Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has been shown to bind noncovalently to peptidoglycan and chitin by interacting with N-acetylglucosamine moieties. The LysM sequence is present singly or repeatedly in a large number of proteins of proka...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4004799/ https://www.ncbi.nlm.nih.gov/pubmed/24652063 http://dx.doi.org/10.1007/s00253-014-5633-7 |
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author | Visweswaran, Ganesh Ram R. Leenhouts, Kees van Roosmalen, Maarten Kok, Jan Buist, Girbe |
author_facet | Visweswaran, Ganesh Ram R. Leenhouts, Kees van Roosmalen, Maarten Kok, Jan Buist, Girbe |
author_sort | Visweswaran, Ganesh Ram R. |
collection | PubMed |
description | The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has been shown to bind noncovalently to peptidoglycan and chitin by interacting with N-acetylglucosamine moieties. The LysM sequence is present singly or repeatedly in a large number of proteins of prokaryotes and eukaryotes. Since the mid-1990s, domains containing one or more of these LysM sequences originating from different LysM-containing proteins have been examined for purely scientific reasons as well as for their possible use in various medical and industrial applications. These studies range from detecting localized binding of LysM-containing proteins onto bacteria to actual bacterial cell surface analysis. On a more applied level, the possibilities of employing the LysM domains for cell immobilization, for the display of peptides, proteins, or enzymes on (bacterial) surfaces as well as their utility in the development of novel vaccines have been scrutinized. To serve these purposes, the chimeric proteins containing one or more of the LysM sequences have been produced and isolated from various prokaryotic and eukaryotic expression hosts. This review gives a succinct overview of the characteristics of the LysM domain and of current developments in its application potential. |
format | Online Article Text |
id | pubmed-4004799 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-40047992014-05-07 Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications Visweswaran, Ganesh Ram R. Leenhouts, Kees van Roosmalen, Maarten Kok, Jan Buist, Girbe Appl Microbiol Biotechnol Mini-Review The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has been shown to bind noncovalently to peptidoglycan and chitin by interacting with N-acetylglucosamine moieties. The LysM sequence is present singly or repeatedly in a large number of proteins of prokaryotes and eukaryotes. Since the mid-1990s, domains containing one or more of these LysM sequences originating from different LysM-containing proteins have been examined for purely scientific reasons as well as for their possible use in various medical and industrial applications. These studies range from detecting localized binding of LysM-containing proteins onto bacteria to actual bacterial cell surface analysis. On a more applied level, the possibilities of employing the LysM domains for cell immobilization, for the display of peptides, proteins, or enzymes on (bacterial) surfaces as well as their utility in the development of novel vaccines have been scrutinized. To serve these purposes, the chimeric proteins containing one or more of the LysM sequences have been produced and isolated from various prokaryotic and eukaryotic expression hosts. This review gives a succinct overview of the characteristics of the LysM domain and of current developments in its application potential. Springer Berlin Heidelberg 2014-03-21 2014 /pmc/articles/PMC4004799/ /pubmed/24652063 http://dx.doi.org/10.1007/s00253-014-5633-7 Text en © The Author(s) 2014 https://creativecommons.org/licenses/by/4.0/ Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. |
spellingShingle | Mini-Review Visweswaran, Ganesh Ram R. Leenhouts, Kees van Roosmalen, Maarten Kok, Jan Buist, Girbe Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications |
title | Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications |
title_full | Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications |
title_fullStr | Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications |
title_full_unstemmed | Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications |
title_short | Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications |
title_sort | exploiting the peptidoglycan-binding motif, lysm, for medical and industrial applications |
topic | Mini-Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4004799/ https://www.ncbi.nlm.nih.gov/pubmed/24652063 http://dx.doi.org/10.1007/s00253-014-5633-7 |
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