title: Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications.
abstract: 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.
authors.affiliation: Department of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Nijenborgh 7, 9747 AG, Groningen, The Netherlands.
authors.forename: Ganesh Ram R
authors.initials: GR
authors.lastname: Visweswaran
authors.forename: Kees
authors.initials: K
authors.lastname: Leenhouts
authors.forename: Maarten
authors.initials: M
authors.lastname: van Roosmalen
authors.forename: Jan
authors.initials: J
authors.lastname: Kok
authors.forename: Girbe
authors.initials: G
authors.lastname: Buist
mesh_terms: D001419:Bacteria / Q000737:chemistry / Q000235:genetics; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D061505:Cell Surface Display Techniques / Q000379:methods; D056890:Eukaryota / Q000737:chemistry / Q000235:genetics; D008565:Membrane Proteins / Q000378:metabolism; D010457:Peptidoglycan / Q000378:metabolism*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D008565:Membrane Proteins; D010457:Peptidoglycan; D011994:Recombinant Proteins