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Volume 38, Number 6, December 2005

The receptor of an oyster juice-borne coliphage OJ367 in the outer membrane of Salmonella derby


Yuan-Tih Ko
Department of Food Science, Biotechnology Division, School of Life Sciences, National Taiwan Ocean University, Keelung, Taiwan

Received: July 15, 2005    Revised: August 9, 2005    Accepted: August 25, 2005   

 

Corresponding author:

Yuan-Tih Ko, Department of Food Science, Biotechnology Division, School of Life Sciences, National Taiwan Ocean University, 2 Pei-Ning Rd., Keelung 20224, Taiwan. E-mail: irisko@mail.ntou.edu.tw This e-mail address is being protected from spam bots, you need JavaScript enabled to view it

 



 

Methods:

The objective of this study was to identify the receptor of OJ367, an oyster juice-borne bacteriophage, in Salmonella derby ATCC 6960. The crude receptor outer membrane (OM) fraction was prepared and examined from the total cell envelope (TCE) by differential extraction with N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid (HEPES)-MgCl2 and then with Triton-HEPES-ethylenediamine tetra-acetic acid buffers. The OM proteins (Omps) were isolated by diethylaminoethyl column chromatography to screen for receptor activity. A 45-kDa protein belonging to a minor Omp species, with phage neutralization ability, was eluted in a homogeneous form. It was a non-peptidoglycan-associated protein which was digestible by trypsin. Lipopolysaccharide had no influence on its receptor activity when coexistent in the diethylaminoethyl column fractions. An S. derby mutant resistant to lysis by phage OJ367 was isolated. The mutant not only showed decreased receptor activity in vitro when its TCE was tested but had an altered Omp profile. This implied that the 45-kDa Omp is involved as a receptor in coliphage binding; however, this role is affected by the expression of other Omps.

 



 

Key words:

Bacterial outer membrane, coliphages, outer membrane protein, Salmonella, virus binding sites


 



 

J Microbiol Immunol Infect 2005;38:399-408.