The Staphylococcus aureus Autoinducer-2 Synthase LuxS Is Regulated by Ser/Thr Phosphorylation

ABSTRACT The Staphylococcus aureus autoinducer-2 (AI-2) producer protein LuxS is phosphorylated by the Ser/Thr kinase Stk1 at a unique position, Thr14. The enzymatic activity of the phosphorylated isoform of LuxS was abrogated compared to that of nonphosphorylated LuxS, thus providing the first evidence of an AI-2-producing enzyme regulated by phosphorylation and demonstrating that S. aureus possesses an original and specific system for controlling AI-2 synthesis.

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Sortase mutants with improved protein thermostability and enzymatic activity obtained by consensus design

Protein Engineering Design and Selection ◽

10.1093/protein/gzaa018 ◽

2019 ◽

Vol 32 (12) ◽

pp. 555-564

Author(s):

Magdalena Wójcik ◽

Susana Vázquez Torres ◽

Wim J Quax ◽

Ykelien L Boersma

Keyword(s):

Staphylococcus Aureus ◽

Amino Acid ◽

Enzymatic Activity ◽

Sortase A ◽

Wild Type ◽

Protein Thermostability ◽

Consensus Analysis ◽

Gram Positive Bacteria ◽

Covalently Linked

Abstract Staphylococcus aureus sortase A (SaSrtA) is an enzyme that anchors proteins to the cell surface of Gram-positive bacteria. During the transpeptidation reaction performed by SaSrtA, proteins containing an N-terminal glycine can be covalently linked to another protein with a C-terminal LPXTG motif (X being any amino acid). Since the sortase reaction can be performed in vitro as well, it has found many applications in biotechnology. Although sortase-mediated ligation has many advantages, SaSrtA is limited by its low enzymatic activity and dependence on Ca2+. In our study, we evaluated the thermodynamic stability of the SaSrtA wild type and found the enzyme to be stable. We applied consensus analysis to further improve the enzyme’s stability while at the same time enhancing the enzyme’s activity. As a result, we found thermodynamically improved, more active and Ca2+-independent mutants. We envision that these new variants can be applied in conjugation reactions in low Ca2+ environments.

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Biosurfactants of Lactobacillus helveticus for biodiversity inhibit the biofilm formation of Staphylococcus aureus and cell invasion

Future Microbiology ◽

10.2217/fmb-2018-0354 ◽

2019 ◽

Vol 14 (13) ◽

pp. 1133-1146 ◽

Cited By ~ 3

Author(s):

Xinpeng Jiang ◽

Xin Yan ◽

Shanshan Gu ◽

Yan Yang ◽

Lili Zhao ◽

...

Keyword(s):

Staphylococcus Aureus ◽

Host Cell ◽

Biofilm Formation ◽

Lactobacillus Helveticus ◽

Real Time Quantitative Pcr ◽

Autoinducer 2 ◽

New Strategy ◽

Better Than

Aim: This study aimed to evaluate the differences of biosurfactants produced by two Lactobacillus helveticus strains against the biofilm formation of Staphylococcus aureus in vitro and in vivo. Materials & methods: Scanning electron microscopy, Real time-quantitative PCR (RT-qPCR) and cell assay were used to analyze the inhibiting effect of biosurfactants against biofilm formation. Results & conclusion: Results showed that the biosurfactants have anti-adhesive and inhibiting effects on biofilm formation in vivo and in vitro. The biofilm-formative genes and autoinducer-2 signaling regulated these characteristics, and the biosurfactant L. helveticus 27170 is better than that of 27058. Host cell adhesion and invasion results indicated that the biosurfactants L. helveticus prevented the S. aureus invading the host cell, which may be a new strategy to eliminate biofilms.

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Detection of endogenous MazF enzymatic activity in Staphylococcus aureus

Analytical Biochemistry ◽

10.1016/j.ab.2013.08.018 ◽

2013 ◽

Vol 443 (1) ◽

pp. 81-87 ◽

Cited By ~ 4

Author(s):

Julia J. van Rensburg ◽

Paul J. Hergenrother

Keyword(s):

Staphylococcus Aureus ◽

Enzymatic Activity

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Effects of Helichrysum italicum extract on growth and enzymatic activity of Staphylococcus aureus

International Journal of Antimicrobial Agents ◽

10.1016/s0924-8579(01)00336-3 ◽

2001 ◽

Vol 17 (6) ◽

pp. 517-520 ◽

Cited By ~ 59

Author(s):

Antonia Nostro ◽

Giuseppe Bisignano ◽

Maria Angela Cannatelli ◽

Giuseppe Crisafi ◽

Maria Paola Germanò ◽

...

