Oxidative Regulation of Galectin-1 Antimicrobial Properties Público

Evavold, Birk (Spring 2019)

Permanent URL: https://etd.library.emory.edu/concern/etds/5t34sk51n?locale=pt-BR
Published

Abstract

       Galectin-1 (Gal-1) is a protein that binds carbohydrates with β-galactoside linkages. Through this binding, Gal-1 exerts a variety of immune modulatory effects. Gal-1, however, has a high propensity to oxidative inactivation. Here, we demonstrate that Gal-1 cysteine residues can be altered by alkylation with iodoacetamide. This alteration inhibits oxidation of Gal-1 as measured by column affinity binding and HL-60 cell agglutination. Additionally, we show that Gal-1 possesses antimicrobial properties and can directly kill Providencia alcalifaciens O5 (PAO5), a pathogenic bacteria species known to cause traveler’s diarrhea. Furthermore, we demonstrate that oxidation regulates Gal-1’s antimicrobial properties as alkylated Gal-1 exhibits stronger bactericidal activity despite similar binding potential. We also studied the oxidation of Gal-1 to understand structural changes between reduced and oxidized Gal-1. While we do not presently have a crystal structure of oxidized Gal-1, we successfully optimized oxidation conditions such that we can produce purely oxidized monomeric Gal-1. We intend to use this optimization to make crystals of oxidized Gal-1 and elucidate atomic level structural changes of Gal-1 oxidation.  

Table of Contents

Background........1

Methods.............8

Results...............17

Discussion..........38

References.........43

About this Honors Thesis

Rights statement
  • Permission granted by the author to include this thesis or dissertation in this repository. All rights reserved by the author. Please contact the author for information regarding the reproduction and use of this thesis or dissertation.
School
Department
Degree
Submission
Language
  • English
Research Field
Palavra-chave
Committee Chair / Thesis Advisor
Committee Members
Última modificação

Primary PDF

Supplemental Files