Cloning of the gene Lecanicillium psalliotae chitinase Lpchi1 and identification of its potential role in the biocontrol of root-knot nematode Meloidogyne incognita

The nematophagous fungus Lecanicillium psalliotae (syn. Verticillium psalliotae) is a well-known biocontrol agent. In this study, a chitinase gene Lpchi1 was isolated for the first time from L. psalliotae using degenerate primers and DNA-walking technique. The cloned gene Lpchi1 encoding 423 amino a...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 2007-10, Vol.76 (6), p.1309-1317
Main Authors: Gan, Zhongwei, Yang, Jinkui, Tao, Nan, Liang, Lianming, Mi, Qili, Li, Juan, Zhang, Ke-Qin
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Base Sequence
Biological and medical sciences
Biological control
Biotechnology
Chitinase
Chitinases - genetics
Chitinases - metabolism
Chitinases - pharmacology
Cloning
Cloning, Molecular
Deoxyribonucleic acid
DNA
Expression
Fundamental and applied biological sciences. Psychology
Fungal Proteins - genetics
Fungal Proteins - metabolism
Gene Expression Regulation, Fungal
Lecanicillium psalliotae
Meloidogyne incognita
Microbiology
Molecular Sequence Data
Nematoda
Ovum - drug effects
Pathogens
Peptide Hydrolases - metabolism
Peptide Hydrolases - pharmacology
Pest Control, Biological
Phylogeny
Pichia pastoris
Proteins
Tylenchoidea - drug effects
Verticillium
Verticillium - enzymology
Verticillium - genetics
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Summary:The nematophagous fungus Lecanicillium psalliotae (syn. Verticillium psalliotae) is a well-known biocontrol agent. In this study, a chitinase gene Lpchi1 was isolated for the first time from L. psalliotae using degenerate primers and DNA-walking technique. The cloned gene Lpchi1 encoding 423 amino acid residues shares a high degree of homology with other pathogenicity-related chitinases from entomopathogenic and mycoparasitic fungi. The complementary DNA sequence of the mature chitinase was amplified via reverse transcription polymerase chain reaction and expressed well in Pichia pastoris GS115. Through gel filtration, the recombinant chitinase was purified as a protein of ca. 45 kDa with an optimal activity at pH 7.0 and 37.6°C. The purified chitinase LPCHI1 was found degrading chitinous components of eggs of the root-knot nematode Meloidogyne incognita and significantly influence its development. Moreover, our results also demonstrate that the protease Ver112 and the chitinase LPCHI1 from the same fungus interacted on the egg infection.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-007-1111-9