaf until its tip or side contacted a host cell. A septum then delimited a binucleate or trinucleate terminal haustorial mother cell from the remainder of the infection hypha. The wall of the haustorial mother cell became closely appressed to that of the host cell. Following differentiation of the haustorial mother cell, a penetration peg arose from it and penetrated the host cell wall. The peg invaginated the host cell plasma membrane as it elongated and then expanded at its tip to form the haustorium body into which most of the contents of the haustorial mother cell moved. Meanwhile, the primary infection hypha formed secondary hyphae that gave rise to additional haustorial mother cells and haustoria. Key words: Puccinia arachidis, peanut rust, infection process, ultrastructure.

Ultrastructural observations of the rust fungus Physopella zeae in Zea mays

1983 ◽  
Vol 61 (8) ◽  
pp. 2231-2242 ◽  
Author(s):  
Michèle C. Heath ◽  
M. R. Bonde
Keyword(s):  
Plant Cell Wall ◽  
Rust Fungus ◽  
Plant Cells ◽  
Similar Material ◽  
Mesophyll Cells ◽  
Intracellular Location ◽  
Transmission Electron ◽  
The Matrix ◽  
Ultrastructural Characteristics ◽  
Mother Cells

Examination of sporulating uredia of the tropical corn rust fungus, Physopella zeae, with the transmission electron microscope revealed that this fungus possessed most of the distinguishing ultrastructural characteristics reported for temperate zone inhabiting members of the Uredinales. Physopella zeae differed from these latter fungi in the repeated production of urediospores from the same site on the sporogenous cell, and in the intracellular location of most of the mycelium. The intracellular mycelium was differentiated into structurally unspecialized hyphae and structurally distinct haustoria arising from differentiated haustorial mother cells which were located in the neighbouring host cell. Both types of intracellular structures were covered with a matrix, and that around the intracellular hyphae was continuous with similar material lining the plant cell wall. The matrix was thicker and more compact around intracellular hyphae than around the bodies of haustoria. The matrix lining the host walls was thinnest in sections of mesophyll cells containing a ratio of haustoria – intracellular hyphae profiles greater than one. These data suggest that the haustorium may actively inhibit matrix formation in invaded plant cells.

scholarly journals Differentiation of aecidiospore- and uredospore-derived infection structures on cowpea leaves and on artificial surfaces by Uromyces vignae

1993 ◽  
Vol 71 (9) ◽  
pp. 1236-1242 ◽  
Author(s):  
M. Stark-Urnau ◽  
K. Mendgen
Keyword(s):  
Key Words ◽  
Mother Cell ◽  
Host Plants ◽  
Rust Fungus ◽  
Host Cells ◽  
In Planta ◽  
Infection Structures ◽  
Artificial Surfaces ◽  
Uromyces Vignae ◽  
Mother Cells

Aecidiospores and uredospores are the two dikaryotic spore forms of the cowpea rust fungus Uromyces vignae. After germination they can be induced to develop a series of infection structures including appressoria, infection hyphae, and haustorial mother cells. Haustoria are then formed within host cells. The differentiation of infection structures was compared on polystyrene membranes with defined topographies, on scratched polyethylene membranes, and in planta. On polystyrene membranes with defined topographies both sporelings showed highest rates of differentiation on ridges 0.3 μm high but aecidiosporelings responded less efficiently to this stimulus than uredosporelings. On scratched polyethylene membranes, almost 90% of both sporelings differentiated appressoria, but only 10% formed haustorial mother cells; haustoria were not observed. On the host plant, by contrast, only 50% of the sporelings differentiated appressoria, but most of these formed haustorial mother cells and haustoria. In planta haustorial mother cell development occurred approximately 6 h earlier than on inductive membranes. Infection structures formed on artificial membranes and on host plants were similar in morphology and nuclear condition. Key words: cowpea rust fungus, nucleus, appressorium.

