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Article

Glucose Catabolite Repression Participates in the Regulation of Sialidase Biosynthesis by Antarctic Strain Penicillium griseofulvum P29

1
Department of Mycology, The Stephan Angeloff Institute of Microbiology, Bulgarian Academy of Sciences, Academician G. Bonchev 26, 1113 Sofia, Bulgaria
2
Department of General Microbiology, The Stephan Angeloff Institute of Microbiology, Bulgarian Academy of Sciences, Academician G. Bonchev 26, 1113 Sofia, Bulgaria
3
Institute of Experimental Morphology, Pathology and Anthropology with Museum, Bulgarian Academy of Sciences, Academician G. Bonchev 25, 1113 Sofia, Bulgaria
*
Author to whom correspondence should be addressed.
J. Fungi 2024, 10(4), 241; https://doi.org/10.3390/jof10040241
Submission received: 28 February 2024 / Revised: 18 March 2024 / Accepted: 21 March 2024 / Published: 23 March 2024
(This article belongs to the Special Issue Fungal Diversity and Ecology in Extreme Environments)

Abstract

Sialidases (neuraminidases) catalyze the removal of terminal sialic acid residues from glycoproteins. Novel enzymes from non-clinical isolates are of increasing interest regarding their application in the food and pharmaceutical industry. The present study aimed to evaluate the participation of carbon catabolite repression (CCR) in the regulation of cold-active sialidase biosynthesis by the psychrotolerant fungal strain Penicillium griseofulvum P29, isolated from Antarctica. The presence of glucose inhibited sialidase activity in growing and non-growing fungal mycelia in a dose- and time-dependent manner. The same response was demonstrated with maltose and sucrose. The replacement of glucose with glucose-6-phosphate also exerted CCR. The addition of cAMP resulted in the partial de-repression of sialidase synthesis. The CCR in the psychrotolerant strain P. griseofulvum P29 did not depend on temperature. Sialidase might be subject to glucose repression by both at 10 and 25 °C. The fluorescent assay using 4MU-Neu5Ac for enzyme activity determination under increasing glucose concentrations evidenced that CCR may have a regulatory role in sialidase production. The real-time RT-PCR experiments revealed that the sialidase gene was subject to glucose repression. To our knowledge, this is the first report that has studied the effect of CCR on cold-active sialidase, produced by an Antarctic strain.
Keywords: Antarctic fungi; sialidase; cold-active enzyme; catabolite repression; cAMP; glucose-6-phosphate; sialidase gene expression Antarctic fungi; sialidase; cold-active enzyme; catabolite repression; cAMP; glucose-6-phosphate; sialidase gene expression

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MDPI and ACS Style

Abrashev, R.; Krumova, E.; Petrova, P.; Eneva, R.; Dishliyska, V.; Gocheva, Y.; Engibarov, S.; Miteva-Staleva, J.; Spasova, B.; Kolyovska, V.; et al. Glucose Catabolite Repression Participates in the Regulation of Sialidase Biosynthesis by Antarctic Strain Penicillium griseofulvum P29. J. Fungi 2024, 10, 241. https://doi.org/10.3390/jof10040241

AMA Style

Abrashev R, Krumova E, Petrova P, Eneva R, Dishliyska V, Gocheva Y, Engibarov S, Miteva-Staleva J, Spasova B, Kolyovska V, et al. Glucose Catabolite Repression Participates in the Regulation of Sialidase Biosynthesis by Antarctic Strain Penicillium griseofulvum P29. Journal of Fungi. 2024; 10(4):241. https://doi.org/10.3390/jof10040241

Chicago/Turabian Style

Abrashev, Radoslav, Ekaterina Krumova, Penka Petrova, Rumyana Eneva, Vladislava Dishliyska, Yana Gocheva, Stefan Engibarov, Jeny Miteva-Staleva, Boryana Spasova, Vera Kolyovska, and et al. 2024. "Glucose Catabolite Repression Participates in the Regulation of Sialidase Biosynthesis by Antarctic Strain Penicillium griseofulvum P29" Journal of Fungi 10, no. 4: 241. https://doi.org/10.3390/jof10040241

APA Style

Abrashev, R., Krumova, E., Petrova, P., Eneva, R., Dishliyska, V., Gocheva, Y., Engibarov, S., Miteva-Staleva, J., Spasova, B., Kolyovska, V., & Angelova, M. (2024). Glucose Catabolite Repression Participates in the Regulation of Sialidase Biosynthesis by Antarctic Strain Penicillium griseofulvum P29. Journal of Fungi, 10(4), 241. https://doi.org/10.3390/jof10040241

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