title: Expression of two functionally distinct plant endo-beta-1,4-glucanases is essential for the compatible interaction between potato cyst nematode and its hosts.
abstract: For the proliferation of their feeding sites (syncytia), the potato cyst nematode Globodera rostochiensis is thought to recruit plant endo-beta-1,4-glucanases (EGases, EC. 3.2.1.4). Reverse-transcription polymerase chain reaction experiments on tomato (Solanum lycopersicum) indicated that the expression of two out of the at least eight EGases, namely Sl-cel7 and Sl-cel9C1, is specifically upregulated during syncytium formation. In situ hybridization and immunodetection studies demonstrated that both EGases are specifically expressed inside and adjacent to proliferating syncytia. To assess the importance of Sl-cel7 and Sl-cel9C1 for nematode development, we decided to knock them out individually. Sl-cel9C1 probably is the only class C EGase in tomato, and we were unable to regenerate Sl-cel9C1-silenced plants. Potato (S. tuberosum), a close relative of tomato, harbors at least two class C EGases, and St-cel7-or St-cel9C1-silenced potato plants showed no obvious aberrant phenotype. Infection with potato cyst nematodes resulted in a severe reduction of the number of adult females (up to 60%) and a sharp increase in the fraction of females without eggs (up to 89%). Hence, the recruitment of CEL7, an enzyme that uses xyloglucan and noncrystalline cellulose as natural substrates, and CEL9C1, an enzyme that uses crystalline cellulose, is essential for growth and development of potato cyst nematodes.
authors.affiliation: Laboratory of Nematology, Department of Plant Sciences, Wageningen University, Binnenhaven 5, 6709 PD Wageningen, The Netherlands.
authors.forename: Aneta
authors.initials: A
authors.lastname: Karczmarek
authors.forename: Sylwia
authors.initials: S
authors.lastname: Fudali
authors.forename: Malgorzata
authors.initials: M
authors.lastname: Lichocka
authors.forename: Miroslaw
authors.initials: M
authors.lastname: Sobczak
authors.forename: Wojciech
authors.initials: W
authors.lastname: Kurek
authors.forename: Slawomir
authors.initials: S
authors.lastname: Janakowski
authors.forename: Jan
authors.initials: J
authors.lastname: Roosien
authors.forename: Wladyslaw
authors.initials: W
authors.lastname: Golinowski
authors.forename: Jaap
authors.initials: J
authors.lastname: Bakker
authors.forename: Aska
authors.initials: A
authors.lastname: Goverse
authors.forename: Johannes
authors.initials: J
authors.lastname: Helder
mesh_terms: D000818:Animals; D002480:Cellulase / Q000235:genetics / Q000378:metabolism*; D005260:Female; D015971:Gene Expression Regulation, Enzymologic; D018506:Gene Expression Regulation, Plant; D006790:Host-Parasite Interactions; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D018551:Solanum lycopersicum / Q000201:enzymology* / Q000235:genetics / Q000469:parasitology; D009348:Nematoda / Q000254:growth & development / Q000502:physiology*; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D018517:Plant Roots / Q000201:enzymology / Q000235:genetics / Q000469:parasitology; D030821:Plants, Genetically Modified; D020133:Reverse Transcriptase Polymerase Chain Reaction; D011198:Solanum tuberosum / Q000201:enzymology / Q000235:genetics / Q000469:parasitology
chemical_list: D007527:Isoenzymes; D010940:Plant Proteins; D002480:Cellulase