Document Detail

Identification of an extracellular acid trehalase and its gene involved in fungal pathogenesis of Metarizium anisopliae.
MedLine Citation:
PMID:  16980715     Owner:  NLM     Status:  MEDLINE    
Trehalose is the main sugar in the haemolymph of insects and is a key nutrient source for an insect pathogenic fungus. Secretion of trehalose-hydrolysing enzymes may be a prerequisite for successful exploitation of this resource by the pathogen. An acid trehalase [EC] was purified to homogeneity from a culture of a locust-specific pathogen, Metarhizium anisopliae, and its properties were characterized. The gene (ATM1) of this acid trehalase was also isolated. The pure enzyme can efficiently hydrolyze haemolymph trehalose into glucose in vitro. The new acid trehalase appearing in the haemolymph of Locusta migratoria infected with M. anisopliae had the same pI and substrate specificity as the purified fungal acid trehalase, and the concentration of trehalose in the haemolymph decreased sharply after infection. RT-PCR also revealed the ATM1 gene's expression in the haemolymph of the infected insects. Our results indicated that the acid trehalase may serve as an "energy scavenger" and deplete blood trehalose during fungal pathogenesis.
Hua Zhao; Anthony Keith Charnley; Zhongkang Wang; Youping Yin; Zhenlun Li; Yanling Li; Yueqing Cao; Guoxiong Peng; Yuxian Xia
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  140     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  2006 Sep 
Date Detail:
Created Date:  2006-09-18     Completed Date:  2007-01-16     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  319-27     Citation Subset:  IM    
Genetic Engineering Research Center, Bioengineering College, Chongqing University, Chongqing, P.R. China 400030.
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MeSH Terms
Amino Acid Sequence
Base Sequence
DNA Primers
Electrophoresis, Polyacrylamide Gel
Extracellular Fluid / enzymology*
Isoelectric Focusing
Locusta migratoria / microbiology*
Metarhizium / enzymology*
Molecular Sequence Data
Reverse Transcriptase Polymerase Chain Reaction
Sequence Alignment
Sequence Analysis, DNA
Substrate Specificity
Trehalase / genetics*
Reg. No./Substance:
0/DNA Primers; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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