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 Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...
B Cell Activation and Differentiation01:24

B Cell Activation and Differentiation

The adaptive immune response, a sophisticated defense mechanism, relies on the activation and differentiation of B lymphocytes, or B cells. These processes enable our bodies to mount a tailored response against specific pathogens such as bacteria, free virus particles, toxins, and parasites.
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...

You might also read

Related Articles

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

Sort by
Same author

Discovery of TCR-like antibodies to the KRAS G12D neoantigen via in silico-in vitro workflow.

Molecular therapy : the journal of the American Society of Gene Therapy·2026
Same author

Nuclear Galectin-1 Drives Cancer Progression through <i>O</i>-GlcNAcylation-Dependent Regulation of SOX2.

International journal of biological sciences·2026
Same author

Nanobody-Based Biotemplating Enables Nanoscale-Precision Metallization of Cellular, Tissue, and Plant Architectures.

ACS applied materials & interfaces·2026
Same author

De novo and scaffold-based design of GDF15 binders for cancer cachexia diagnostics and therapeutics.

Experimental & molecular medicine·2026
Same author

Plant NLRs are getting into higher-order architectures.

The Plant journal : for cell and molecular biology·2026
Same author

The Journey of Histones: Molecular Mechanisms of the Histone Chaperoning Cascade.

Biochemistry·2026

Related Experiment Video

Updated: May 14, 2026

Microscopy-based Assays for High-throughput Screening of Host Factors Involved in Brucella Infection of Hela Cells
15:29

Microscopy-based Assays for High-throughput Screening of Host Factors Involved in Brucella Infection of Hela Cells

Published on: August 5, 2016

Brucella immunogenic BP26 forms a channel-like structure.

Daegeun Kim1, Jihye Park, Soo Jin Kim

  • 1Department of Biological Sciences, KI for the BioCentury, KAIST, 335 Gwahangno, Daejeon 305-701, Korea.

Journal of Molecular Biology
|January 29, 2013
PubMed
Summary
This summary is machine-generated.

Brucella

More Related Videos

Immuno-fluorescence Assay of Leptospiral Surface-exposed Proteins
10:47

Immuno-fluorescence Assay of Leptospiral Surface-exposed Proteins

Published on: July 1, 2011

The MultiBac Protein Complex Production Platform at the EMBL
13:51

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

Related Experiment Videos

Last Updated: May 14, 2026

Microscopy-based Assays for High-throughput Screening of Host Factors Involved in Brucella Infection of Hela Cells
15:29

Microscopy-based Assays for High-throughput Screening of Host Factors Involved in Brucella Infection of Hela Cells

Published on: August 5, 2016

Immuno-fluorescence Assay of Leptospiral Surface-exposed Proteins
10:47

Immuno-fluorescence Assay of Leptospiral Surface-exposed Proteins

Published on: July 1, 2011

The MultiBac Protein Complex Production Platform at the EMBL
13:51

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

Area of Science:

  • Structural biology
  • Microbiology
  • Immunology

Background:

  • Brucella outer membrane protein BP26 is a key diagnostic marker and vaccine candidate for brucellosis.
  • The structure and function of BP26's SIMPL domain were previously unknown.
  • Understanding BP26's structure is crucial for developing effective brucellosis diagnostics and vaccines.

Purpose of the Study:

  • To determine the crystal structure of Brucella outer membrane protein BP26.
  • To elucidate the oligomeric state and potential function of BP26.
  • To provide a structural model for SIMPL domains.

Main Methods:

  • X-ray crystallography to determine the high-resolution structure of BP26.
  • Electron microscopy to confirm the oligomeric assembly of BP26.
  • Structural comparison with known proteins to infer functional roles.

Main Results:

  • The crystal structure revealed that 16 BP26 molecules assemble into a novel channel-like structure.
  • Electron microscopy confirmed an octameric ring formation with a central hole, further assembling into a larger channel.
  • BP26 shows structural similarity to a bacteriophage protein, suggesting a role in Brucella infection.

Conclusions:

  • BP26 functions as a multimeric channel, likely playing a role during Brucella infection.
  • The determined structure provides the first canonical model for SIMPL domains.
  • This structural insight can guide the development of new strategies against brucellosis.