Lipid II: A central component in bacterial cell wall synthesis and a target for antibiotics

被引:102
作者
de Kruijff, Ben [1 ]
van Dam, Vincent [1 ]
Breukink, Eeflan [1 ]
机构
[1] Univ Utrecht, Utrecht, Netherlands
来源
PROSTAGLANDINS LEUKOTRIENES AND ESSENTIAL FATTY ACIDS | 2008年 / 79卷 / 3-5期
关键词
D O I
10.1016/j.plefa.2008.09.020
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The bacterial cell wall is mainly composed of peptidoglycan, which is a three-dimensional network of long aminosugar strands located on the exterior of the cytoplasmic membrane. These strands consist of alternating MurNAc and GIcNAc units and are interlinked to each other via peptide moieties that are attached to the MurNAc residues. Peptidoglycan subunits are assembled on the cytoplasmic side of the bacterial membrane on a polyisoprenoid anchor and one of the key components in the synthesis of peptidoglycan is Lipid II. Being essential for bacterial cell survival, it forms an attractive target for antibacterial compounds such as vancomycin and several lantibiotics. Lipid II consists of one GIcNAc-MurNAc-pentapeptide subunit linked to a polyiosoprenoid anchor II subunits long via a pyrophosphate linker. This review focuses on this special molecule and addresses three questions. First, why are special lipid carriers as polyprenols used in the assembly of peptidoglycan? Secondly, how is Lipid II translocated across the bacterial cytoplasmic membrane? And finally, how is Lipid II used as a receptor for lantibiotics to kill bacteria? (c) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:117 / 121
页数:5
相关论文
共 27 条
[1]   TOPOGRAPHY OF GLYCOSYLATION REACTIONS IN THE ENDOPLASMIC-RETICULUM [J].
ABEIJON, C ;
HIRSCHBERG, CB .
TRENDS IN BIOCHEMICAL SCIENCES, 1992, 17 (01) :32-36
[2]   Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic [J].
Breukink, E ;
Wiedemann, I ;
van Kraaij, C ;
Kuipers, OP ;
Sahl, HG ;
de Kruijff, B .
SCIENCE, 1999, 286 (5448) :2361-2364
[3]   Lipid II is an intrinsic component of the pore induced by nisin in bacterial membranes [J].
Breukink, E ;
van Heusden, HE ;
Vollmerhaus, PJ ;
Swiezewska, E ;
Brunner, L ;
Walker, S ;
Heck, AJR ;
de Kruijff, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (22) :19898-19903
[4]  
BUGG TDH, 1994, FEMS MICROBIOL LETT, V119, P255
[5]   The dolichol pathway of N-linked glycosylation [J].
Burda, P ;
Aebi, M .
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1999, 1426 (02) :239-257
[6]   Size and orientation of the lipid II headgroup as revealed by AFM imaging [J].
Ganchev, D. N. ;
Hasper, H. E. ;
Breukink, E. ;
de Kruijff, B. .
BIOCHEMISTRY, 2006, 45 (19) :6195-6202
[7]   Assembly and stability of nisin-Lipid II pores [J].
Hasper, HE ;
de Kruijff, B ;
Breukink, E .
BIOCHEMISTRY, 2004, 43 (36) :11567-11575
[8]   An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II [J].
Hasper, Hester E. ;
Kramer, Naomi E. ;
Smith, James L. ;
Hillman, J. D. ;
Zachariah, Cherian ;
Kuipers, Oscar P. ;
de Kruijff, Ben ;
Breukink, Eefjan .
SCIENCE, 2006, 313 (5793) :1636-1637
[9]   Transmembrane movement of dolichol linked carbohydrates during N-glycoprotein biosynthesis in the endoplasmic reticulum [J].
Helenius, J ;
Aebi, M .
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY, 2002, 13 (03) :171-178
[10]  
HIRSCHBERG CB, 1987, ANNU REV BIOCHEM, V56, P63, DOI 10.1146/annurev.bi.56.070187.000431