Protein A of Staphylococcus aureus strain NCTC8325 interacted with heparin

2021 ◽  
Author(s):  
Hui Shi ◽  
Jiaqin Tang ◽  
Cuiying An ◽  
Lingkang Yang ◽  
Xianxuan Zhou
Keyword(s):  
Staphylococcus Aureus ◽  
Protein A ◽  
Aureus Strain

scholarly journals Impacts of sarA and agr in Staphylococcus aureus Strain Newman on Fibronectin-Binding Protein A Gene Expression and Fibronectin Adherence Capacity In Vitro and in Experimental Infective Endocarditis

2004 ◽  
Vol 72 (3) ◽  
pp. 1832-1836 ◽  
Author(s):  
Yan-Qiong Xiong ◽  
Arnold S. Bayer ◽  
Michael R. Yeaman ◽  
Willem van Wamel ◽  
Adhar C. Manna ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Capacity ◽  
Protein A ◽  
Aureus Strain ◽  
Global Regulators ◽  
Fibronectin Binding Protein ◽  
Regulatory Loci ◽  
Fibronectin Binding

ABSTRACT We investigated the impacts of sarA and agr on fnbA expression and fibronectin-binding capacity in Staphylococcus aureus in vitro and in experimental endocarditis. Although sarA up-regulated and agr down-regulated both fnbA expression and fibronectin binding in vitro and in vivo, fnbA expression was positively regulated in the absence of both global regulators. Thus, additional regulatory loci contribute to fnbA regulation and fibronectin-binding capacities in S. aureus.

scholarly journals Molecular basis of surface anchored protein A deficiency in the Staphylococcus aureus strain Wood 46

PLoS ONE ◽  
2017 ◽  
Vol 12 (8) ◽  
pp. e0183913 ◽  
Author(s):  
Manasi Balachandran ◽  
Richard J. Giannone ◽  
David A. Bemis ◽  
Stephen A. Kania
Keyword(s):  
Staphylococcus Aureus ◽  
Molecular Basis ◽  
Protein A ◽  
Aureus Strain

scholarly journals A protein component of the cell surface of Staphylococcus aureus

1968 ◽  
Vol 108 (2) ◽  
pp. 257-262 ◽  
Author(s):  
A. M. James ◽  
J. E. Brewer
Keyword(s):  
Staphylococcus Aureus ◽  
Protein A ◽  
Surface Protein ◽  
Protein Component ◽  
The Other ◽  
Animal Origin ◽  
Aureus Strain ◽  
Similar Treatment ◽  
Ph Values ◽  
Protein Components

1. Treatment with trypsin of cells of Staphylococcus aureus strain Cowan I, known to carry a protein component that includes the Jensen protein A, results in an increase in the negative mobility of the cells at pH values greater than 6. 2. Similar treatment of cells of strain Wood 46, which has no surface protein component, causes no change in the electrophoretic mobility. 3. Electrokinetically heterogeneous populations are observed in two strains of S. aureus, one of human and the other of animal origin. Evidence is presented ascribing this to the presence of varying amounts of protein components on the surface of different cells.

Detection of Rabies Virus and Its Antibodies Using Staphylococcus aureus Protein A

2015 ◽  
Vol 43 (1) ◽  
pp. 87-93
Author(s):  
Hemmat A ◽  
A Albehwar ◽  
M Shendy
Keyword(s):  
Staphylococcus Aureus ◽  
Rabies Virus ◽  
Protein A

scholarly journals Virulence Factors Found in Nasal Colonization and Infection of Methicillin-Resistant Staphylococcus aureus (MRSA) Isolates and Their Ability to Form a Biofilm

Toxins ◽  
2020 ◽  
Vol 13 (1) ◽  
pp. 14
Author(s):  
Thamiris Santana Machado ◽  
Felipe Ramos Pinheiro ◽  
Lialyz Soares Pereira Andre ◽  
Renata Freire Alves Pereira ◽  
Reginaldo Fernandes Correa ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Sccmec Type ◽  
Protein A ◽  
Invasive Infection ◽  
Type I ◽  
Methicillin Resistant ◽  
Type Iv ◽  
Spa Gene ◽  
The City

