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

Penicillin-binding proteins in Bacteroides fragilis.

N H Georgopapadakou, S A Smith, R B Sykes

    The Journal of Antibiotics
    |July 1, 1983
    PubMed
    Summary

    Penicillin-binding proteins (PBPs) in Bacteroides fragilis were identified. Beta-lactam antibiotics targeted specific PBPs, affecting bacterial cell growth and survival.

    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

    Fungal diagnostics, pathogenesis and chemotherapy symposia.

    IDrugs : the investigational drugs journal·2005
    Same author

    From moulds to drugs.

    Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases·2001
    Same author

    Update on antifungals targeted to the cell wall: focus on beta-1,3-glucan synthase inhibitors.

    Expert opinion on investigational drugs·2001
    Same author

    Antifungals targeted to sphingolipid synthesis: focus on inositol phosphorylceramide synthase.

    Expert opinion on investigational drugs·2000
    Same author

    Inhibition of inositol phosphorylceramide synthase by aureobasidin A in Candida and Aspergillus species.

    Antimicrobial agents and chemotherapy·2000
    Same author

    Inhibition of yeast inositol phosphorylceramide synthase by aureobasidin A measured by a fluorometric assay.

    FEBS letters·1999

    Area of Science:

    • Microbiology
    • Bacterial Cell Wall Synthesis
    • Antibiotic Resistance Mechanisms

    Background:

    • Bacteroides fragilis is a significant Gram-negative pathogen.
    • Understanding its penicillin-binding proteins (PBPs) is crucial for developing effective treatments.
    • Existing knowledge of PBP patterns in other bacteria like Enterobacteria and Pseudomonads provides a comparative basis.

    Purpose of the Study:

    • To characterize the penicillin-binding proteins (PBPs) of Bacteroides fragilis.
    • To investigate the association of beta-lactam antibiotic activity with specific PBPs in B. fragilis.

    Main Methods:

    • Polyacrylamide gel electrophoresis and fluorography were used to detect and analyze PBPs.
    • B. fragilis strains were exposed to beta-lactam antibiotics to observe binding patterns.

    Main Results:

    • Four distinct PBPs were identified in B. fragilis, with PBP 4 being a minor component.
    • The PBP profile of B. fragilis differs from that of Enterobacteria and Pseudomonads.
    • Antibacterial activity of beta-lactam antibiotics correlated with binding to PBP 1, PBP 2, and PBP 3.
    • Binding to PBP 2 induced filamentation, while binding to PBP 1 led to cell lysis.

    Conclusions:

    • Bacteroides fragilis possesses a unique set of penicillin-binding proteins.
    • Specific PBPs (PBP 1, 2, and 3) are key targets for beta-lactam antibiotics in B. fragilis.
    • Differential binding to PBPs results in distinct cellular responses, including filamentation and lysis, offering insights into antibiotic action.

    Related Experiment Videos