1. IntroductionPhosphopyruvate hydr

1. Introduction
Phosphopyruvate hydratase, also known as 14-3-2 protein, 2-phosphoglycerate dehydratase or enolase, is involved in glycolysis and catalyzing the conversion of 2-phosphoglycerate to phosphoenolpyruvate (Bruns and Gerald, 1976). A previous study has reported that the expression of this metabolic enzyme is increased in blood cancer cells (Lopez-Pedrera et al., 2006). Another study found that its expression is decreased in ovarian cancer cells treated by antitumor drug (Li et al., 2005). These reports suggest that NaBu, which is a well-known antitumor agent, down-regulated the expression of enolase and hindered cell growth. Enolase is a housekeeping gene related to energy production, and it shows obvious changes to hypoxic stress in shrimp (Boonchuoy et al., 1999). Another study reported that NaBu treatment could decrease the enolase expression level in Fenneropenaeus chinensis by over twofold ( Jiang et al., 2009). Enolase was also found to act as a novel IgE reactive protein in prawn (Tomm et al., 2013).

Recent studies have verified that enolase activates plasminogen, is involved in the processes of parasite infection and migration (Fox and Smulian, 2001 and Bao et al., 2014), and contributes to parasite survival by preventing parasites from the immune attack of the host (Liu et al., 2012 and Nogueira et al., 2012). Current advances in research have demonstrated the diagnostic potential of enolase parasitic diseases, as well as its importance in drug development and as a vaccine target (Chen et al., 2012 and Manneck et al., 2012). Furthermore, the important role of enolase in other microbes has already been established. Viruses do need to utilize host cell components in their infection but bacteria do not need to use host cell components as bacterial enolase exists. The DNA methyltransferase of the Escherichia coli bacteriophage T1 appears to interact with E. coli enolase upon infection ( Gassner et al., 1998). Recently, some research reports have showed that enolase is critical for infection and enhances bacterial survival. Vibrio parahaemolyticus enolase, which has plasminogen-binding activity, is an adhesion-related factor and plays an important role in pathogenicity ( Jiang et al., 2014). As collagen is a target of pathogens for adhesion, colonization, and invasion of host tissue, enolase can act as a collagen-binding protein in Lactobacillus plantarum ( Salzillo et al., 2015). Streptococcus canis enolase has shown to significantly enhance bacterial survival in phagocytosis analyses using human neutrophils ( Fulde et al., 2013). In fungi, the extracellular enolase of Candida albicans has been shown to mediate colonization on its primary translocation site. As enolase functions as a glycolytic enzyme and extracellular peptide, it is a remarkable example of gene sharing in fungi ( Silva et al., 2014). In invertebrates, host enolase has been reported to be involved in viral infection. Bombyx mori enolase may play an important role in intracellular transportation of B. mori nucleopolyhedrovirus (BmNPV) ( Cheng et al., 2014). In addition, mosquito enolase has been also reported to bind to West Nile and dengue virus envelope and capsid proteins, respectively ( Colpitts et al., 2011 and Munoz Mde et al., 2013).

In this study, the enolase sequence of M. japonicus was cloned and characterized. The expression profile of enolase in different tissues was studied by quantitative real-time PCR (qRT-PCR). The role of enolase on the innate immunity of shrimp was investigated by RNA interference and challenge experiments. The data from this study will improve our knowledge of the functions of enolase.

ผลลัพธ์ (อังกฤษ) 2:

1. Introduction
Phosphopyruvate hydratase, also Known as 14-3-2 protein, 2-phosphoglycerate Dehydratase or enolase, is involved in glycolysis and catalyzing the conversion of 2-phosphoglycerate to Phosphoenolpyruvate (Bruns and Gerald, the 1,976th). A previous study has reported that the expression of this metabolic enzyme is increased in blood cancer cells (Lopez-Pedrera et al., 2006). Another study found that its expression is decreased in ovarian cancer cells treated by antitumor drug (Li et al., 2005). These reports suggest that NaBu, which is a well-known antitumor agent, down-regulated the expression of enolase and hindered cell growth. Enolase is a housekeeping gene related to energy production, and it shows obvious changes to hypoxic stress in shrimp (Boonchuoy et al., 1999). Another study reported that NaBu treatment could decrease the enolase expression level in Fenneropenaeus chinensis by over twofold (Jiang et al., 2009). Enolase was also Found to Act as a novel IgE reactive protein in Prawn (Tomm et al., 2013th). Recent Studies have Verified that enolase activates plasminogen, is involved in the processes of parasite infection and Migration (Fox and Smulian, 2,001th and Bao. et al., 2014), and contributes to parasite survival by preventing parasites from the immune attack of the host (Liu et al., 2012 and Nogueira et al., 2012). Current advances in research have demonstrated the diagnostic potential of enolase parasitic diseases, as well as its importance in drug development and as a vaccine target (Chen et al., 2012 and Manneck et al., 2012). Furthermore, the important role of enolase in other microbes has already been established. Viruses do need to utilize host cell components in their infection but bacteria do not need to use host cell components as bacterial enolase exists. The DNA methyltransferase of the Escherichia coli bacteriophage T1 appears to interact with E. coli enolase upon infection (Gassner et al., 1998). Recently, some research reports have showed that enolase is critical for infection and enhances bacterial survival. Vibrio parahaemolyticus enolase, which has plasminogen-binding activity, is an adhesion-related factor and plays an important role in pathogenicity (Jiang et al., 2014). As collagen is a target of pathogens for adhesion, colonization, and invasion of host tissue, enolase can act as a collagen-binding protein in Lactobacillus plantarum (Salzillo et al., 2015). Streptococcus canis enolase has shown to significantly enhance bacterial survival in phagocytosis analyses using human neutrophils (Fulde et al., 2013). In fungi, the extracellular enolase of Candida albicans has been shown to mediate colonization on its primary translocation site. As enolase functions as a glycolytic enzyme and extracellular peptide, it is a remarkable example of gene sharing in fungi (Silva et al., 2014). In invertebrates, host enolase has been reported to be involved in viral infection. Bombyx mori enolase may play an important role in intracellular transportation of B. mori nucleopolyhedrovirus (BmNPV) (Cheng et al., 2014). In addition, Mosquito enolase has also been reported to bind to West Nile and Dengue Virus Envelope Proteins and capsid, respectively (Colpitts et al., 2011th and Munoz et al Mde., 2013th). In this Study, the enolase Sequence of M. japonicus was cloned and characterized. The expression profile of enolase in different tissues was studied by quantitative real-time PCR (qRT-PCR). The role of enolase on the innate immunity of shrimp was investigated by RNA interference and challenge experiments. The data from this study will improve our knowledge of the functions of enolase.