PMID- 20405036
OWN - NLM
STAT- MEDLINE
DCOM- 20110616
LR  - 20211020
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 5
IP  - 4
DP  - 2010 Apr 12
TI  - Different functions of the insect soluble and membrane-bound trehalase genes in 
      chitin biosynthesis revealed by RNA interference.
PG  - e10133
LID - 10.1371/journal.pone.0010133 [doi]
LID - e10133
AB  - BACKGROUND: Trehalase, an enzyme that hydrolyzes trehalose to yield two glucose 
      molecules, plays a pivotal role in various physiological processes. In recent 
      years, trehalase proteins have been purified from several insect species and are 
      divided into soluble (Tre-1) and membrane-bound (Tre-2) trehalases. However, no 
      functions of the two trehalases in chitin biosynthesis in insects have yet been 
      reported. PRINCIPAL FINDINGS: The membrane-bound trehalase of Spodoptera exigua 
      (SeTre-2) was characterized in our laboratory previously. In this study, we 
      cloned the soluble trehalase gene (SeTre-1) and investigated the tissue 
      distribution and developmental expression pattern of the two trehalase genes. 
      SeTre-1 was expressed highly in cuticle and Malpighian tubules, while SeTre-2 was 
      expressed in tracheae and fat body. In the midgut, the two trehalase genes were 
      expressed in different locations. Additionally, the expression profiles of both 
      trehalase mRNAs and their enzyme activities suggest that they may play different 
      roles in chitin biosynthesis. The RNA interference (RNAi) of either SeTre-1 or 
      SeTre-2 was gene-specific and effective, with efficiency rates up to 83% at 72 h 
      post injection. After RNAi of SeTre-1 and SeTre-2, significant higher mortality 
      rates were observed during the larva-pupa stage and pupa-adult stage, and the 
      lethal phenotypes were classified and analyzed. Additionally, the change trends 
      of concentration of trehalose and glucose appeared reciprocally in RNAi-mutants. 
      Moreover, knockdown of SeTre-1 gene largely inhibited the expression of chitin 
      synthase gene A (CHSA) and reduced the chitin content in the cuticle to 
      two-thirds relative to the control insects. The chitin synthase gene B (CHSB) 
      expression, however, was inhibited more by the injection of dsRNA for SeTre-2, 
      and the chitin content in the midgut decreased by about 25%. CONCLUSIONS: SeTre-1 
      plays a major role in CHSA expression and chitin synthesis in the cuticle, and 
      SeTre-2 has an important role in CHSB expression and chitin synthesis in the 
      midgut.
FAU - Chen, Jie
AU  - Chen J
AD  - State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen 
      University, Guangzhou, China.
FAU - Tang, Bin
AU  - Tang B
FAU - Chen, Hongxin
AU  - Chen H
FAU - Yao, Qiong
AU  - Yao Q
FAU - Huang, Xiaofeng
AU  - Huang X
FAU - Chen, Jing
AU  - Chen J
FAU - Zhang, Daowei
AU  - Zhang D
FAU - Zhang, Wenqing
AU  - Zhang W
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100412
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
RN  - 0 (RNA, Small Interfering)
RN  - 1398-61-4 (Chitin)
RN  - EC 2.4.1.16 (Chitin Synthase)
RN  - EC 3.2.1.28 (Trehalase)
SB  - IM
MH  - Animals
MH  - Chitin/*biosynthesis
MH  - Chitin Synthase/genetics
MH  - Gene Expression Profiling
MH  - Insecta
MH  - *RNA Interference
MH  - RNA, Small Interfering/pharmacology
MH  - Solubility
MH  - Spodoptera/enzymology/genetics
MH  - Tissue Distribution
MH  - Trehalase/*genetics
PMC - PMC2853572
COIS- Competing Interests: The authors have declared that no competing interests exist.
EDAT- 2010/04/21 06:00
MHDA- 2011/06/17 06:00
PMCR- 2010/04/12
CRDT- 2010/04/21 06:00
PHST- 2010/01/30 00:00 [received]
PHST- 2010/03/22 00:00 [accepted]
PHST- 2010/04/21 06:00 [entrez]
PHST- 2010/04/21 06:00 [pubmed]
PHST- 2011/06/17 06:00 [medline]
PHST- 2010/04/12 00:00 [pmc-release]
AID - 10-PONE-RA-15921R1 [pii]
AID - 10.1371/journal.pone.0010133 [doi]
PST - epublish
SO  - PLoS One. 2010 Apr 12;5(4):e10133. doi: 10.1371/journal.pone.0010133.