Hospitalizations related to Methicillin-resistant Staphylococcus aureus (MRSA) are frequent, increasing mortality and health costs. In this way, this study aimed to compare the genotypic and phenotypic characteristics of MRSA isolates that colonize and infect patients seen at two hospitals in the city of Niterói—Rio de Janeiro, Brazil. A total of 147 samples collected between March 2013 and December 2015 were phenotyped and genotyped to identify the protein A (SPA) gene, the mec staphylococcal chromosomal cassette (SCCmec), mecA, Panton-Valentine Leucocidin (PVL), icaC, icaR, ACME, and hla virulence genes. The strength of biofilm formation has also been exploited. The prevalence of SCCmec type IV (77.1%) was observed in the colonization group; however, in the invasive infection group, SCCmec type II was prevalent (62.9%). The Multilocus Sequence Typing (MLST), ST5/ST30, and ST5/ST239 analyses were the most frequent clones in colonization, and invasive infection isolates, respectively. Among the isolates selected to assess the ability to form a biofilm, 51.06% were classified as strong biofilm builders. Surprisingly, we observed that isolates other than the Brazilian Epidemic Clone (BEC) have appeared in Brazilian hospitals. The virulence profile has changed among these isolates since the ACME type I and II genes were also identified in this collection.

scholarly journals Malonyl-proteome profiles of Staphylococcus aureus reveal lysine malonylation modification in enzymes involved in energy metabolism

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Yanan Shi ◽  
Jingjing Zhu ◽  
Yan Xu ◽  
Xiaozhao Tang ◽  
Zushun Yang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Energy Metabolism ◽  
Active Sites ◽  
Current Knowledge ◽  
Tricarboxylic Acid Cycle ◽  
Protein A ◽  
Pentose Phosphate ◽  
Post Translational Modification ◽  
Bacterial Physiology ◽  
Dihydrolipoyl Dehydrogenase

Abstract Background Protein lysine malonylation, a novel post-translational modification (PTM), has been recently linked with energy metabolism in bacteria. Staphylococcus aureus is the third most important foodborne pathogen worldwide. Nonetheless, substrates and biological roles of malonylation are still poorly understood in this pathogen. Results Using anti-malonyl-lysine antibody enrichment and high-resolution LC-MS/MS analysis, 440 lysine-malonylated sites were identified in 281 proteins of S. aureus strain. The frequency of valine in position − 1 and alanine at + 2 and + 4 positions was high. KEGG pathway analysis showed that six categories were highly enriched, including ribosome, glycolysis/gluconeogenesis, pentose phosphate pathway (PPP), tricarboxylic acid cycle (TCA), valine, leucine, isoleucine degradation, and aminoacyl-tRNA biosynthesis. In total, 31 malonylated sites in S. aureus shared homology with lysine-malonylated sites previously identified in E. coli, indicating malonylated proteins are highly conserved among bacteria. Key rate-limiting enzymes in central carbon metabolic pathways were also found to be malonylated in S. aureus, namely pyruvate kinase (PYK), 6-phosphofructokinase, phosphoglycerate kinase, dihydrolipoyl dehydrogenase, and F1F0-ATP synthase. Notably, malonylation sites were found at or near protein active sites, including KH domain protein, thioredoxin, alanine dehydrogenase (ALD), dihydrolipoyl dehydrogenase (LpdA), pyruvate oxidase CidC, and catabolite control protein A (CcpA), thus suggesting that lysine malonylation may affect the activity of such enzymes. Conclusions Data presented herein expand the current knowledge on lysine malonylation in prokaryotes and indicate the potential roles of protein malonylation in bacterial physiology and metabolism.

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