Related Experiment Video

Updated: Jun 14, 2026

Identification of Host Pathways Targeted by Bacterial Effector Proteins using Yeast Toxicity and Suppressor Screens
07:40

Identification of Host Pathways Targeted by Bacterial Effector Proteins using Yeast Toxicity and Suppressor Screens

Published on: October 25, 2019

Specific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that

Jeffrey Mital1, Natalie J Miller, Elizabeth R Fischer

  • 1Host-Parasite Interactions Section, Laboratory of Intracellular Parasites, National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, MT 59840, USA.

Cellular Microbiology
|March 25, 2010
PubMed

Insights

Chlamydia trachomatis bacteria form a novel structure on their vacuole membrane, recruiting host kinases and interacting with centrosomes. This structure may explain how these bacteria manipulate the host cell's microtubule network.

Area of Science:

  • Microbiology
  • Cell Biology
  • Bacterial Pathogenesis

Background:

  • Chlamydiae are Gram-negative, obligate intracellular bacteria causing significant disease.
  • Chlamydia trachomatis forms a modified vacuole (inclusion) trafficked to the microtubule-organizing centre (MTOC).
  • Bacterial effector proteins, inclusion membrane proteins (Incs), modify the inclusion.

Purpose of the Study:

  • To characterize a novel structure on the Chlamydia trachomatis inclusion membrane.
  • To investigate the role of this structure in host-microtubule interactions.

Main Methods:

  • Microscopy to observe inclusion membrane structures.
  • Biochemical assays to study protein interactions.
  • Analysis of host-pathogen interactions in infected and transfected cells.

Main Results:

  • A novel microdomain-like structure was identified on the inclusion membrane.
  • This structure recruits active Src family kinases and is enriched in cholesterol.
  • Four specific inclusion membrane proteins (Incs) colocalized within this structure, with evidence of stable interactions.
  • Host centrosomes associated with these microdomain proteins.

Conclusions:

  • The identified inclusion membrane structure, involving host kinases and bacterial Incs, may mediate Chlamydia trachomatis interactions with the host microtubule network.
  • This structure could be responsible for observed effects on centrosome stability.
  • Further research into this structure can elucidate bacterial pathogenesis mechanisms.

More Related Videos

Using Fluorescent Proteins to Visualize and Quantitate Chlamydia Vacuole Growth Dynamics in Living Cells07:42

Using Fluorescent Proteins to Visualize and Quantitate Chlamydia Vacuole Growth Dynamics in Living Cells

Published on: October 13, 2015

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis10:32

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis

Published on: June 10, 2020

Related Concept Videos

Bacterial Phylum Chlamydiae01:29

Bacterial Phylum Chlamydiae

The phylum Chlamydiae or Chlamydiota is composed of a single order, Chlamydiales. This phylum consists entirely of obligate intracellular parasites that infect eukaryotic hosts. While human pathogens within this group have been studied extensively, the phylum encompasses many species capable of interacting with various eukaryotic organisms. Members of Chlamydiae are typically small cocci, approximately 0.5 μm in diameter, and exhibit a distinctive developmental cycle. As is characteristic of...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Attachment of Sister Chromatids02:57

Attachment of Sister Chromatids

As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall of a...
Intracellular Movement of Viruses and Bacteria01:10

Intracellular Movement of Viruses and Bacteria

Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a virus that...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...