Effects of the Srl5 allele for resistance on development of the stem rust fungus and cellular responses in wheat

1986 ◽  
Vol 64 (3) ◽  
pp. 626-631 ◽  
Author(s):  
H. D. M. Gousseau ◽  
B. J. Deverall
Keyword(s):  
Stem Rust ◽  
Rust Fungus ◽  
Cell Formation ◽  
Cellular Responses ◽  
Host Cells ◽  
Puccinia Graminis ◽  
Wheat Line ◽  
Cell Necrosis ◽  
Virulent Strains ◽  
Mother Cells

The development of avirulent and virulent strains of stem rust (Puccinia graminis Pers. f.sp. tritici Eriks. & Henn.) in a susceptible wheat line and two cultivars bearing the Sr15 allele for resistance was studied, mainly by fluorescence microscopy. Formation of appressoria, substomatal vesicles, infection hyphae, and the first haustorium was unaffected by resistance. The first effect of Sr15 expression was a slower rate of haustorial mother cell formation and was first seen 48 h after inoculation. Effects on hyphal branching and colony radii followed. Necrosis of host cells was first seen at 42 h, but inspection of individual infection sites showed that necrosis did not coincide with effects on haustorial mother cells. It is possible that deterioration of host cells leading to visible host cell necrosis may be related to effects on rust development. Sr15 expression gave a mesothetic reaction, first seen microscopically 60 h after inoculation. Differences between individual infection sites in this reaction may be related to the timing of the onset of necrosis.

An ultrastructural comparison of monokaryotic and dikaryotic haustoria formed by the fusiform rust fungus Cronartium quercuum f.sp. fusiforme

1982 ◽  
Vol 60 (12) ◽  
pp. 2914-2922 ◽  
Author(s):  
D. J. Gray ◽  
H. V. Amerson ◽  
C. G. Van Dyke
Keyword(s):  
Cell Wall ◽  
Host Cell ◽  
Pinus Taeda ◽  
Mother Cell ◽  
Rust Fungus ◽  
Neck Region ◽  
Cronartium Quercuum ◽  
Host Cell Wall ◽  
Mother Cells ◽  
Mother Cell Wall

Haustoria formed by the monokaryotic stage of Cronartium quercuum f. sp. fusiforme in Pinus taeda differed from those of the dikaryotic phase in Quercus rubra. Monokaryotic (M) haustorial walls were continuous with the walls of relatively undifferentiated haustorial mother cells. The septate M-haustorial neck and expanded M-haustorial body were separated from the invaginated host plasmalemma by a sheath which was continuous with the host cell wall. Collars encasing sheaths were infrequently observed. Dikaryotic (D) haustoria were morphologically similar to M-haustoria; however, they differed in several respects when examined with TEM. The D-haustorial mother cell wall was thickened at the penetration site but a reduction in the number of wall layers occurred between the thickened portion of the mother cell and the D-haustorium. A darkly staining neckband was present in the wall of the nonseptate D-haustorial neck but was lacking in the M-haustorium. An extensive sheath separated the invaginated host plasmalemma from the D-haustorial wall distally from the neckband. However, the sheath was separated from the D-haustorial wall and from the host cell wall by an invaginated host plasmalemma doubled in the haustorial neck region proximally from the neckband.

scholarly journals Metabolic Signatures of Cryptosporidium parvum-Infected HCT-8 Cells and Impact of Selected Metabolic Inhibitors on C. parvum Infection under Physioxia and Hyperoxia

Biology ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 60
Author(s):  
Juan Vélez ◽  
Zahady Velasquez ◽  
Liliana M. R. Silva ◽  
Ulrich Gärtner ◽  
Klaus Failing ◽  
...  
Keyword(s):  
Host Cell ◽  
Cryptosporidium Parvum ◽  
Cell Metabolism ◽  
Lactate Production ◽  
Glucose Consumption ◽  
Host Cells ◽  
Metabolic Inhibitors ◽  
Low Oxygen ◽  
Metabolic Signatures

