NDLI: Enzymatic and biological characteristics of enolase in Brucella abortus A19

Content Provider	Springer Nature Link
Author	Han, Xiangan Ding, Chan Chen, Hongjun Hu, Qinghai Yu, Shengqing
Copyright Year	2011
Abstract	Brucella abortus is the etiological agent of brucellosis, a disease causing human public health problems as well as major economic losses in domestic animal industries. In this study, the enolase gene of B. abortus A19 was cloned, sequenced and expressed in Escherichia coli BL21. Bacterial-expressed enolase protein (His-eno) was purified and its ability to catalyze the conversion of 2-phosphoglycerate (2-PGE) to phosphoenolpyruvate (PEP) (hereon referred to as enolase activity) was analyzed. Michaelis constant (K $_{ m }$) and maximum reaction velocity (V $_{ max }$) of the reaction was determined to be 2.0 × 10$^{−3}$ M and 178 μM l$^{−1 }$min$^{−1}$, respectively. Factors influencing the enolase activity of His-eno, such as pH, the presence of metal ions and temperature were investigated in vitro. The results showed that His-eno exhibited maximal enolase activity in pH 8.5 reaction buffer containing 10 mM MgSO$_{4}$ at 37°C. In addition to studying the enzyme activity, binding assays were performed to provide insights into the function of His-eno on pathogenesis and immunity. His-eno exhibits fibronectin-binding ability in immunoblotting assay, suggesting that enolase may play a role in B. abortus colonization, persistence, and invasion of host tissue. Furthermore, Western blot demonstrated His-eno’s binding ability to 34 bovine B. abortus positive sera, suggesting that future studies may find enolase a useful as a diagnostic marker or a vaccine candidate for brucellosis.
Starting Page	2705
Ending Page	2711
Page Count	7
File Format	PDF
ISSN	03014851
Journal	Molecular Biology Reports
Volume Number	39
Issue Number	3
e-ISSN	15734978
Language	English
Publisher	Springer Netherlands
Publisher Date	2011-06-15
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Brucella abortus A19 Enolase Enzyme activity Fibronectin-binding ability Animal Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Genetics Medicine Molecular Biology

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