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  • 1
    Online Resource
    Online Resource
    Proceedings of the National Academy of Sciences ; 2001
    In:  Proceedings of the National Academy of Sciences Vol. 98, No. 14 ( 2001-07-03), p. 8133-8138
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 98, No. 14 ( 2001-07-03), p. 8133-8138
    Abstract: Biotrophic plant pathogenic fungi differentiate specialized infection structures within the living cells of their host plants. These haustoria have been linked to nutrient uptake ever since their discovery. We have for the first time to our knowledge shown that the flow of sugars from the host Vicia faba to the rust fungus Uromyces fabae seems to occur largely through the haustorial complex. One of the most abundantly expressed genes in rust haustoria, the expression of which is negligible in other fungal structures, codes for a hexose transporter. Functional expression of the gene termed HXT1 in Saccharomyces cerevisiae and Xenopus laevis oocytes assigned a substrate specificity for d -glucose and d -fructose and indicated a proton symport mechanism. Abs against HXT1p exclusively labeled haustoria in immunofluorescence microscopy and the haustorial plasma membrane in electron microscopy. These results suggest that the fungus concentrates this transporter in haustoria to take advantage of a specialized compartment of the haustorial complex. The extrahaustorial matrix, delimited by the plasma membranes of both host and parasite, constitutes a newly formed apoplastic compartment with qualities distinct from those of the bulk apoplast. This organization might facilitate the competition of the parasite with natural sink organs of the host.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    RVK:
    RVK:
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2001
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
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  • 2
    Online Resource
    Online Resource
    Elsevier BV ; 2000
    In:  Physiological and Molecular Plant Pathology Vol. 56, No. 4 ( 2000-04), p. 141-145
    In: Physiological and Molecular Plant Pathology, Elsevier BV, Vol. 56, No. 4 ( 2000-04), p. 141-145
    Type of Medium: Online Resource
    ISSN: 0885-5765
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2000
    detail.hit.zdb_id: 1471461-9
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Wiley ; 2003
    In:  New Phytologist Vol. 159, No. 1 ( 2003-07), p. 93-100
    In: New Phytologist, Wiley, Vol. 159, No. 1 ( 2003-07), p. 93-100
    Abstract: Haustoria are morphological features of an extremely successful class of plant parasites, the obligate biotrophs. The broad phylogenetic spectrum of organisms producing haustoria suggests that these structures have arisen many times in the course of evolution and represent specific adaptations of these organisms to the close interaction with their respective host plants. This close interaction and the fact that these structures cannot be produced in vitro have hampered an analysis of the roles of haustoria in biotrophy for many decades. Only recently has it become possible to analyse haustorial function at a molecular level. A picture is beginning to emerge indicating that haustoria do not only serve in nutrient uptake – a task postulated for these elements ever since their discovery. Moreover, they seem to perform enormous biosynthetic duties. They also seem to be engaged in the suppression of host defense responses and in redirecting or reprogramming the host's metabolic flow. This review intends to summarize current knowledge about the structure and function especially of rust haustoria.
    Type of Medium: Online Resource
    ISSN: 0028-646X , 1469-8137
    Language: English
    Publisher: Wiley
    Publication Date: 2003
    detail.hit.zdb_id: 208885-X
    detail.hit.zdb_id: 1472194-6
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  • 4
    Online Resource
    Online Resource
    Portland Press Ltd. ; 2005
    In:  Biochemical Journal Vol. 389, No. 2 ( 2005-07-15), p. 289-295
    In: Biochemical Journal, Portland Press Ltd., Vol. 389, No. 2 ( 2005-07-15), p. 289-295
    Abstract: We have identified and characterized a novel NADP+-dependent D-arabitol dehydrogenase and the corresponding gene from the rust fungus Uromyces fabae, a biotrophic plant pathogen on broad bean (Vicia faba). The new enzyme was termed ARD1p (D-arabitol dehydrogenase 1). It recognizes D-arabitol and mannitol as substrates in the forward reaction, and D-xylulose, D-ribulose and D-fructose as substrates in the reverse reaction. Co-factor specificity was restricted to NADP(H). Kinetic data for the major substrates and co-factors are presented. A detailed analysis of the organization and expression pattern of the ARD1 gene are also given. Immunocytological data indicate a localization of the gene product predominantly in haustoria, the feeding structures of these fungi. Analyses of metabolite levels during pathogenesis indicate that the D-arabitol concentration rises dramatically as infection progresses, and D-arabitol was shown in an in vitro system to be capable of quenching reactive oxygen species involved in host plant defence reactions. ARD1p may therefore play an important role in carbohydrate metabolism and in establishing and/or maintaining the biotrophic interaction in U. fabae.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    RVK:
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 2005
    detail.hit.zdb_id: 1473095-9
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  • 5
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2005
    In:  Plant Physiology Vol. 137, No. 1 ( 2005-01-01), p. 190-198
    In: Plant Physiology, Oxford University Press (OUP), Vol. 137, No. 1 ( 2005-01-01), p. 190-198
    Abstract: Levels of the C6-polyol mannitol were observed to rise dramatically in the biotrophic interaction of the rust fungus Uromyces fabae and its host plant Vicia faba. Mannitol was found in millimolar concentrations in extracts and apoplastic fluids of infected leaves and also in extracts of spores. We suggest that this polyol might have at least a dual function: first, as a carbohydrate storage compound, and second, as a scavenger of reactive oxygen species. Mannitol accumulation is accompanied by high expression of a mannitol dehydrogenase (MAD1) in haustoria. While MAD1 transcripts were detected in haustoria only, immunolocalization studies show that the gene product is also present in spores. Kinetic and thermodynamic analyses of the MAD1p catalyzed reactions indicate that the enzyme might be responsible for the production of mannitol in haustoria and for the utilization of mannitol in spores. Since V. faba is normally unable to synthesize or utilize polyols, the multipurpose usage of mannitol seems an ideal strategy for the fungal pathogen.
