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Jundishapur Journal of Microbiology
Ahvaz Jundishapur University of Medical Sciences
Cloning and periplasmic expression of peptidoglycan-associated lipoprotein (PAL) protein of Legionella pneumophila in Escherichia coli
Author(s):
Abolfazl Gholipour
1,*, 
Mojtaba Moosavian2, Hamid Galehdari2, Manoochehr Makvandi2, Hamid Rajabi Memari2, Amirhoushang Alvandi21Department of Medical Microbiology, School of Medicine and Infectious and Tropical Disease Research Center, Ahvaz Jundishapur University of Medical Science, [email protected], Iran
2Department of Medical Microbiology, School of Medicine and Infectious and Tropical Disease Research Center, Ahvaz Jundishapur University of Medical Science, Iran
*Corresponding Author: Department of Medical Microbiology, School of Medicine and Infectious and Tropical Disease Research Center, Ahvaz Jundishapur University of Medical Science, [email protected], Iran. Email: [email protected]
Published online:Jan 31, 2010
Article type:Research Article
Received:Nov 01, 2009
Accepted:Jan 01, 2010
How to Cite:Gholipour A, Moosavian M, Galehdari H, Makvandi M, Rajabi Memari H, et al. Cloning and periplasmic expression of peptidoglycan-associated lipoprotein (PAL) protein of Legionella pneumophila in Escherichia coli. Jundishapur J Microbiol. 2010;3(1):. doi:
Abstract
Introduction and objective: Legionella pneumophila, the etiological agent of Legionnaires’ disease, is an important cause of both community-acquired and nosocomial pneumonia; therefore, rapid diagnosis and early antibiotic treatment of pneumonia are required. Urinary antigen testing to detect Legionella antigen has proven to be the most powerful diagnostic method. Peptidoglycan-associated lipoprotein (PAL) protein of L. pneumophila, as a component of Legionella antigens, will be detected efficiently by the PAL antigen capture assay and is considered as useful diagnostic antigen to diagnose Legionella infection. Because of the transfer of protein to the periplasmic region of Escherichia coli has numerous advantages including separation from cytoplasmic proteins and the concentration of recombinant proteins in periplasm, the aim of this study was to produce periplasmic PAL protein of L. pneumophila in E. coli.
Materials and methods: The pal gene of L. pneumophila serogroup 1 was amplified with specific primers, cloned and expressed under pelB signal sequence and T7 lac promoter in pET26b+ plasmid.
Results: The cloning was confirmed with digestion and sequencing of recombinant pET-26b-pal plasmid. The expression of r-PAL protein in cytoplasm and periplasmic space of E. coli was approved by SDS-PAGE and western blotting.
Conclusion: The results of this study demonstrated that the r-PAL protein successfully expressed in E. coli.
Copyright
© 2010, Author(s). This open-access article is available under the Creative Commons Attribution 4.0 (CC BY 4.0) International License (https://creativecommons.org/licenses/by/4.0/), which allows for unrestricted use, distribution, and reproduction in any medium, provided that the original work is properly cited.
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