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

Abstract

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.

Authors:
 [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
Publication Date:
Research Org.:
Univ. of Tennessee, Knoxville, TN (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE; Tennessee Center of Excellence in Livestock Diseases and Human Health (United States)
OSTI Identifier:
1394588
Grant/Contract Number:
AC05-00OR22725
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
PLoS ONE
Additional Journal Information:
Journal Volume: 12; Journal Issue: 8; Journal ID: ISSN 1932-6203
Publisher:
Public Library of Science
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Staphylococcus aureus; sequence motif analysis; polymerase chain reaction; antibodies; flow cytometry; gene expression; protein expression; peptidoglycans

Citation Formats

Balachandran, Manasi, Giannone, Richard J., Bemis, David A., and Kania, Stephen A.. Molecular basis of surface anchored protein A deficiency in the Staphylococcus aureus strain Wood 46. United States: N. p., 2017. Web. doi:10.1371/journal.pone.0183913.
Balachandran, Manasi, Giannone, Richard J., Bemis, David A., & Kania, Stephen A.. Molecular basis of surface anchored protein A deficiency in the Staphylococcus aureus strain Wood 46. United States. doi:10.1371/journal.pone.0183913.
Balachandran, Manasi, Giannone, Richard J., Bemis, David A., and Kania, Stephen A.. 2017. "Molecular basis of surface anchored protein A deficiency in the Staphylococcus aureus strain Wood 46". United States. doi:10.1371/journal.pone.0183913. https://www.osti.gov/servlets/purl/1394588.
@article{osti_1394588,
title = {Molecular basis of surface anchored protein A deficiency in the Staphylococcus aureus strain Wood 46},
author = {Balachandran, Manasi and Giannone, Richard J. and Bemis, David A. and Kania, Stephen A.},
abstractNote = {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.},
doi = {10.1371/journal.pone.0183913},
journal = {PLoS ONE},
number = 8,
volume = 12,
place = {United States},
year = 2017,
month = 8
}

Journal Article:
Free Publicly Available Full Text
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  • No abstract prepared.