Abstract
The UDP-glucose pyrophosphorylase of Streptococcus pneumoniae (GalUSpn) is absolutely required for the biosynthesis of capsular polysaccharide, the sine qua non virulence factor of pneumococcus. Since the eukaryotic enzymes are completely unrelated to their prokaryotic counterparts, we propose that the GalU enzyme is a critical target to fight the pneumococcal disease. A recombinant GalUSpn was overexpressed and purified. An enzymatic assay that is rapid, sensitive and easy to perform was developed. This assay was appropriate for screening chemical libraries for searching GalU inhibitors. This work represents a fundamental step in the exploration of novel antipneumococcal drugs.
Highlights
IntroductionStreptococcus pneumoniae (the pneumococcus) is the main cause of community-acquired pneumonia and produces meningitis, bacteremia and otitis media
Streptococcus pneumoniae is the main cause of community-acquired pneumonia and produces meningitis, bacteremia and otitis media
Many different virulence factors have been described in S. pneumoniae[1,2], but the capsular polysaccharide is only absolutely required for virulence in vivo[3,4]
Summary
Streptococcus pneumoniae (the pneumococcus) is the main cause of community-acquired pneumonia and produces meningitis, bacteremia and otitis media. At least 94 different pneumococcal capsular types have been described[5,6,7,8,9]. This remarkable phenotypic variability appears to be present at the genetic level[10]. The galU gene encodes a uridine diphosphate glucose pyrophosphorylase (UDPG:PP; UTP:glucose 1-phosphate uridylyltransferase; EC 2.7.7.9; GalU). The enzyme UDPG:PP catalyzes the reversible formation of uridine diphosphate glucose (UDP-Glc) and inorganic pyrophosphate (PPi) from uridine 3-phosphate (UTP) and glucose-1-phosphate (Glc-lP)
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