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Neuraminidase (sialidase) from Aeromonas sp. strain 40/02 – isolation and partial purification

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Abstract

Neuraminidase is a virulence factor in many viruses and pathogenic bacteria. There are few reports of the detection of neuraminidase in the Aeromonas genus, but they do not include biochemical studies on the enzyme. In this work the neuraminidase production of Aeromonas sp. 40/02 strain and some properties of the enzyme were investigated for the first time. Neuraminidase was found in the supernatant, as well as in the cytosolic and membrane fractions of disrupted cells. It was demonstrated that the enzyme production is induced by a number of compounds structurally related to sialic acid. New data on the presence of extracellular and intracellular N-acylneuraminate lyase were obtained, suggesting a nutritional role of sialometabolism in this strain. For the first time, Aeromonas neuraminidase was isolated and partially purified by ion-exchange chromatography. Different purification profiles were registered depending on the growth media. The preparations containing neuraminidase activity were analyzed by native PAGE, and one of them was associated with an active protein band with a molecular weight of about 130 kDa. Our results suggest the presence of neuraminidase isoforms in Aeromonas sp. 40/02.

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Acknowledgments

This work was supported by grant G-2-02/05 from the Ministry of Education and Science, Science Research Fund, Bulgaria. We thank Mr. Dejan Draganov for providing the 4MU-Neu5Ac substrate.

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  1. Bulgarian Academy of Sciences, The Stephan Angeloff Institute of Microbiology, 26Acad. G. Bonchev Str, 1113, Sofia, Bulgaria

    Stephan Engibarov, Rumyana Еneva & Ignat Abrashev

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  1. Stephan Engibarov
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  2. Rumyana Еneva
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  3. Ignat Abrashev
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Correspondence to Stephan Engibarov.

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Engibarov, S., Еneva, R. & Abrashev, I. Neuraminidase (sialidase) from Aeromonas sp. strain 40/02 – isolation and partial purification. Ann Microbiol 65, 1515–1523 (2015). https://doi.org/10.1007/s13213-014-0990-0

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  • DOI: https://doi.org/10.1007/s13213-014-0990-0

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