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Molecular characterization and functional analysis of two new β‐1,4‐endoglucanase genes ( H a‐eng‐2 , H a‐eng‐3 ) from the cereal cyst nematode H eterodera avenae
Author(s) -
Long H.,
Peng D.,
Huang W.,
Peng H.,
Wang G.
Publication year - 2013
Publication title -
plant pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.928
H-Index - 85
eISSN - 1365-3059
pISSN - 0032-0862
DOI - 10.1111/ppa.12000
Subject(s) - biology , heterodera avenae , nematode , signal peptide , gene , heterodera , cellulase , parasitism , microbiology and biotechnology , recombinant dna , host (biology) , biochemistry , cellulose , genetics , ecology
Parasitism genes encoding secretory proteins expressed in the pharyngeal glands of plant‐parasitic nematodes play a crucial role in nematode parasitism of plants. Two new β‐1,4‐endoglucanase genes ( H a‐eng‐2 and H a‐eng‐3 ) expressed in the pharyngeal glands of the sedentary cyst nematode, H eterodera avenae , were cloned. Both of the predicted proteins have a putative signal peptide for secretion and a catalytic domain. Neither peptide linkers nor cellulose binding domains were present. In situ hybridization showed that the transcripts of H a‐eng‐2 and H a‐eng‐3 accumulated specifically in the two subventral gland cells of H . avenae . RT ‐ PCR analysis confirmed that their transcriptions were strong in the preparasitic and early parasitic second‐stage juveniles, and were undetectable at the late parasitic stages of the nematode. Cellulase activities of the recombinant proteins HA ‐ ENG ‐2 and HA ‐ ENG ‐3 were confirmed in vitro . K nocking down H a‐eng‐2 using RNA interference reduced nematode infectivity by 40%. The results indicate that these β‐1,4‐endoglucanases can be secreted into plant tissues and play an important role in the wall degradation of plant cells during penetration and the migration of second‐stage juveniles in host roots.