caa a22 4500 475745574 CHVBK 20180406123512.0 cr unu---uuuuu 170329e20000101xx s 000 0 eng 10.1007/s002849910005 doi (NATIONALLICENCE)springer-10.1007/s002849910005 Selective Acylation of Plasma Membrane Proteins of Mycoplasma agalactiae [Elektronische Daten] The Causal Agent of Agalactia [Michel Le Hénaff, Marie-Madeleine Guéguen, Catherine Fontenelle] Abstract.: Revealed by in vivo labeling with 14C-palmitic acid, about 15 acylated proteins were identified in the plasma membrane of Mycoplasma agalactiae (type strain PG2), including the major component p40. Triton X-114 phase partitioning and Western blotting demonstrated the amphiphilic properties of the acyl proteins and showed that they were also antigenic components. Chemical analyses of fatty acids bound to proteins revealed the following selectivity order within acylation: stearic acid (18:0) > linoleic acid (18:2c) ≈ palmitic acid (16:0) > oleic acid (18:1c) > myristic acid (14:0), with 16:0 and 18:1c preferred for the O-acylation and 18:0 for the N-acylation. The ratio [O-ester- + amide-bound acyl chains]/O-ester-linked chains being close to 1.4 as well as the presence of S-glycerylcysteine suggest that acyl proteins in M. agalactiae are true lipoproteins containing N-acyl diacyl glycerylcysteine, probably processed by a mechanism analogous to that described for Gram-negative eubacteria. Springer-Verlag New York Inc., 2000 Le Hénaff Michel Université de Rennes 1, UPRES-A CNRS 6026, Groupe "Membranes et Osmorégulation,” Campus de Beaulieu, F-35042 Rennes Cedex, France, FR aut Guéguen Marie-Madeleine Université de Rennes 1, UPRES-A CNRS 6026, Groupe "Membranes et Osmorégulation,” Campus de Beaulieu, F-35042 Rennes Cedex, France, FR aut Fontenelle Catherine Université de Rennes 1, UPRES-A CNRS 6026, Groupe "Membranes et Osmorégulation,” Campus de Beaulieu, F-35042 Rennes Cedex, France, FR aut https://doi.org/10.1007/s002849910005 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s002849910005 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Le Hénaff Michel Université de Rennes 1, UPRES-A CNRS 6026, Groupe "Membranes et Osmorégulation,” Campus de Beaulieu, F-35042 Rennes Cedex, France, FR aut NATIONALLICENCE 700 1- Guéguen Marie-Madeleine Université de Rennes 1, UPRES-A CNRS 6026, Groupe "Membranes et Osmorégulation,” Campus de Beaulieu, F-35042 Rennes Cedex, France, FR aut NATIONALLICENCE 700 1- Fontenelle Catherine Université de Rennes 1, UPRES-A CNRS 6026, Groupe "Membranes et Osmorégulation,” Campus de Beaulieu, F-35042 Rennes Cedex, France, FR aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer