期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 289, 期 22, 页码 15680-15690出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M114.567669
关键词
Carbohydrate Biosynthesis; Cell Wall; Peptidoglycan; Staphylococcus aureus (S; aureus); Teichoic Acid; LytR-CpsA-Psr; Capsular Polysaccharide; Hydrolase; Undecaprenol
资金
- National Institutes of Health from the NIAID [AI38897]
- Novartis Vaccines and Diagnostics (Siena, Italy)
- Region V Great Lakes Regional Center of Excellence in Biodefense and Emerging Infectious Diseases Consortium (GLRCE)
- National Institutes of Health NIAID [1-U54-AI-057153]
- American Heart Association [13POST16980091]
Envelope biogenesis in bacteria involves synthesis of intermediates that are tethered to the lipid carrier undecaprenol-phosphate. LytR-CpsA-Psr (LCP) enzymes have been proposed to catalyze the transfer of undecaprenol-linked intermediates onto the C6-hydroxyl of MurNAc in peptidoglycan, thereby promoting attachment of wall teichoic acid (WTA) in bacilli and staphylococci and capsular polysaccharides (CPS) in streptococci. S. aureus encodes three lcp enzymes, and a variant lacking all three genes (lcp) releases WTA from the bacterial envelope and displays a growth defect. Here, we report that the type 5 capsular polysaccharide (CP5) of Staphylococcus aureus Newman is covalently attached to the glycan strands of peptidoglycan. Cell wall attachment of CP5 is abrogated in the lcp variant, a defect that is best complemented via expression of lcpC in trans. CP5 synthesis and peptidoglycan attachment are not impaired in the tagO mutant, suggesting that CP5 synthesis does not involve the GlcNAc-ManNAc linkage unit of WTA and may instead utilize another Wzy-type ligase to assemble undecaprenyl-phosphate intermediates. Thus, LCP enzymes of S. aureus are promiscuous enzymes that attach secondary cell wall polymers with discrete linkage units to peptidoglycan.
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