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Title: Molecular basis of surface anchored protein A deficiency in the Staphylococcus aureus strain Wood 46

Journal Article · · PLoS ONE
 [1];  [2];  [1]; ORCiD logo [1]
  1. Univ. of Tennessee, Knoxville, TN (United States). Dept. of Biomedical and Diagnostic Sciences
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Chemical Sciences Division. Mass Spectrometry and Laser Spectrometry

Protein A in Staphylococcus aureus is encoded by the spa (staphylococcal protein A) gene and binds to immunoglobulin (Ig). The S. aureus strain Wood 46 has been variously reported as protein A-deficient and/or spa negative and used as a control in animal models of staphylococcal infections. The results of this study indicate that Wood 46 has normal spa expression but transcribes very low levels of the srtA gene which encodes the sortase A (SrtA) enzyme. This is consistent with unique mutations in the srtA promoter. In this study, a low level of sortase A explains deficient anchoring of proteins with an LPXTG motif, such as protein A, fibrinogen-binding protein and fibronectin-binding proteins A and B on to the peptidoglycan cell wall. The activity of secreted protein A is an important consideration for use of Wood 46 in functional experiments and animal models.

Research Organization:
Univ. of Tennessee, Knoxville, TN (United States); Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Organization:
USDOE; Tennessee Center of Excellence in Livestock Diseases and Human Health (United States)
Grant/Contract Number:
AC05-00OR22725
OSTI ID:
1394588
Journal Information:
PLoS ONE, Vol. 12, Issue 8; ISSN 1932-6203
Publisher:
Public Library of ScienceCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 4 works
Citation information provided by
Web of Science

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Cited By (1)