Structural studies of the epidermolytic toxins from Staphylococcus aureus and bothropstoxin-I from Bothrops jararacussu

Toxicon ◽  
2000 ◽  
Vol 38 (4) ◽  
pp. 509-510
Keyword(s):  
Staphylococcus Aureus ◽  
Structural Studies ◽  
Bothrops Jararacussu

Synthesis and structural studies of 1-phenyl-1,3-butanedione copper(II) complexes as an excellent antimicrobial agent against methicillin-resistant Staphylococcus aureus

2019 ◽  
Vol 484 ◽  
pp. 227-236 ◽  
Author(s):  
Hema M. Krishnegowda ◽  
Chimatahalli S. Karthik ◽  
Manukumar H. Marichannegowda ◽  
Karthik Kumara ◽  
Pampa J. Kudigana ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Antimicrobial Agent ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Structural Studies ◽  
Methicillin Resistant

scholarly journals Structural insights into the intermolecular interaction of the adhesin SdrC in the pathogenicity of Staphylococcus aureus

2021 ◽  
Vol 77 (2) ◽  
pp. 47-53
Author(s):  
Junchao Wang ◽  
Min Zhang ◽  
Mingzhu Wang ◽  
Jianye Zang ◽  
Xuan Zhang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Intermolecular Interaction ◽  
Medical Equipment ◽  
Cell Attachment ◽  
Surface Protein ◽  
Structural Studies ◽  
Toxic Shock ◽  
Opportunistic Disease ◽  
Bacterial Aggregation ◽  
Structural Insights

Staphylococcus aureus is an opportunistic disease-causing pathogen that is widely found in the community and on medical equipment. A series of virulence factors secreted by S. aureus can trigger severe diseases such as sepsis, endocarditis and toxic shock, and thus have a great impact on human health. The transformation of S. aureus from a colonization state to a pathogenic state during its life cycle is intimately associated with the initiation of bacterial aggregation and biofilm accumulation. SdrC, an S. aureus surface protein, can act as an adhesin to promote cell attachment and aggregation by an unknown mechanism. Here, structural studies demonstrate that SdrC forms a unique dimer through intermolecular interaction. It is proposed that the dimerization of SdrC enhances the efficiency of bacteria–host attachment and therefore contributes to the pathogenicity of S. aureus.

scholarly journals High Level Expression and Purification of Atl, the Major Autolytic Protein ofStaphylococcus aureus

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Vineet K. Singh
Keyword(s):  
Staphylococcus Aureus ◽  
Structural Properties ◽  
Biofilm Formation ◽  
Structural Studies ◽  
Ofstaphylococcus Aureus ◽  
Expression And Purification ◽  
High Level Expression ◽  
Over Expression ◽  
Important Protein ◽  
High Level

Staphylococcus aureusis a major human and animal pathogen. Autolysins regulate the growth, turnover, cell lysis, biofilm formation, and the pathogenicity ofS. aureus. Atl is the major autolysin inS. aureus. The biochemical and structural studies of staphylococcal Atl have been limited due to difficulty in cloning, high level overexpression, and purification of this protein. This study describes successful cloning, high level over-expression, and purification of two forms of fully functional Atl proteins. These pure proteins can be used to study the functional and structural properties of this important protein.

NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus

2020 ◽  
Vol 49 (3-4) ◽  
pp. 223-230 ◽  
Author(s):  
Alexander Golubev ◽  
Bulat Fatkhullin ◽  
Azat Gabdulkhakov ◽  
Aydar Bikmullin ◽  
Liliya Nurullina ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Elongation Factor ◽  
Structural Studies ◽  
Elongation Factor P

Repurposing an Ancient Protein Core Structure: Structural Studies on FmtA, a Novel Esterase of Staphylococcus aureus

2019 ◽  
Vol 431 (17) ◽  
pp. 3107-3123 ◽  
Author(s):  
Vikram Dalal ◽  
Pramod Kumar ◽  
Gaddy Rakhaminov ◽  
Aneela Qamar ◽  
Xin Fan ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Core Structure ◽  
Structural Studies ◽  
Protein Core ◽  
Novel Esterase

scholarly journals Abstract P-31: Assembly of the Complex of the 30S Ribosomal Subunit and the Ribosome Maturation Factor P from Staphylococcus aureus for Structural Studies by Cryo-Electron Microscopy

2021 ◽  
Vol 11 (Suppl_1) ◽  
pp. S25-S25
Author(s):  
Natalia Garaeva ◽  
Aydar Bikmullin ◽  
Evelina Klochkova ◽  
Shamil Validov ◽  
Marat Yusupov ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Staphylococcus Aureus ◽  
Bacterial Infections ◽  
Ribosomal Subunit ◽  
Size Exclusion ◽  
Structural Studies ◽  
Cryo Electron Microscopy ◽  
Maturation Factor ◽  
30S Subunit

Background: Staphylococcus aureus (S. aureus) is one of the main human pathogens causing numerous nosocomial soft tissue infections and is among the best-known causes of bacterial infections. The bacterial 70S ribosome consists of two subunits, designated the 30S (small) and 50S (large) subunits. The small subunit (30S) consists of 16S ribosomal RNA (rRNA), from which the assembly of 30S begins, and 21 ribosomal proteins (r-proteins). The ribosome maturation factor P (RimP protein) binds to the free 30S subunit. Strains lacking RimP accumulate immature 16S rRNA, and fewer polysomes and an increased amount of unassociated 30S and 50S subunits compared to wild-type strains are observed in the ribosomal profile. Structural studies of the 30S subunit complex and the ribosome maturation factor RimP will make it possible in the future to develop an antibiotic that slows down or completely stops the translation of Staphylococcus aureus, which will complicate the synthesis and isolation of its pathogenic factors. Here we present the protocol of the in vitro reconstruction of S. aureus 30S ribosome subunit in a complex with RimP for further structural studies by cryo-electron microscopy. Methods: Recombinant RimP protein from S. aureus was expressed in E. coli and purified by Ni-NTA chromatography and size exclusion chromatography. Reconstitution of the 30S–RimP complex was performed by mixing RimP protein with 30S ribosome. Unbound RimP protein was removed by Amicon Ultra Concentration (Merk KGaA, Darmstadt, Germany) with a cut-off limit of 100 kDa. The presence of RimP protein in the resulting 30S-RimP complex was confirmed by SDS-PAGE, and the quality of the final sample was analyzed by the negative staining EM. Results: Finally, by in vitro reconstruction, the 30S-RimP complex from S. aureus was obtained for further structural studies by cryo-electron microscopy.

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