Related Experiment Video
Updated: Jan 27, 2026

Murine Model of Leukemia Relapse to Induction Chemotherapy for Acute Lymphoblastic Leukemia
Published on: October 17, 2025
Bacterial translocation in acute lymphocytic leukemia.
1University of Illinois College of Medicine Peoria, Peoria, Illinois, United States of America.
Bloodstream infections in acute lymphocytic leukemia (ALL) stem from gut bacteria entering the bloodstream (bacterial translocation). This occurs due to damage in the gut-associated lymphoid tissue (GALT) during leukemia.
Area of Science:
- Immunology
- Gastroenterology
- Oncology
Background:
- Bloodstream infection (BSI) is a primary cause of mortality in acute lymphocytic leukemia (ALL).
- BSI often results from bacterial translocation (BT), where gut bacteria enter circulation due to increased intestinal permeability.
- The gut-associated lymphoid tissue (GALT) normally regulates gut microbiota and prevents BT.
Purpose of the Study:
- To investigate the mechanisms of bacterial translocation in leukemia.
- To identify and characterize alterations in the GALT in a mouse model of ALL.
Main Methods:
- Utilized a leukemic mouse model.
- Characterized alterations in the gut-associated lymphoid tissue (GALT).
- Identified differentially expressed genes in the intestinal intraepithelium and lamina propria.
Main Results:
- ALL severely impairs GALT function, characterized by a loss of lymphatic cells.
- This GALT impairment leads to increased bacterial translocation and subsequent BSI.
- Specific gene expression changes were identified that may drive BT and hinder lymphocyte migration.
Conclusions:
- Leukemia-induced damage to the GALT is a critical factor in the development of BSI via bacterial translocation.
- Targeting GALT integrity and lymphocyte migration pathways could offer new therapeutic strategies for BSI in ALL patients.
Related Concept Videos
Bacterial Translocation and Protein Secretion
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Energy to Drive Translocation
Generally, polypeptides are unfolded by two distinct...
Cotranslational Protein Translocation
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Protein Translocation Machinery on the ER Membrane
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
Post-translational Translocation of Proteins to the RER
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

