Structural and Functional Characterization of a Putative CitMHS Protein from Bacillus anthracis

Author

Qi Wen Li

Degree Type

Honors Capstone Project

Date of Submission

Spring 5-1-2011

Capstone Advisor

Dr. Robert Doyle

Honors Reader

Dr. Samual Chan

Capstone Major

Biology

Capstone College

Arts and Science

Audio/Visual Component

no

Capstone Prize Winner

no

Won Capstone Funding

yes

Honors Categories

Sciences and Engineering

Subject Categories

Biochemistry | Biochemistry, Biophysics, and Structural Biology

Abstract

The growing number of strains of antibiotic-resistant bacteria poses a new threat to human health. The development of innovative strategies to treat bacterial infections is essential. The recent discovery of a new class of membrane transporters, CitMHS, unique to bacteria, presents a potential new target for antibacterial therapeutics. CitMHS is a class of secondary metal citrate membrane transporters, with only five members characterized to date (2,3,5,6,7). No crystal structures have been reported. Detailed structural and functional studies of CitMHS are essential to the understanding of infection pathways and, consequently, the ability to block such pathways. Cit_Ba is a CitMHS transporter postulated in the Gram-positive bacterium, Bacillus anthracis, which is the causative agent of anthrax. Heterologous expression of Cit_Ba in Lactococcus lactis following functional flux assays may reveal its metal citrate transport capability. Additionally, protein purification may enable antibody production, which may then be used as a vaccine or vaccine component for anthrax.

Recommended Citation

Li, Qi Wen, "Structural and Functional Characterization of a Putative CitMHS Protein from Bacillus anthracis" (2011). Honors Capstone Projects - All. 244.
https://surface.syr.edu/honors_capstone/244

Creative Commons License

This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.