    Type of Medium: Online Resource
    ISSN: 1532-2548 , 0032-0889
    RVK:
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2005
    detail.hit.zdb_id: 2004346-6
    detail.hit.zdb_id: 208914-2
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Scientific Societies ; 2000
    In:  Molecular Plant-Microbe Interactions® Vol. 13, No. 6 ( 2000-06), p. 629-636
    In: Molecular Plant-Microbe Interactions®, Scientific Societies, Vol. 13, No. 6 ( 2000-06), p. 629-636
    Abstract: In the rust fungus Uromyces fabae, the transition from the early stages of host plant invasion toward parasitic growth is accompanied by the activation of many genes (PIGs = in planta induced genes). Two of them, PIG1 = THI1) and PIG4 (= THI2), were found to be highly transcribed in haustoria, and are homologous to genes involved in thiamine (vitamin B1) biosynthesis in yeast. Their functional identity was confirmed by complementation of Schizosac-charomyces pombe thiamine auxotrophic thi3 (nmt1) and thi2 (nmt2) mutants, respectively. In contrast to thiamine biosynthesis genes of other fungi that are completely suppressed by thiamine, THI1 and THI2 expression was not affected by the addition of thiamine to rust hyphae grown either in vitro or in planta. Immunoblot analysis revealed decreasing amounts of THI1p in extracts from spores, germlings, and in vitro-grown infection structures with increasing time after inoculation. Immunofluorescence microscopy of rust-infected leaves detected high concentrations of THI1p in haustoria, and only low amounts in intercellu-lar hyphae. In the sporulating mycelium, THI1p was found in the basal hyphae of the uredia, but not in the pedicels and only at very low levels in uredospores. These data indicate that the haustorium is an essential structure of the biotrophic rust mycelium not only for nutrient uptake but also for the biosynthesis of metabolites such as thiamine.
    Type of Medium: Online Resource
    ISSN: 0894-0282 , 1943-7706
    Language: English
    Publisher: Scientific Societies
    Publication Date: 2000
    detail.hit.zdb_id: 2037108-1
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Scientific Societies ; 2005
    In:  Molecular Plant-Microbe Interactions® Vol. 18, No. 11 ( 2005-11), p. 1130-1139
    In: Molecular Plant-Microbe Interactions®, Scientific Societies, Vol. 18, No. 11 ( 2005-11), p. 1130-1139
    Abstract: 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.
    Type of Medium: Online Resource
    ISSN: 0894-0282 , 1943-7706
    Language: English
    Publisher: Scientific Societies
    Publication Date: 2005
    detail.hit.zdb_id: 2037108-1
    SSG: 12
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  • 8
    In: Molecular Plant-Microbe Interactions®, Scientific Societies, Vol. 19, No. 6 ( 2006-06), p. 625-634
    Abstract: Invertases are key enzymes in carbon partitioning in higher plants. They gain additional importance in the distribution of carbohydrates in the event of wounding or pathogen attack. Although many researchers have found an increase in invertase activity upon infection, only a few studies were able to determine whether the source of this activity was host or parasite. This article analyzes the role of invertases involved in the biotrophic interaction of the rust fungus Uromyces fabae and its host plant, Vicia faba. We have identified a fungal gene, Uf-INV1, with homology to invertases and assessed its contribution to pathogenesis. Expression analysis indicated that transcription began upon penetration of the fungus into the leaf, with high expression levels in haustoria. Heterologous expression of Uf-INV1 in Saccharomyces cerevisiae and Pichia pastoris allowed a biochemical characterization of the enzymatic activity associated with the secreted gene product INV1p. Expression analysis of the known vacuolar and cell-wall-bound invertase isoforms of V. faba indicated a decrease in the expression of a vacuolar invertase, whereas one cell-wall-associated invertase exhibited increased expression. These changes were not confined to the infected tissue, and effects also were observed in remote plant organs, such as roots. These findings hint at systemic effects of pathogen infection. Our results support the hypothesis that pathogen infection establishes new sinks which compete with physiological sink organs.
    Type of Medium: Online Resource
    ISSN: 0894-0282 , 1943-7706
    Language: English
    Publisher: Scientific Societies
    Publication Date: 2006
    detail.hit.zdb_id: 2037108-1
    SSG: 12
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  • 9
    In: Molecular Plant Pathology, Wiley, Vol. 15, No. 4 ( 2014-05), p. 379-393
    Abstract: Haustoria of biotrophic rust fungi are responsible for the uptake of nutrients from their hosts and for the production of secreted proteins, known as effectors, which modulate the host immune system. The identification of the transcriptome of haustoria and an understanding of the functions of expressed genes therefore hold essential keys for the elucidation of fungus–plant interactions and the development of novel fungal control strategies. Here, we purified haustoria from infected leaves and used 454 sequencing to examine the haustorial transcriptomes of P hakopsora pachyrhizi and U romyces appendiculatus , the causal agents of soybean rust and common bean rust, respectively. These pathogens cause extensive yield losses in their respective legume crop hosts. A series of analyses were used to annotate expressed sequences, including transposable elements and viruses, to predict secreted proteins from the assembled sequences and to identify families of candidate effectors. This work provides a foundation for the comparative analysis of haustorial gene expression with further insights into physiology and effector evolution.
    Type of Medium: Online Resource
    ISSN: 1464-6722 , 1364-3703
    URL: Issue
    Language: English
    Publisher: Wiley
    Publication Date: 2014
    detail.hit.zdb_id: 2020755-4
    SSG: 12
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