Work

Genes Required for Glycolipid Synthesis and Lipoteichoic Acid Anchoring in Staphylococcus aureus

Year: 2007

Type: article

Abstract: Staphylococcus aureus lipoteichoic acid (LTA) is composed of a linear 1,3-linked polyglycerolphosphate chain and is tethered to the bacterial membrane by a glycolipid (diglucosyl-diacylglycerol [Glc2-DAG]). Glc2-DAG is synthesized in the bacterial cytoplasm by YpfP, a processive enzyme that transfers glucose to diacylglycerol (DAG), using UDP-glucose as its substrate. Here we present evidence that the S. aureus alpha-phosphoglucomutase (PgcA) and UTP:alpha-glucose 1-phosphate uridyltransferase (GtaB) homologs are required for the synthesis of Glc2-DAG. LtaA (lipoteichoic acid protein A), a predicted membrane permease whose structural gene is located in an operon with ypfP, is not involved in Glc2-DAG synthesis but is required for synthesis of glycolipid-anchored LTA. Our data suggest a model in which LtaA facilitates the transport of Glc2-DAG from the inner (cytoplasmic) leaflet to the outer leaflet of the plasma membrane, delivering Glc2-DAG as a substrate for LTA synthesis, thereby generating glycolipid-anchored LTA. Glycolipid anchoring of LTA appears to play an important role during infection, as S. aureus variants lacking ltaA display defects in the pathogenesis of animal infections.

Source: Journal of Bacteriology

DOI: 10.1128/jb.01683-06

Authors: Angelika Gründling, Olaf Schneewind

Institution: University of Chicago

Language: English

Topic: Antimicrobial Resistance in Staphylococcus

Subfield: Infectious Diseases

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funder: National Institute of Allergy and Infectious Diseases

Awards: Molecular Analyses and Interventions for Biodefense and Emerging Pathogens, Surface Proteins of Gram-Positive Bacteria, Vaccine Assembly from Surface Proteins of Staphylococcus aureus