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Anchors away: contribution of a glycolipid anchor to bacterial invasion of host cells
Miriam J. Baron, Dennis L. Kasper
Miriam J. Baron, Dennis L. Kasper
Published September 1, 2005
Citation Information: J Clin Invest. 2005;115(9):2325-2327. https://doi.org/10.1172/JCI26285.
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Commentary

Anchors away: contribution of a glycolipid anchor to bacterial invasion of host cells

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Abstract

Group B Streptococcus (GBS) is an important cause of infections, including meningitis. The molecular events underlying its pathogenesis are poorly understood. A study in this issue of the JCI reports that the GBS invasion-associated gene (iagA) contributes to meningeal infection and virulence by facilitating invasion of the cells that compose the blood-brain barrier and of other host cells. The mechanism involved most likely relates to the gene product’s role in synthesis of a glycolipid anchor for a bacterial cell-surface entity that interacts directly with host cells.

Authors

Miriam J. Baron, Dennis L. Kasper

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Figure 1

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Cell wall structure of GBS. Electron micrograph image of a type III GBS ...
Cell wall structure of GBS. Electron micrograph image of a type III GBS organism labeled with antiserum raised to whole organism; the inset shows detailed representation of important surface structures. The GBS cytoplasm is bounded by an inner cell membrane. Surrounding this membrane is a peptidoglycan layer that anchors the negatively-charged CPS and group B antigen polysaccharide. Extending from the cell membrane are lipoproteins and glycolipids, including an anchor for LTA; LTA is a structure composed of a repeating carbohydrate phosphate polymer. Most surface proteins attach to the peptidoglycan. CPS, LTA, and cell-surface proteins contribute to the organism's ability to adhere to and invade host cells and evade host immune defenses in the course of pathogenesis. Data reported by Doran et al. (15) in this issue of the JCI reveal that an enzyme involved in the synthesis of a glycolipid anchor is required for normal GBS invasion of host cells in vitro and for GBS virulence in vivo.

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ISSN: 0021-9738 (print), 1558-8238 (online)

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