The ability of Gremmeniella abietina to hydrolyze polygalacturonic acid

Petäistö, Raija-Liisa; Kajander, E. Olavi

doi:10.1111/j.1439-0329.1993.tb00967.x

Cited by 7 publications

(6 citation statements)

References 12 publications

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“…No specific studies, however, are available on enzymes of spores or mycelium of C. pirolata, or in fact in related species to allow us to confirm these findings. Some pathogenic ascomycetes have been reported to excrete enzymes capable of hydrolyzing xylan (Petäistö et al 1992) and pectin, and further can induce polygalacturonase activity in vitro (Petäistö and Kajander 1993). Pectinase activities during pathogenesis are controlled through the physiological conditions of the host cells rather than those of fungi cells (Martin 1980).…”

Section: Discussionmentioning

confidence: 99%

Fungal injury to seed tissues of Norway spruce, Picea abies (L.) Karst.

Tillman-Sutela¹,

Kauppi

Hilli³

et al. 2004

Trees - Structure and Function

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Norway spruce bore an abundance of cones in Finland in 2000, but these cones were often fungalinfected. The seeds had structural injuries that were revealed when seed samples were examined using light (LM) and a field emission scanning electron microscope (FESEM). Two main types of spores were found either in the tissues inside the seed coat or on the sarcotesta, the outermost layer of seed coat. The spores of Chrysomyxa pirolata appeared particularly in the nucellar tissue, where the cell walls were disintegrated at the middle lamellae and cytoplasm was disrupted. Degenerated remnants of fungal structures resembling aecial peridium were found close to aeciospores. The tissue of the megagametophyte differed also from that of a normal mature seed. Conidia of Thysanophora penicillioides were often encountered on the sarcotesta where the ordinary wax cover was missing. Fungal injury occurred in the nucellar layers that shelter the embryo and megagametophyte from desiccation and oxidation. Destruction of these structures together with rapid opening of the seed coat advance deterioration of seeds during storage and may cause unexpected economic losses in forest plant production.

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Section: Discussionmentioning

confidence: 99%

Fungal injury to seed tissues of Norway spruce, Picea abies (L.) Karst.

Tillman-Sutela¹,

Kauppi

Hilli³

et al. 2004

Trees - Structure and Function

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“…Polygalacturonase activity was analysed from the culture fluids as described by PETAISTO and KAJANDER (1993), usmg polygalacturonic acid as substrate and galacturonic acid as the standard at a concentration of 5 /imol/ml-25 ^mol/ml. The galacturonic acid produced was measured using the dinitrosalicylic-acid (DNS) method (MiLLER 1959;BAILEY and PESSA 1990).…”

Section: Methodsmentioning

confidence: 99%

“…Gremmeniella abientina has been found to hydrolyse polygalacturonic acid in vitro and the activity is inducible by pectin (PETAISTO and KAJANDER 1993). To characterize the European and North American race of G. abietina, the polygalacturonic-acid hydrolysing activity produced in vitro (nmol galacturonic acid/mg mycelial dry weight) was compared between the European and North American race.…”

Section: Introductionmentioning

confidence: 99%

Capability of the European and North American race of Gremmeniella abietina to hydrolyse polygalacturonic acid in vitro

Petäistö

Lappi

1996

European Journal of Forest Pathology

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Polygalacturonase was found to be one of the first enzymes secreted by a pathogen during infection. The polygalacturonic-acid hydrolysing activity was compared between the North American and the European race of Gremmeniella abietina in vitro. Isolates were grown in pure pectin media from which the enzyme activity was analysed. Altogether, 29 isolates were tested in hve experiments (experimental runs in a growing chamber). The data were analysed using variance-component models that included fixed-race effects and random-experiment, isolate, flask and measurement effects. The European race secreted more poJygalacturonic-acid hydrolysing enzyme than the North American race and the mycelial dry weight produced was smaller for the European race. The differences between races were of the same order of magnitude as the variation between isolates within races; variance components relating to experimental errors were quite large. No correlation was found between the activity and mycelial dry-matter production within the races. Logarithmic transformation removed the apparent racial differences in the variabihty of the activity and mycelial dry weight. Results from the additionally tested A-and B-type of Fmnish isolates indicated differences in dry-matter production.

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“…Herron et al 2000). Previous reports (Petäistö and Kajander 1993;Petäistö and Lappi 1996) have proposed that both races (EU and NA) of GAA could potentially secrete at least one enzyme with polygalacturonase activity because G. abietina can grow on a medium with pectin as a sole carbon source. Pectin degradation in the susceptible P. resinosa was also clearly reported using two monoclonal antibodies, JIM-5 and JIM-7, specific to pectin with varying degrees of esterification (Ylimartimo et al 1997).…”

Section: Anti-b-13-glucansmentioning

confidence: 98%

“…This pathogen penetrates its hosts through stomata (Ylimartimo et al 1997) but soon has to deal with various cell walls in order to colonize the host further. In vitro studies revealed that G. abietina is surrounded by an extracellular sheath (ES) containing chitin, galactose, proteins, lipids and polygalacturonic acids (Benhamou and Ouellette 1987a,b) and that it could produce several enzymes such as cellulase, glucanase, xylanase and polygalacturonase (Petäistö et al 1992(Petäistö et al , 1994Petäistö and Kajander 1993;Petäistö and Lappi 1996). Using histo-and cytochemical tests, significant progress has been made in understanding host-pathogen interactions involving G. abietina.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic interactions between Gremmeniella abietina var. abietina, European race, and two resistant hosts, Pinus banksiana and P. contorta

2012

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Summary Ultrastructural observations showed that the European race of Gremmeniella abietina var. abietina can secrete several cell wall–degrading enzymes that help the invasion of Pinus banksiana and P. contorta shoot tip tissues. Alterations in the content or distribution of cellulose were obvious, indicating that colonization might be achieved primarily through the action of glucanases. Polygalacturonases seemed more abundant in the cortex and the phloem of the stem, suggesting they are among the first enzymes secreted by the pathogen during infection. Production of laccases and peroxidases was also revealed but always close to fungal cells or in areas where host wall degradation was obvious. In places where there was an accumulation of phenolic compounds in the infected zones of the shoot, particularly in or near the transition zone, immunolocalization of both enzymes was limited or absent. Laccases and polygalacturonases were regularly detected over the extracellular sheath of G. abietina, and this indicates that the sheath could play a significant role during host wall degradation. Finally, examination of G. abietina wall constituents, such as chitin and β‐1,3‐glucans, suggests that the composition of the pathogen wall changes during the infection process. This change may be associated with the secretion of fungal enzymes but could also be linked to host reactions altering the integrity of pathogen cell walls.

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The ability of Gremmeniella abietina to hydrolyze polygalacturonic acid

Abstract: Gremmeniella ahietina grew well in media with pectin as the sole carbon source. The fungus secreted at least one enzyme with polygalacturonase activity, and this was induced by addition of pectin to the culture medium.

Cited by 7 publications

References 12 publications

Fungal injury to seed tissues of Norway spruce, Picea abies (L.) Karst.

Fungal injury to seed tissues of Norway spruce, Picea abies (L.) Karst.

Capability of the European and North American race of Gremmeniella abietina to hydrolyse polygalacturonic acid in vitro

Enzymatic interactions between Gremmeniella abietina var. abietina, European race, and two resistant hosts, Pinus banksiana and P. contorta

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