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Profiling lethal factor interacting proteins from human stomach using T7 phage display screening.

Albin Cardona-Correa1, Carlos Rios-Velazquez1

  • 1Department of Biology, College of Arts and Sciences, University of Puerto Rico‑Mayagüez, Mayagüez 00681‑9000, PR, USA.

Molecular Medicine Reports
|April 2, 2016
PubMed
Summary
This summary is machine-generated.

Researchers identified new protein interactions involved in gastrointestinal anthrax pathogenesis. This study used T7 phage display to find potential therapeutic targets for Bacillus anthracis infection.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Bacillus anthracis lethal factor (LF) is a metalloproteinase causing cell apoptosis.
  • Gastrointestinal (GI) anthrax mechanisms and molecular pathways of LF-induced tissue damage remain unclear.
  • Previous studies noted gastric ulceration and bacterial growth in Peyer's patches.

Purpose of the Study:

  • To identify proteins involved in GI anthrax pathogenesis.
  • To investigate protein-protein interactions with Bacillus anthracis lethal factor (LF).
  • To elucidate molecular pathways for potential therapeutic development.

Main Methods:

  • Utilized human stomach T7 phage display (T7PD) cDNA libraries to identify protein ligands.
  • Employed wild type and mutant LF (E687A) to differentiate interaction sites.
  • Performed in silico analysis of 124 identified clones from 194 interacting phages.

Main Results:

  • Identified 10 LF-interacting peptides, including pepsin A3 pre-protein (PAP).
  • PAP demonstrated affinity to both wild type and mutant LF at concentrations as low as 1 µg/ml.
  • Selected candidates included proteins from lipase, peptidase-A1, and cation transport families.

Conclusions:

  • Findings contribute to understanding GI anthrax molecular pathogenesis.
  • Identified PAP as a potential interacting partner of LF.
  • This research aids in developing novel therapeutic strategies against anthrax.