Abstract
C-terminal domain of peptidoglycan hydrolase enterolysin A (EnlA) is involved in specific recognition and binding to the target cell envelopes and represents true cell wall binding (CWB) domain. Sensitivity/resistance to EnlA is dependent on binding ability/disability of its CWB domain. We assume that main mechanism of resistance against EnlA is absence of the specific receptor on the cell surface, which is necessary for binding of the enzyme molecule. Using competitive and enzymatic assays we have uncovered the chemical nature of the EnlA receptor, which is a lipoteichoic acid.
Keywords: Cell wall binding, Enterococcus, enterolysin A, hydrolase, lipoteichoic acid, peptidoglycan
Protein & Peptide Letters
Title:Peptidoglycan Hydrolase Enterolysin A Recognizes Lipoteichoic Acid Chains in the Cell Walls of Sensitive Bacteria
Volume: 19 Issue: 9
Author(s): Lenka Malinicova, Katarina Dubikova, Maria Piknova, Peter Pristas and Peter Javorsky
Affiliation:
Keywords: Cell wall binding, Enterococcus, enterolysin A, hydrolase, lipoteichoic acid, peptidoglycan
Abstract: C-terminal domain of peptidoglycan hydrolase enterolysin A (EnlA) is involved in specific recognition and binding to the target cell envelopes and represents true cell wall binding (CWB) domain. Sensitivity/resistance to EnlA is dependent on binding ability/disability of its CWB domain. We assume that main mechanism of resistance against EnlA is absence of the specific receptor on the cell surface, which is necessary for binding of the enzyme molecule. Using competitive and enzymatic assays we have uncovered the chemical nature of the EnlA receptor, which is a lipoteichoic acid.
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Cite this article as:
Malinicova Lenka, Dubikova Katarina, Piknova Maria, Pristas Peter and Javorsky Peter, Peptidoglycan Hydrolase Enterolysin A Recognizes Lipoteichoic Acid Chains in the Cell Walls of Sensitive Bacteria, Protein & Peptide Letters 2012; 19 (9) . https://dx.doi.org/10.2174/092986612802084410
DOI https://dx.doi.org/10.2174/092986612802084410 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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