Functional characterization of lipase in the pathogenesis of Staphylococcus aureus

Biochem Biophys Res Commun. 2012 Mar 23;419(4):617-20. doi: 10.1016/j.bbrc.2012.02.057. Epub 2012 Feb 17.

Abstract

During infection, Staphylococcus aureus produces multiple enzymes that enable it to invade and destroy host tissues and metastasize to other sites. One such enzyme, lipase, has been recognized for its relationship in the virulence of S. aureus. However, a direct involvement of lipase in the pathogenesis of S. aureus remains to be demonstrated. Our prior study indicated that anti-lipase serum inhibits biofilm formation in S. aureus clinical strains. The aim of this study was to further characterize the roles of lipase in the pathogenesis in S. aureus. We found that deletion of the lipase-coding gene reduced biofilm formation relative to the wild-type strain. This was shown by culture in 96-well plates coated with collagen to resemble the in vivo infection process. Intraperitoneal inoculation of mice with a lipase mutant strain showed defective formation of peritoneal abscesses, and bacterial loads in different organs were much lower compared with the wild-type. Importantly, active immunization with recombinant lipase protected mice against a lethal challenge with S. aureus. Altogether, our data provide evidence that S. aureus lipase plays important roles in the pathogenesis of S. aureus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Abdominal Abscess / microbiology
  • Animals
  • Bacterial Proteins / metabolism*
  • Biofilms
  • Gene Expression Regulation, Bacterial
  • Gene Expression Regulation, Enzymologic
  • Immunization
  • Lipase / genetics
  • Lipase / immunology
  • Lipase / metabolism*
  • Male
  • Mice
  • Mice, Inbred BALB C
  • Mutation
  • Peritoneum / microbiology
  • Staphylococcal Infections / immunology
  • Staphylococcal Infections / microbiology*
  • Staphylococcal Infections / prevention & control
  • Staphylococcus aureus / enzymology*
  • Staphylococcus aureus / genetics
  • Staphylococcus aureus / pathogenicity*

Substances

  • Bacterial Proteins
  • Lipase