the bacterial defensin resistance protein mprf consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion抗细菌defensin蛋白质为脂质lysinylation mprf由可分域和抗菌肽排斥.pdf

The Bacterial Defensin Resistance Protein MprF Consists of Separable Domains for Lipid Lysinylation and Antimicrobial Peptide Repulsion 1 1¤ 2 2 1 Christoph M. Ernst , Petra Staubitz , Nagendra N. Mishra , Soo-Jin Yang , Gabriele Hornig , Hubert 3 2,4 1 1 Kalbacher , Arnold S. Bayer , Dirk Kraus , Andreas Peschel * ¨ ¨ 1 Cellular and Molecular Microbiology Division, Interfaculty Institute of Microbiology and Infection Medicine, University of Tubingen, Tubingen, Germany, 2 Division of Infectious Diseases, Los Angeles Biomedical Research Institute at Harbor–University of California at Los Angeles (UCLA) Medical Center, Torrance, California, United States ¨ ¨ of America, 3 Medical and Natural Sciences Research Center, University of Tubingen, Tubingen, Germany, 4 David Geffen School of Medicine at UCLA, Los Angeles, California, United States of America Abstract Many bacterial pathogens achieve resistance to defensin-like cationic antimicrobial peptides (CAMPs) by the multiple peptide resistance factor (MprF) protein. MprF plays a crucial role in Staphylococcus aureus virulence and it is involved in resistance to the CAMP-like antibiotic daptomycin. MprF is a large membrane protein that modifies the anionic phospholipid phosphatidylglycerol with L-lysine, thereby diminishing the bacterial affinity for CAMPs. Its widespread