Isolation and Heterologous Expression of a Polygalacturonase Produced by Fusarium oxysporum f. sp. cubense Race 1 and 4

Dong, Zhangyong; Wang, Zhenzhong

doi:10.3390/ijms16047595

Cited by 14 publications

(12 citation statements)

References 28 publications

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“…Thus, our results suggest that the expression of genes encoding CWDEs in Foc during infection could be properly stimulated under in vitro growth conditions in the presence of host cell wall. In previous studies, the activity of polygalacturonases (PGs) and pectate lyases has been detected in the culture supernatant when Foc is grown in media containing pectin, which is also in agreement with our results (Dong and Wang 2010, 2015; Dong et al 2011). …”

Section: Discussionsupporting

confidence: 93%

Comparative Transcriptomic Analysis of Race 1 and Race 4 of Fusarium oxysporum f. sp. cubense Induced with Different Carbon Sources

Qin

et al. 2017

G3 Genes|Genomes|Genetics

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The fungal pathogen Fusarium oxysporum f. sp. cubense causes Fusarium wilt, one of the most destructive diseases in banana and plantain cultivars. Pathogenic race 1 attacks the “Gros Michel” banana cultivar, and race 4 is pathogenic to the Cavendish banana cultivar and those cultivars that are susceptible to Foc1. To understand the divergence in gene expression modules between the two races during degradation of the host cell wall, we performed RNA sequencing to compare the genome-wide transcriptional profiles of the two races grown in media containing banana cell wall, pectin, or glucose as the sole carbon source. Overall, the gene expression profiles of Foc1 and Foc4 in response to host cell wall or pectin appeared remarkably different. When grown with host cell wall, a much larger number of genes showed altered levels of expression in Foc4 in comparison with Foc1, including genes encoding carbohydrate-active enzymes (CAZymes) and other virulence-related genes. Additionally, the levels of gene expression were higher in Foc4 than in Foc1 when grown with host cell wall or pectin. Furthermore, a great majority of genes were differentially expressed in a variety-specific manner when induced by host cell wall or pectin. More specific CAZymes and other pathogenesis-related genes were expressed in Foc4 than in Foc1 when grown with host cell wall. The first transcriptome profiles obtained for Foc during degradation of the host cell wall may provide new insights into the mechanism of banana cell wall polysaccharide decomposition and the genetic basis of Foc host specificity.

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Section: Discussionsupporting

confidence: 93%

Comparative Transcriptomic Analysis of Race 1 and Race 4 of Fusarium oxysporum f. sp. cubense Induced with Different Carbon Sources

Qin

et al. 2017

G3 Genes|Genomes|Genetics

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“…Previously, one endo-PG, Pgc1 (GenBank Accession no. GI: 223960661) and two exo-PGs, Pgc2 and Pgc3, have been reported in Foc4 [9,10]. In this study, we purified and isolated a novel exo-PG named Pgc4.…”

Section: Discussionmentioning

confidence: 96%

“…It is mainly composed of pectin, cellulose, and hemicellulose. Some CAZymes secreted by Foc4 have been proved to be important pathogenicity factors during infection [9,10]. Many studies have been conducted to compare the differences between Foc1 and Foc4 to explore the important pathogenic genes specific to Foc4 [11,12].…”

Section: Introductionmentioning

confidence: 99%

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An Exo-Polygalacturonase Pgc4 Regulates Aerial Hyphal Growth and Virulence in Fusarium oxysporum f. sp. cubense race 4

Dong

Luo

Wang

2020

IJMS

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Fusarium oxysporum f. sp. cubense race 4 (Foc4) causes Fusarium wilt that affects banana plants, and hence, the molecular mechanisms of its virulence need to be investigated. We purified an exo-polygalacturonase (exo-PG), Pgc4, from Foc4. Pgc4 has an apparent molecular weight of 50.87 kDa based on sodium dodecyl sulphate–polyacrylamide gel electrophoresis. We further performed its sequence analysis and biochemical characterization. The two pgc4 genes encoding Pgc4 from Foc4 and Foc1 were 1434 bp in length and encoded 477 amino acids with differences, due to some nucleotide differences between the two. The Km and Vmax values of Pgc4 purified from Foc4 were determined to be 0.45 mg/mL and 105.26 Units·mg·protein−1 ·min−1, respectively. The recombinant proteins, r-Foc1-Pgc4 and r-Foc4-Pgc4, were expressed and purified from Pichia pastoris and showed optimal Pgc4 activity at 55 °C and pH 4.0; both could induce tissue maceration and necrosis in the “Guangfen-1” and “Baxi” varieties of banana but to a different extent. Phenotypic assays and complementation analyses revealed that, compared to the wild-type, the generated Foc4Δpgc4 mutant strain showed a lower aerial hyphal growth, grew slower, and had a reduced virulence. Therefore, our results demonstrate the function of Pgc4 as a pathogenicity factor of Foc4.

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“…Polygalacturonase represents an attractive functional enzyme to be applied in the production of small oligomers of PGA (Kong & Singh, 2016), and fermented beverages and fruit juices (Carrasco, Rozas, Alcaino, Cifuentes, & Baeza, 2019). Endo-polygalacturonase was widely reported in Aspergillus species (Abdulrachman et al, 2017;Fratebianchi, Cavello, & Cavalitto, 2017;Wang et al, 2017), Penicillium (Amin, Bhatti, Bilal, & Asgher, 2017), Botrytis (Rowe & Kliebenstein, 2007), Sclerotinia (Bashi, Rimmer, Khachatourians, & Hegedus, 2013) and Fusarium (Dong & Wang, 2015) species, etc.…”

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confidence: 99%

Identification and characterization of thermostable endo‐polygalacturonase II B from Aspergillus luchuensis

et al. 2020

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Endo‐polygalacturonase II B (PgaB) from Aspergillus luchuensis was orthologous to endo‐polygalacturonase from Aspergillus niger with mutant sites Thr42Ser and Glu52Ala. Mature pgaB gene was cloned from the genomic DNA of A. luchuensis and secreted expressed with over 90% purity in Pichia Pastoris and reached 1.0 g/L after 144 hr culture. The recombinant PgaB was further purified by Ni‐NTA chromatography. Using polygalacturonic acid (PGA) as substrate, the optimal condition for PgaB activity was 40°C and pH 4.5, respectively. Km and Vmax of PgaB were 0.19 mmol/l and 103.58 μmol min−1 mg−1, respectively. The relative activity of PgaB remained more than 60% and 40% of maximum activity at 50 and 60°C for 7 hr. PgaB increased the light transmittance by 85% and showed high efficiency in juice clarification. The main product was galacturonic acid oligosaccharides with degrees of polymers (DP) 1–3. The PgaB is a potential pectinolytic enzyme in food industries. Practical applications Endo‐polygalacturonase II B (PgaB) was identified from Aspergillus luchuensis, a filamentous fungus widely used in food and beverage fermentation in East Asia. PgaB still kept its most activity at 60°C for 7 hr. Polygalacturonic acid (PGA) can be digested effectively by the PgaB and the main products are galacturonic acid oligosaccharides with degrees of polymers (DP) 1–3. PgaB shows high efficiency in juice clarification. The PgaB is a potential pectinolytic enzyme for the applications in food industries.

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Isolation and Heterologous Expression of a Polygalacturonase Produced by Fusarium oxysporum f. sp. cubense Race 1 and 4

Cited by 14 publications

References 28 publications

Comparative Transcriptomic Analysis of Race 1 and Race 4 of Fusarium oxysporum f. sp. cubense Induced with Different Carbon Sources

Comparative Transcriptomic Analysis of Race 1 and Race 4 of Fusarium oxysporum f. sp. cubense Induced with Different Carbon Sources

An Exo-Polygalacturonase Pgc4 Regulates Aerial Hyphal Growth and Virulence in Fusarium oxysporum f. sp. cubense race 4

Identification and characterization of thermostable endo‐polygalacturonase II B from Aspergillus luchuensis

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