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
|
|
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), 664–672) 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
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Publisher |
|
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. |