Cryptosporidium parvum is an apicomplexan zoonotic parasite recognized as the second leading-cause of diarrhoea-induced mortality in children. In contrast to other apicomplexans, C.parvum has minimalistic metabolic capacities which are almost exclusively based on glycolysis. Consequently, C. parvum is highly dependent on its host cell metabolism. In vivo (within the intestine) infected epithelial host cells are typically exposed to low oxygen pressure (1–11% O2, termed physioxia). Here, we comparatively analyzed the metabolic signatures of C. parvum-infected HCT-8 cells cultured under both, hyperoxia (21% O2), representing the standard oxygen condition used in most experimental settings, and physioxia (5% O2), to be closer to the in vivo situation. The most pronounced effect of C. parvum infection on host cell metabolism was, on one side, an increase in glucose and glutamine uptake, and on the other side, an increase in lactate release. When cultured in a glutamine-deficient medium, C. parvum infection led to a massive increase in glucose consumption and lactate production. Together, these results point to the important role of both glycolysis and glutaminolysis during C. parvum intracellular replication. Referring to obtained metabolic signatures, we targeted glycolysis as well as glutaminolysis in C. parvum-infected host cells by using the inhibitors lonidamine [inhibitor of hexokinase, mitochondrial carrier protein (MCP) and monocarboxylate transporters (MCT) 1, 2, 4], galloflavin (lactate dehydrogenase inhibitor), syrosingopine (MCT1- and MCT4 inhibitor) and compound 968 (glutaminase inhibitor) under hyperoxic and physioxic conditions. In line with metabolic signatures, all inhibitors significantly reduced parasite replication under both oxygen conditions, thereby proving both energy-related metabolic pathways, glycolysis and glutaminolysis, but also lactate export mechanisms via MCTs as pivotal for C. parvum under in vivo physioxic conditions of mammals.

scholarly journals The Campylobacter jejuni CiaD effector co-opts the host cell protein IQGAP1 to promote cell entry

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Nicholas M. Negretti ◽  
Christopher R. Gourley ◽  
Prabhat K. Talukdar ◽  
Geremy Clair ◽  
Courtney M. Klappenbach ◽  
...  
Keyword(s):  
Host Cell ◽  
Campylobacter Jejuni ◽  
Foodborne Pathogen ◽  
Small Gtpase ◽  
Host Cells ◽  
Cell Protein ◽  
Host Cell Protein ◽  
Cell Binding ◽  
Actin Reorganization ◽  
Cell Cytosol

AbstractCampylobacter jejuni is a foodborne pathogen that binds to and invades the epithelial cells lining the human intestinal tract. Maximal invasion of host cells by C. jejuni requires cell binding as well as delivery of the Cia proteins (Campylobacter invasion antigens) to the host cell cytosol via the flagellum. Here, we show that CiaD binds to the host cell protein IQGAP1 (a Ras GTPase-activating-like protein), thus displacing RacGAP1 from the IQGAP1 complex. This, in turn, leads to the unconstrained activity of the small GTPase Rac1, which is known to have roles in actin reorganization and internalization of C. jejuni. Our results represent the identification of a host cell protein targeted by a flagellar secreted effector protein and demonstrate that C. jejuni-stimulated Rac signaling is dependent on IQGAP1.

scholarly journals A Single-Pass Type I Membrane Protein from the Apicomplexan Parasite Cryptosporidium parvum with Nanomolar Binding Affinity to Host Cell Surface

2021 ◽  
Vol 9 (5) ◽  
pp. 1015
Author(s):  
Tianyu Zhang ◽  
Xin Gao ◽  
Dongqiang Wang ◽  
Jixue Zhao ◽  
Nan Zhang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Host Cell ◽  
Binding Affinity ◽  
Cryptosporidium Parvum ◽  
Host Cells ◽  
Watery Diarrhea ◽  
Type I ◽  
Single Pass ◽  
Host Cell Surface

Cryptosporidium parvum is a globally recognized zoonotic parasite of medical and veterinary importance. This parasite mainly infects intestinal epithelial cells and causes mild to severe watery diarrhea that could be deadly in patients with weakened or defect immunity. However, its molecular interactions with hosts and pathogenesis, an important part in adaptation of parasitic lifestyle, remain poorly understood. Here we report the identification and characterization of a C. parvum T-cell immunomodulatory protein homolog (CpTIPH). CpTIPH is a 901-aa single-pass type I membrane protein encoded by cgd5_830 gene that also contains a short Vibrio, Colwellia, Bradyrhizobium and Shewanella (VCBS) repeat and relatively long integrin alpha (ITGA) N-terminus domain. Immunofluorescence assay confirmed the location of CpTIPH on the cell surface of C. parvum sporozoites. In congruence with the presence of VCBS repeat and ITGA domain, CpTIPH displayed high, nanomolar binding affinity to host cell surface (i.e., Kd(App) at 16.2 to 44.7 nM on fixed HCT-8 and CHO-K1 cells, respectively). The involvement of CpTIPH in the parasite invasion is partly supported by experiments showing that an anti-CpTIPH antibody could partially block the invasion of C. parvum sporozoites into host cells. These observations provide a strong basis for further investigation of the roles of CpTIPH in parasite-host cell interactions.

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