Keyword(s):

Staphylococcus Aureus ◽

Enzymatic Activity

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Enzymatic Activity of Coagulase-positive Staphylococcus aureus Strains Isolated from Patients and Healthy Carriers

Pathobiology ◽

10.1159/000161915 ◽

1966 ◽

Vol 29 (3) ◽

pp. 307-323

Author(s):

W. Kedzia ◽

M. Musielak ◽

B. Kedzia ◽

H. Koniar ◽

E. Pniewska

Keyword(s):

Staphylococcus Aureus ◽

Enzymatic Activity ◽

Healthy Carriers

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Enzymatic Activity of the Staphylococcus aureus SplB Serine Protease is Induced by Substrates Containing the Sequence Trp-Glu-Leu-Gln

Journal of Molecular Biology ◽

10.1016/j.jmb.2008.03.059 ◽

2008 ◽

Vol 379 (2) ◽

pp. 343-356 ◽

Cited By ~ 28

Author(s):

Grzegorz Dubin ◽

Justyna Stec-Niemczyk ◽

Magdalena Kisielewska ◽

Katarzyna Pustelny ◽

Grzegorz M. Popowicz ◽

...

Keyword(s):

Staphylococcus Aureus ◽

Enzymatic Activity ◽

Serine Protease

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Staphylococcus aureus autoinducer-2 quorum sensing decreases biofilm formation in an icaR-dependent manner

BMC Microbiology ◽

10.1186/1471-2180-12-288 ◽

2012 ◽

Vol 12 (1) ◽

pp. 288 ◽

Cited By ~ 69

Author(s):

Dan Yu ◽

Liping Zhao ◽

Ting Xue ◽

Baolin Sun

Keyword(s):

Staphylococcus Aureus ◽

Quorum Sensing ◽

Biofilm Formation ◽

Dependent Manner ◽

Autoinducer 2

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Staphylococcus aureus AI-2 Quorum Sensing Associates with the KdpDE Two-Component System To Regulate Capsular Polysaccharide Synthesis and Virulence

Infection and Immunity ◽

10.1128/iai.00131-10 ◽

2010 ◽

Vol 78 (8) ◽

pp. 3506-3515 ◽

Cited By ~ 75

Author(s):

Liping Zhao ◽

Ting Xue ◽

Fei Shang ◽

Haipeng Sun ◽

Baolin Sun

Keyword(s):

Staphylococcus Aureus ◽

Capsular Polysaccharide ◽

Two Component System ◽

Signal Molecule ◽

Component System ◽

Gram Positive Bacteria ◽

Autoinducer 2 ◽

Polysaccharide Synthesis ◽

Signaling Function ◽

Two Component

ABSTRACT Autoinducer 2 (AI-2) is widely recognized as a signal molecule for intra- and interspecies communication in Gram-negative bacteria, but its signaling function in Gram-positive bacteria, especially in Staphylococcus aureus, remains obscure. Here we reveal the role of LuxS in the regulation of capsular polysaccharide synthesis in S. aureus NCTC8325 and show that AI-2 can regulate gene expression and is involved in some physiological activities in S. aureus as a signaling molecule. Inactivation of luxS in S. aureus NCTC8325 resulted in higher levels of transcription of capsular polysaccharide synthesis genes. The survival rate of the luxS mutant was higher than that of the wild type in both human blood and U937 macrophages. In comparison to the luxS mutant, a culture supplemented with chemically synthesized 4,5-dihydroxy-2,3-pentanedione (DPD), the AI-2 precursor molecule, restored all the parental phenotypes, suggesting that AI-2 has a signaling function in S. aureus. Furthermore, we demonstrated that the LuxS/AI-2 signaling system regulates capsular polysaccharide production via a two-component system, KdpDE, whose function has not yet been clarified in S. aureus. This regulation occurred via the phosphorylation of KdpE binding to the cap promoter.

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