Literature DB >> 31945439

Diversity of sialidases found in the human body - A review.

Sabina Lipničanová1, Daniela Chmelová2, Miroslav Ondrejovič3, Vladimír Frecer4, Stanislav Miertuš5.   

Abstract

Sialidases are enzymes essential for numerous organisms including humans. Hydrolytic sialidases (EC 3.2.1.18), trans-sialidases and anhydrosialidases (intramolecular trans-sialidases, EC 4.2.2.15) are glycoside hydrolase enzymes that cleave the glycosidic linkage and release sialic acid residues from sialyl substrates. The paper summarizes diverse sialidases present in the human body and their potential impact on development of antiviral compounds - inhibitors of viral neuraminidases. It includes a brief overview of catalytic mechanisms of action of sialidases and describes the origin of sialidases in the human body. This is followed by description of the structure and function of sialidase families with a special focus on the GH33 and GH34 families. Various effects of sialidases on human body are also briefly described. Modulation of sialidase activity may be considered a useful tool for effective treatment of various diseases. In some cases, it is desired to completely suppress the activity of sialidases by suitable inhibitors. Specific sialidase inhibitors are useful for the treatment of influenza, epilepsy, Alzheimer's disease, diabetes, different types of cancer, or heart defects. Challenges and future directions are shortly depicted in the final part of the paper.
Copyright © 2020 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Anhydrosialidase; Human sialidases; Neuraminidase; Pathogen sialidases; Trans-sialidase

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Year:  2020        PMID: 31945439     DOI: 10.1016/j.ijbiomac.2020.01.123

Source DB:  PubMed          Journal:  Int J Biol Macromol        ISSN: 0141-8130            Impact factor:   6.953


  5 in total

1.  Anomeric 1,2,3-triazole-linked sialic acid derivatives show selective inhibition towards a bacterial neuraminidase over a trypanosome trans-sialidase.

Authors:  Peterson de Andrade; Sanaz Ahmadipour; Robert A Field
Journal:  Beilstein J Org Chem       Date:  2022-02-17       Impact factor: 2.883

2.  Optimization of an Inclusion Body-Based Production of the Influenza Virus Neuraminidase in Escherichia coli.

Authors:  Sabina Lipničanová; Barbora Legerská; Daniela Chmelová; Miroslav Ondrejovič; Stanislav Miertuš
Journal:  Biomolecules       Date:  2022-02-19

Review 3.  How microbial glycosyl hydrolase activity in the gut mucosa initiates microbial cross-feeding.

Authors:  Maryse D Berkhout; Caroline M Plugge; Clara Belzer
Journal:  Glycobiology       Date:  2022-03-30       Impact factor: 4.313

4.  Mammalian Neuraminidases in Immune-Mediated Diseases: Mucins and Beyond.

Authors:  Erik P Lillehoj; Irina G Luzina; Sergei P Atamas
Journal:  Front Immunol       Date:  2022-04-11       Impact factor: 8.786

Review 5.  Aberrant Sialylation in Cancer: Therapeutic Opportunities.

Authors:  Jennifer Munkley
Journal:  Cancers (Basel)       Date:  2022-08-31       Impact factor: 6.575

  5 in total

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