title: A distinct role of pectate lyases in the formation of feeding structures induced by cyst and root-knot nematodes.
abstract: Pectin in the primary plant cell wall is thought to be responsible for its porosity, charge density, and microfibril spacing and is the main component of the middle lamella. Plant-parasitic nematodes secrete cell wall-degrading enzymes that macerate the plant tissue, facilitating the penetration and migration within the roots. In sedentary endoparasitic nematodes, these enzymes are released only during the migration of infective juveniles through the root. Later, nematodes manipulate the expression of host plant genes, including various cell wall enzymes, in order to induce specific feeding sites. In this study, we investigated expression of two Arabidopsis pectate lyase-like genes (PLL), PLL18 (At3g27400) and PLL19 (At4g24780), together with pectic epitopes with different degrees of methylesterification in both syncytia induced by the cyst nematode Heterodera schachtii and giant cells induced by the root-knot nematode Meloidogyne incognita. We confirmed upregulation of PLL18 and PLL19 in both types of feeding sites with quantitative reverse-transcriptase polymerase chain reaction (RT-PCR) and in situ RT-PCR. Furthermore, the functional analysis of mutants demonstrated the important role of both PLL genes in the development and maintenance of syncytia but not giant cells. Our results show that both enzymes play distinct roles in different infected root tissues as well as during parasitism of different nematodes.
authors.forename: K
authors.initials: K
authors.lastname: Wieczorek
authors.forename: A
authors.initials: A
authors.lastname: Elashry
authors.forename: M
authors.initials: M
authors.lastname: Quentin
authors.forename: F M W
authors.initials: FM
authors.lastname: Grundler
authors.forename: B
authors.initials: B
authors.lastname: Favery
authors.forename: G J
authors.initials: GJ
authors.lastname: Seifert
authors.forename: H
authors.initials: H
authors.lastname: Bohlmann
mesh_terms: D000818:Animals; D017360:Arabidopsis / Q000166:cytology / Q000201:enzymology* / Q000235:genetics / Q000469:parasitology; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D005260:Female; D018506:Gene Expression Regulation, Plant; D017930:Genes, Reporter; D015726:Giant Cells / Q000166:cytology; D006790:Host-Parasite Interactions; D008297:Male; D016254:Mutagenesis, Insertional; D010641:Phenotype; D010935:Plant Diseases / Q000469:parasitology*; D018517:Plant Roots / Q000166:cytology / Q000201:enzymology / Q000235:genetics / Q000469:parasitology; D018520:Plant Shoots / Q000166:cytology / Q000201:enzymology / Q000235:genetics / Q000469:parasitology; D011133:Polysaccharide-Lyases / Q000235:genetics / Q000378:metabolism*; D036226:Seedlings / Q000166:cytology / Q000201:enzymology / Q000235:genetics / Q000469:parasitology; D013045:Species Specificity; D017187:Tylenchida / Q000166:cytology / Q000502:physiology*; D014431:Tylenchoidea / Q000166:cytology / Q000502:physiology*; D015854:Up-Regulation
chemical_list: D029681:Arabidopsis Proteins; D011133:Polysaccharide-Lyases; C023911:pectate lyase