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Title

Immucillin-H, a purine nucleoside phosphorylase transition state analog, causes non-lethal attenuation of growth in Staphylococcus aureus

 

Authors

Christopher F Stratton & Vern L Schramm*

 

Affiliation

Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461

 

Email

vern.schramm@einstein.yu.edu; *Corresponding author

 

Article Type

Hypothesis

 

Date

Received December 01, 2012; Accepted December 04, 2012; Published January 09, 2013

 

Abstract

Purine nucleoside phosphorylase (PNP; EC: 2.4.2.1) is a key enzyme involved in the purine salvage pathway. A recent bioinformatic study by Yadav, P. K. et al. (Bioinformation 2012, 8(14), 664672) reports PNP as an essential enzyme and potential drug target in community-acquired methicillin-resistant Staphylococcus aureus (CA-MRSA). We conducted an analysis using the methodology outlined by the authors, but were unable to identify PNP as an essential gene product in CA-MRSA. In addition, the treatment of Staphylococcus aureus cultures with immucillin-H, a powerful inhibitor of PNP, resulted in the non-lethal attenuation of growth, suggesting that PNP activity is not essential for cell viability.  

 

Citation

Stratton & Schramm,   Bioinformation 9(1): 009-017 (2013)
 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.