Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Functional and structural characterization of Spl proteases from Staphylococcus aureus.

Grzegorz M Popowicz1, Grzegorz Dubin, Justyna Stec-Niemczyk

  • 1Max-Planck Institute of Biochemistry, Am Klopferspitz 18A, 82-152 Martinsried, Germany.

Journal of Molecular Biology
|March 7, 2006
PubMed
Summary

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Identification of a Shiga toxin A-derived peptide internalized into Gb3 receptor-bearing cells via interaction with the Shiga toxin B subunit.

FEBS letters·2026
Same author

Loss of immunological control at CD28 superfamily checkpoints links brain and peripheral immunity to depressive-like behaviors in animal models.

Neurobiology of disease·2026
Same author

The Binding of 3-O-Methylfluorescein Phosphate to the Catalytic Domain of the Human CDC25B Phosphatase: A Structural Investigation.

Chembiochem : a European journal of chemical biology·2026
Same author

MHC in newts illuminates the evolutionary dynamics of complex regions in giant genomes.

Genome research·2026
Same author

The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle.

Molecular cell·2025
Same author

Structure of Trypanosoma peroxisomal import complex unveils conformational heterogeneity.

Nature communications·2025

Staphylococcus aureus serine protease-like (spl) genes were expressed and characterized. A novel mechanism protects the cytoplasm from SplB activity, and SplC

Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • Staphylococcus aureus is a leading cause of hospital-acquired infections, with rising antibiotic resistance and no available vaccine.
  • Understanding S. aureus pathogenicity is crucial due to increasing multi-drug resistance, including vancomycin resistance.
  • Comparative genomics aids in identifying novel virulence factors in S. aureus.

Purpose of the Study:

  • To develop an efficient expression system for recombinant SplB and SplC proteases from S. aureus.
  • To structurally and functionally characterize these purified proteases.
  • To elucidate the mechanism of protease latency and substrate specificity.

Main Methods:

  • Efficient recombinant expression of SplB and SplC proteases in Escherichia coli.

Related Experiment Videos

  • Purification and subsequent structural and functional characterization of the enzymes.
  • X-ray crystallography was used to determine the structure of SplC protease.

    • Main Results:

    • An efficient system for producing recombinant SplB and SplC proteases was established.
    • A unique mechanism involving a co-translated signal peptide was identified for protecting the cytoplasm from SplB.
    • The crystal structure of SplC revealed a fold similar to V8 protease and epidermolytic toxins, explaining its latency and substrate specificity.

    Conclusions:

    • The study successfully produced and characterized SplB and SplC proteases, providing insights into S. aureus pathogenicity.
    • A novel mechanism of cytoplasmic protection against protease activity was uncovered, mediated by signal peptides.
    • The structural and functional characterization of SplC suggests a restricted substrate specificity, similar to other known S. aureus virulence factors.