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Identification and functional characterization of intracellular sialidase NeuA3 from Streptomyces avermitilis

Paper ID Volume ID Publish Year Pages File Format Full-Text
34332 45018 2015 7 PDF Available
Title
Identification and functional characterization of intracellular sialidase NeuA3 from Streptomyces avermitilis
Abstract

•The protein NeuA3 from Streptomyces avermitilis ATCC31267 was a novel intracellular sialidase.•NeuA3 preferentially cleaved α2,3- and α2,6-linked sialic acids from glycoconjugates.•NeuA3 efficiently converted crude polysialogangliosides from porcine brain to GM1.•NeuA3 treatment of human bladder cancer cells YTS-1 caused enhanced expression of GM1 on cell surface.

Sialidases (EC 3.2.1.18), glycosidases that cleave the linkages whereby sialic acids are attached to glycoconjugates, are found in most bacterial species. Because sialidases can convert polysialogangliosides to monosialoganglioside GM1, they have potential clinical application for treatment of human neurological and other disorders including Alzheimer's disease, Parkinson's disease, and spinal cord injury. Sialidases with high substrate specificity are desirable for more efficient GM1 production. In this study, the sialidase neuA3 gene from the non-pathogenic bacterium Streptomyces avermitilis, which is commonly used for industrial applications, was analyzed, cloned, and expressed in E. coli BL21 (DE3). Purified NeuA3 enzyme was characterized using 2′-(4-methylumbelliferyl)-α-d-N-acetylneuraminic acid (4-MUN) as a synthetic substrate. NeuA3 has a low molecular weight (∼38 kDa), showed strong stability in the presence of various divalent metal ions and temperature and pH values, preferentially cleaved α2,3- and α2,6-linked sialic acids from gangliosides, and efficiently converted crude porcine brain gangliosides to GM1. NeuA3 treatment of malignant human bladder cancer cells YTS-1 presented enhanced cell surface expression of GM1. The novel sialidase NeuA3 will be useful for functional studies of sialylated oligosaccharides and other sialoglycoconjugates, especially for studying the functions of GM1 in cancer research.

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Keywords
Sialidase; Streptomyces avermitilis; Monosialoganglioside GM1; Bladder cancer; Conversion
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Identification and functional characterization of intracellular sialidase NeuA3 from Streptomyces avermitilis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 50, Issue 5, May 2015, Pages 752–758
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us