Molecular and biochemical markers for monitoring dynamic shifts of cellulolytic protozoa in Reticulitermes flavipes

Wheeler, Marsha M.; Zhou, Xuguo; Scharf, Michael E.; Oi, Faith M.

doi:10.1016/j.ibmb.2007.09.010

Cited by 26 publications

(24 citation statements)

References 16 publications

(29 reference statements)

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“…These results of undetectable cellulase-producing bacteria from the Thai lower termites agree well with the previous reports that the lower termites do not use bacteria for degrading cellulose, but rather rely on protozoa to degrade cellulose to glucose [27][28][29]. Forty-seven from 57 of the bacterial isolates from the higher termites, Microcerotermes sp., showed clear zones on the culture plates, suggesting that cellulaseproducing bacteria presumably inhabit in termite guts as flora.…”

Section: Isolation Resultssupporting

confidence: 91%

Cellulase-Producing Bacteria from Thai Higher Termites, Microcerotermes sp.: Enzymatic Activities and Ionic Liquid Tolerance

Taechapoempol

Sreethawong

Rangsunvigit

et al. 2010

Appl Biochem Biotechnol

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The three highest hydrolysis-capacity-value isolates of Bacillus subtilis (A 002, M 015, and F 018) obtained from Thai higher termites, Microcerotermes sp., under different isolation conditions (aerobic, anaerobic, and anaerobic/aerobic) were tested for cellulase activities--FPase, endoglucanase, and β-glucosidase--at 37 °C and pH 7.2 for 24 h. Their tolerance to an ionic liquid, 1-butyl-3-methylimidazolium chloride ([BMIM]Cl), was also investigated. The results showed that the isolate M 015 provided the highest endoglucanase activity whereas the highest FPase and β-glucosidase activities were observed for the isolate F 018. The isolate F 018 also showed the highest tolerance to [BMIM]Cl in the range of 0.1-1.0 vol.%. In contrast, the isolate A 002 exhibited growth retardation in the presence of 0.5-1.0 vol.% [BMIM]Cl.

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Section: Isolation Resultssupporting

confidence: 91%

Cellulase-Producing Bacteria from Thai Higher Termites, Microcerotermes sp.: Enzymatic Activities and Ionic Liquid Tolerance

Taechapoempol

Sreethawong

Rangsunvigit

et al. 2010

Appl Biochem Biotechnol

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“…Cellulase activity assay protocols were executed as described previously (Zhou et al, 2007bWheeler et al, 2007). After Cell-1 dsRNA feeding assays, termites stored at À20 1C were homogenized using a motorized Teflon-glass tissue homogenizer in 0.1-M sodium acetate (pH 5.8).…”

Section: Cellulase Enzyme Activity Assaysmentioning

confidence: 99%

“…Two termite genes were specifically investigated as prototype targets for RNAi-based termiticides. The first gene encodes the Cell-1 salivary endoglucanase, which plays a central role in cellulose digestion (Scharf et al, 2003;Zhou et al, 2007b;Wheeler et al, 2007). Silencing of the Cell-1 gene resulted in both compromised group fitness and significant termite mortality.…”

Section: Overviewmentioning

confidence: 99%

“…This study was conducted to determine the feasibility of RNAi via feeding (Timmons and Fire, 1998) as a termiticidal mode of action, and to investigate two R. flavipes genes as potential termiticidal RNAi targets. These genes included (1) the Cell-1 gene, which encodes a digestive cellulase enzyme (Scharf et al, 2003;Zhou et al, 2007b;Wheeler et al, 2007) and (2) the Hex-2 gene, which encodes a casteregulatory hexamerin storage protein (Scharf et al, 2005aZhou et al, 2006bZhou et al, , c, 2007a. Gene silencing by siRNAs targeted to these two genes was previously documented using low-dose injection protocols (Zhou et al, 2006b).…”

Section: Introductionmentioning

confidence: 99%

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RNA interference in the termite Reticulitermes flavipes through ingestion of double-stranded RNA

Zhou

Wheeler

et al. 2008

Insect Biochemistry and Molecular Biology

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201

144

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“…Information on Cell-1 gene structure, features of the translated protein, tissue expression, and other gene and activity characteristics are provided in previous reports (Wheeler et al, 2007;Zhou et al, 2007Zhou et al, , 2008a. The primary goals of the current report were to compare BEVS-and E. coli-expressed proteins, and to characterize the activity and stability, as well as pH, temperature, and potential cofactor requirements of the recombinant insect-expressed protein.…”

Section: Background and Rationalementioning

confidence: 99%

Production and characterization of a recombinant beta‐1,4‐endoglucanase (glycohydrolase family 9) from the termite Reticulitermes flavipes

Zhou

Kovaleva²,

Wu-Scharf

et al. 2010

Arch Insect Biochem Physiol

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Cell-1 is a host-derived beta-1,4-endoglucanase (Glycohydrolase Family 9 [GHF9]) from the lower termite Reticulitermes flavipes. Here, we report on the heterologous production of Cell-1 using eukaryotic (Baculovirus Expression Vector System; BEVS) and prokaryotic (E. coli) expression systems. The BEVS-expressed enzyme was more readily obtained in solubilized form and more active than the E. coli-expressed enzyme. K(m) and V(max) values for BEVS-expressed Cell-1 against the model substrate CMC were 0.993% w/v and 1.056 micromol/min/mg. Additional characterization studies on the BEVS-expressed enzyme revealed that it possesses activity comparable to the native enzyme, is optimally active around pH 6.5-7.5 and 50-60 degrees C, is inhibited by EDTA, and displays enhanced activity up to 70 degrees C in the presence of CaCl(2). These findings provide a foundation on which to begin subsequent investigations of collaborative digestion by coevolved host and symbiont digestive enzymes from R. flavipes that include GHF7 exoglucanases, GHF1 beta glucosidases, phenol-oxidizing laccases, and others.

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Molecular and biochemical markers for monitoring dynamic shifts of cellulolytic protozoa in Reticulitermes flavipes

Cited by 26 publications

References 16 publications

Cellulase-Producing Bacteria from Thai Higher Termites, Microcerotermes sp.: Enzymatic Activities and Ionic Liquid Tolerance

Cellulase-Producing Bacteria from Thai Higher Termites, Microcerotermes sp.: Enzymatic Activities and Ionic Liquid Tolerance

RNA interference in the termite Reticulitermes flavipes through ingestion of double-stranded RNA

Production and characterization of a recombinant beta‐1,4‐endoglucanase (glycohydrolase family 9) from the termite Reticulitermes flavipes

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