Covalent attachment of proteins to peptidoglycan.
Bacterial surface proteins are key players in host-symbiont or host-pathogen interactions. How these proteins are targeted and displayed at the cell surface are challenging issues of both fundamental and clinical relevance. While surface proteins of Gram-negative bacteria are assembled in the outer membrane, Gram-positive bacteria predominantly utilize their thick cell wall as a platform to anchor their surface proteins. This surface display involves both covalent and noncovalent interactions with either the peptidoglycan or secondary wall polymers such as teichoic acid or lipoteichoic acid. This review focuses on the role of enzymes that covalently link surface proteins to the peptidoglycan, the well-known sortases in Gram-positive bacteria, and the recently characterized l,d-transpeptidases in Gram-negative bacteria.
Dramsi
Shaynoor
S
Unité de Biologie des Bactéries Pathogènes à Gram-positif, Institut Pasteur, Paris, France. sdramsi@pasteur.fr
Magnet
Sophie
S
Davison
Sophie
S
Arthur
Michel
M
D000595:Amino Acid Sequence; D019881:Aminoacyltransferases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D001419:Bacteria / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D053898:Biosynthetic Pathways; D002473:Cell Wall / Q000201:enzymology; D008074:Lipoproteins / Q000378:metabolism; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism*; D010458:Peptidyl Transferases / Q000378:metabolism; D013379:Substrate Specificity
D001426:Bacterial Proteins; D008074:Lipoproteins; D010457:Peptidoglycan; D019881:Aminoacyltransferases; D010458:Peptidyl Transferases