The role of a phospholipase (PLD) in virulence of Purpureocillium lilacinum (Paecilomyces lilacinum)
Microbial Pathogenesis • 2015
Publication Information
Authors
Fan Yang; Hazem Abdelnabby; Yannong Xiao
Keywords
Purpureocillium lilacinum
Phospholipase D (PLD)
Leucinostatins A
Meloidogyne incognita
Journal
Microbial Pathogenesis
Publisher
Elsevier
Volume
85
Issue
Not Available
Pages
11-20
publication.type
International
Paper Link
Open Link
Supplementary Materials
Not Available
Abstract
Phospholipases are key enzymes in pathogenic fungi that cleave host phospholipids, resulting in
membrane destabilization and host cell penetration. However, understanding the role of phospholipases
on the virulence of the filamentous fungus Purpureocillium lilacinum has been still rather limited. In this
study, pld gene was characterized. It encodes the protein phospholipase D (PLD) in P. lilacinum. This gene,
3303 bp open reading frame fragment (ORF), encodes a protein of 1100 amino acids with high similarity
to the same gene from Penicillium oxalicum and Aspergillus fumigatus. Secondary structure prediction
showed two PLD phosphodiesterase domains (437e464 bp and 885e912 bp). The pld gene was significantly
regulated during infection of Meloidogyne incognita eggs by P. lilacinum. The expression of pld
gene using RT-PCR was the highest at 36 and 48 h, which introduce evidence that the presence of
M. incognita may induce the expression of the pld gene in P. lilacinum. In addition, maltose and L-alanine
were found to increase the expression of pld gene. An acidic environment (pH 3.0e4.0) and moderate
temperatures (27e29 C) are favorable for pld expression in P. lilacinum.
membrane destabilization and host cell penetration. However, understanding the role of phospholipases
on the virulence of the filamentous fungus Purpureocillium lilacinum has been still rather limited. In this
study, pld gene was characterized. It encodes the protein phospholipase D (PLD) in P. lilacinum. This gene,
3303 bp open reading frame fragment (ORF), encodes a protein of 1100 amino acids with high similarity
to the same gene from Penicillium oxalicum and Aspergillus fumigatus. Secondary structure prediction
showed two PLD phosphodiesterase domains (437e464 bp and 885e912 bp). The pld gene was significantly
regulated during infection of Meloidogyne incognita eggs by P. lilacinum. The expression of pld
gene using RT-PCR was the highest at 36 and 48 h, which introduce evidence that the presence of
M. incognita may induce the expression of the pld gene in P. lilacinum. In addition, maltose and L-alanine
were found to increase the expression of pld gene. An acidic environment (pH 3.0e4.0) and moderate
temperatures (27e29 C) are favorable for pld expression in P. lilacinum.
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