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

Phase-variable outer membrane proteins in Escherichia coli

P Owen1, M Meehan, H de Loughry-Doherty

  • 1Department of Microbiology, Moyne Institute of Preventive Medicine, Trinity College Dublin, Ireland.

FEMS Immunology and Medical Microbiology
|December 1, 1996
PubMed
Summary
This summary is machine-generated.

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

Risk factors for post-partum colic in a population of UK and Irish Thoroughbred broodmares.

Equine veterinary journal·2026
Same author

First Measurement of Time-Dependent CP Violation in the Flavor-Changing Neutral-Current Decay B^{0}→K_{S}^{0}μ^{+}μ^{-}.

Physical review letters·2026
Same author

Measurement of the Top-Quark Production Cross Section and Charge Asymmetry at LHCb.

Physical review letters·2026
Same author

Searches for B^{0}→K^{+}π^{-}τ^{+}τ^{-} and B_{s}^{0}→K^{+}K^{-}τ^{+}τ^{-} Decays.

Physical review letters·2026
Same author

First Evidence of the B_{s}^{0}→K^{-}π^{+}γ Decay.

Physical review letters·2026
Same author

Precision Measurement of CP Violation and Branching Fractions in B^{±}→K_{S}^{0}h^{±} (h=π, K) Decays and Search for the Rare Decay B_{c}^{±}→K_{S}^{0}K^{±}.

Physical review letters·2026
Same journal

Retraction. The role of nitric oxide in inflammatory reactions.

FEMS immunology and medical microbiology·2013
Same journal

Pluronic P85 enhances the efficacy of outer membrane vesicles as a subunit vaccine against Brucella melitensis challenge in mice.

FEMS immunology and medical microbiology·2012
Same journal

Mannose receptor, C type 1 contributes to bacterial uptake by placental trophoblast giant cells.

FEMS immunology and medical microbiology·2012
Same journal

Immunogenicity and therapeutic effects of Ag85A/B chimeric DNA vaccine in mice infected with Mycobacterium tuberculosis.

FEMS immunology and medical microbiology·2012
Same journal

Alcohol treatment enhances Staphylococcus aureus biofilm development.

FEMS immunology and medical microbiology·2012
Same journal

Human intestinal epithelial cell-derived molecule(s) increase enterohemorrhagic Escherichia coli virulence.

FEMS immunology and medical microbiology·2012
See all related articles

Antigen 43 (Ag43) is a phase-variable outer membrane protein in Escherichia coli that influences colony form and autoaggregation. Its expression is regulated by DNA methylation and OxyR, suggesting a role in bacterial adhesion and variation.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Bacterial Pathogenesis

Background:

  • Escherichia coli outer membrane proteins exhibit phase variation, influencing bacterial behavior.
  • Antigen 43 (Ag43) is a key protein involved in colony morphology and autoaggregation.
  • Ag43 is composed of alpha 43 and beta 43 subunits, with alpha 43 potentially acting as an adhesin.

Purpose of the Study:

  • To investigate the structure, function, and regulation of the phase-variable Antigen 43 (Ag43) protein in Escherichia coli.
  • To elucidate the molecular mechanisms underlying Ag43 phase variation.
  • To explore the potential role of Ag43 and related proteins as adhesins.

Main Methods:

  • Analysis of Ag43 protein subunits (alpha 43 and beta 43) and their properties.

Related Experiment Videos

  • Investigation of Ag43 phase variation rates and regulation by DNA methylation (dam) and OxyR.
  • Sequence homology analysis of alpha 43 with known adhesins.
  • Detection and characterization of a related 94 kDa outer membrane protein.
  • Main Results:

    • Ag43 is a bipartite complex of alpha 43 and beta 43, with alpha 43 expressed on the surface.
    • Ag43 expression undergoes reversible phase variation, regulated by DNA methylation and OxyR.
    • Alpha 43 shares homology with enterobacterial adhesins and contains an RGD motif.
    • A related 94 kDa protein, potentially a precursor, exists in some E. coli strains.

    Conclusions:

    • Ag43 plays a significant role in E. coli colony variation and autoaggregation.
    • Phase variation of Ag43 is controlled by DNA methylation and OxyR, likely through transcriptional regulation.
    • Ag43 represents a potential adhesin and may belong to a family of related outer membrane proteins.
    • The findings suggest Ag43 and similar proteins are important for E. coli adaptation and pathogenesis.