Functional characterization of lipase in the pathogenesis of Staphylococcus aureus

2012 ◽  
Vol 419 (4) ◽  
pp. 617-620 ◽  
Author(s):  
Chunyan Hu ◽  
Ning Xiong ◽  
Yong Zhang ◽  
Simon Rayner ◽  
Shiyun Chen
2005 ◽  
Vol 187 (15) ◽  
pp. 5189-5194 ◽  
Author(s):  
Jason A. Hall ◽  
Ana M. Pajor

ABSTRACT We have cloned and functionally characterized a Na+-coupled dicarboxylate transporter, SdcS, from Staphylococcus aureus. This carrier protein is a member of the divalent anion/Na+ symporter (DASS) family and shares significant sequence homology with the mammalian Na+/dicarboxylate cotransporters NaDC-1 and NaDC-3. Analysis of SdcS function indicates transport properties consistent with those of its eukaryotic counterparts. Thus, SdcS facilitates the transport of the dicarboxylates fumarate, malate, and succinate across the cytoplasmic membrane in a Na+-dependent manner. Furthermore, kinetic work predicts an ordered reaction sequence with Na+ (K 0.5 of 2.7 mM) binding before dicarboxylate (Km of 4.5 μM). Because this transporter and its mammalian homologs are functionally similar, we suggest that SdcS may serve as a useful model for DASS family structural analysis.


2021 ◽  
Author(s):  
Yang Li ◽  
Kasper Mikkelsen ◽  
Oleguer Lluch i Grané ◽  
Zhenyu Wang ◽  
Yuanyue Tang ◽  
...  

2009 ◽  
Vol 419 (3) ◽  
pp. 555-564 ◽  
Author(s):  
Justyna Stec-Niemczyk ◽  
Katarzyna Pustelny ◽  
Magdalena Kisielewska ◽  
Michal Bista ◽  
Kevin T. Boulware ◽  
...  

Staphylococcus aureus is a dangerous human pathogen whose antibiotic resistance is steadily increasing and no efficient vaccine is as yet available. This serious threat drives extensive studies on staphylococcal physiology and pathogenicity pathways, especially virulence factors. Spl (serine protease-like) proteins encoded by an operon containing up to six genes are a good example of poorly characterized secreted proteins probably involved in virulence. In the present study, we describe an efficient heterologous expression system for SplA and detailed biochemical and structural characterization of the recombinant SplA protease. The enzyme shares a significant sequence homology to V8 protease and epidermolytic toxins which are well documented staphylococcal virulence factors. SplA has a very narrow substrate specificity apparently imposed by the precise recognition of three amino acid residues positioned N-terminal to the hydrolysed peptide bond. To explain determinants of this extended specificity we resolve the crystal structure of SplA and define the consensus model of substrate binding. Furthermore we demonstrate that artificial N-terminal elongation of mature SplA mimicking a naturally present signal peptide abolishes enzymatic activity. The probable physiological role of the process is discussed. Of interest, even though precise N-terminal trimming is a common regulatory mechanism among S1 family enzymes, the crystal structure of SplA reveals novel significantly different mechanistic details.


2009 ◽  
Vol 53 (5) ◽  
pp. 1832-1839 ◽  
Author(s):  
Bettina Schulthess ◽  
Stefan Meier ◽  
Dagmar Homerova ◽  
Christiane Goerke ◽  
Christiane Wolz ◽  
...  

ABSTRACT The alternative sigma factor σB of Staphylococcus aureus controls the expression of multiple genes, including virulence determinants and global regulators; promotes capsule production; and increases the resistance levels of methicillin-resistant S. aureus (MRSA) and glycopeptide-intermediate-resistant S. aureus (GISA) strains. We show here that deletion of the σB-controlled yabJ-spoVG operon, which codes for potential downstream regulators of σB, abolished capsule synthesis and reduced resistance in MRSA and GISA to the same extent that σB inactivation did. Introduction of the yabJ-spoVG operon in trans restored the original phenotype. By genetic manipulations, we show that SpoVG but not YabJ is required for complementation. We therefore postulate that SpoVG is the major factor of the yabJ-spoVG operon required in S. aureus for capsule formation and antibiotic resistance.


1991 ◽  
Vol 155 (6) ◽  
pp. 549-553 ◽  
Author(s):  
Valery V. Petrov ◽  
Vladislav Yu. Artzatbanov ◽  
Evgeny N. Ratner ◽  
Anatoly I. Severin ◽  
Igor S. Kulaev

2020 ◽  
Vol 40 (11) ◽  
Author(s):  
Relangi Tulasi Rao ◽  
Shivani Sharma ◽  
Natesan Sivakumar ◽  
Kannan Jayakumar

Abstract Background: Genomic Islands (GIs) are commonly believed to be relics of horizontal transfer and associated with specific metabolic capacities, including virulence of the strain. Horizontal gene transfer (HGT) plays a vital role in the acquisition of GIs and the evolution and adaptation of bacterial genomes. Objective: The present study was designed to predict the GIs and role of HGT in evolution of livestock-associated Staphylococcus aureus (LA-SA). Methods: GIs were predicted with two methods namely, Ensemble algorithm for Genomic Island Detection (EGID) tool, and Seq word Sniffer script. Functional characterization of GI elements was performed with clustering of orthologs. The putative donor predictions of GIs was done with the aid of the pre_GI database. Results: The present study predicted a pan of 46 GIs across the LA-SA genomes. Functional characterization of GI sequences revealed few unique results like the presence of metabolic operons like leuABCD and folPK genes in GIs and showed the importance of GIs in the adaptation to the host niche. The developed framework for GI donor prediction results revealed Rickettsia and Mycoplasma as the major donors of GI elements. Conclusions: The role of GIs during the evolutionary race of LA-SA could be concluded from the present study. Niche adaptation of LA-SA enhanced presumably due to these GIs. Future studies could focus on the evolutionary relationships between Rickettsia and Mycoplasma sp. with S. aureus and also the evolution of Leucine/Isoleucine mosaic operon (leuABCD).


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