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Last update 08 May 2025

SrtA

Last update 08 May 2025

Basic Info

Synonyms

SrtA protein, SrtA sortase

Introduction-

Drugs associated with SrtA

ML346 analogue Y40(Nanjing University of Chinese Medicine)

Target

SrtA

Mechanism

SrtA inhibitors

Active Org.

Shanghai Institute of Materia Medica Chinese Academy of Sci [+1]

Originator Org.

Nanjing University of Chinese Medicine [+1]

Active Indication

Staphylococcus Aureus Infections

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Punicalagin

Target

SrtA

Mechanism

SrtA inhibitors [+1]

Active Org.

Changchun University of Chinese Medicine

Originator Org.

Changchun University of Chinese Medicine

Active Indication

MRSA - Methicillin resistant Staphylococcus aureus infection

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with SrtA

100 Translational Medicine associated with SrtA

0 Patents (Medical) associated with SrtA

822

Literatures (Medical) associated with SrtA

01 Aug 2025·Biosensors and Bioelectronics

In situ cleavage-based sortase A-mediated site-specific immobilization of beta2-adrenoceptor on gold surface for surface plasmon resonance measurement

Article

Author: Zhao, Xinfeng ; Bai, Ruoxue ; Li, Qian ; Yin, Jiatai ; Wang, Ge ; Liang, Yinku ; Wang, Jing ; Zhao, Xue ; Ou, Yuanyuan

Surface Plasmon Resonance (SPR) is a pivotal technique for measuring biomolecular interactions, with the sensor surface typically made of gold or silver and requiring proteins to be immobilized in a controlled manner. Traditional methods, such as random crosslinking via covalent amide bonds (EDC/NHS strategy), resulting in diverse protein orientations. Alternatively, site-specific immobilization strategies offer better orientation control, they are still challenged by the purification needs for protein of interests and steric hindrance produced by bulk protein tags. To address these issues, we proposed a novel protein immobilization strategy relying on in situ cleavage and Sortase A (SrtA) to immobilize functional protein on SPR sensor chips. This strategy involves the β₂-adrenoceptor (β₂AR) as a model, incorporating an endogenous protease recognition site (EPRS) as a linker to fuse SrtA with β₂AR, which contains an SrtA recognition sequence (LPXTG) at its C-terminal. When expressed in Escherichia coli (E. coli), the protease cleaves the EPRS, releasing SrtA and β₂AR. When the lysate is mixed with an oligo-Gly or oligo-Gly-modified SPR chip, transpeptidation occurs, covalently immobilizing β₂AR. The efficacy of the cleavage and transpeptidation reactions was validated through SDS-PAGE, Western blot, and chromatographic analysis. The SPR chip was characterized by scanning electron microscope (SEM), energy dispersive spectroscopy (EDS) mapping, X-ray photoelectron spectroscopy (XPS), and contact angle analysis, while β₂AR activity was evaluated by SPR. When compared to the EDC/NHS-based random method and the haloalkane dehalogenase (HaloTag)-mediated site-specific strategy, β₂AR immobilized through the SrtA-mediated method exhibited higher activity with ligands, demonstrating precision in binding affinity evaluations. This strategy meets the benchmarks for an optimal site-specific immobilization method and holds promise for applications involving the modification of other biological interfaces or biosensors.

01 Jul 2025·Microbial Pathogenesis

Covalent sortase A inhibitor, α, β-unsaturated aldehydes, prevents Staphylococcus aureus infection

Article

Author: Peng, Huayong ; Jin, Lu ; He, Yuan ; Wang, Jianchao ; Wu, Ziqi ; Zhang, Ting ; Chu, Chenliang

Sortase A (SrtA) plays a crucial role in the attachment of virulence factors characterized by the LPXTG sequence to the peptidoglycans present on the cell wall surface, thereby rendering it a significant target for anti-virulence agents aimed at combating Staphylococcus aureus (S. aureus) infections. This study focuses on the compound 3, 3'- (1,4-phenylene) diacrylaldehyde (DCA), selected as an anti-anchoring agent for covalent inhibitors. To elucidate the targets of DCA in inhibiting S. aureus and to investigate the molecular mechanism underlying the covalent inhibition of SrtA, proteomics and high-resolution mass spectrometry were employed. The findings indicate that compounds containing α, β-unsaturated aldehydes can covalently modify the catalytic residue Cys184 of SrtA. This modification effectively inhibits the transpeptidation function of SrtA, which is responsible for cell wall anchoring, thereby obstructing the attachment of virulence factors such as IgG-SpA, FnbA, ClfA, Clfb, SdrC, Sas, and Can to the cell wall. As a result, this inhibition impedes immune evasion, biofilm formation, adhesion, and subsequent infection by S. aureus. Furthermore, it disrupts the NADH/NAD⁺ redox homeostasis and diminishes the virulence phenotype by interfering with the glycolytic pathway and the tricarboxylic acid (TCA) cycle of S. aureus. These findings confirm at the molecular level that compounds containing α, β-unsaturated aldehydes possess the potential to serve as anti-virulence drugs that covalently inhibit SrtA.

01 May 2025·International Journal of Biological Macromolecules

“Box-Behnken Design for optimizing the synthesis of chitosan/PVA/Camellia sinensis essential oil composite: Thermal stability, in vitro release, antioxidant, in silico studies and antibacterial activities”

Article

Author: Hanafi, Asmaa A ; Mamdouh, Wael ; El Salakawy, Noha ; Ali, Isra H ; Shetta, Amro ; Osama, Aya

Bacterial pathogens and chemical contaminants in food threaten human health globally. This work addresses two critical knowledge gaps: optimizing Camellia sinensis Oil (CSO) incorporation into chitosan/polyvinyl alcohol (CS/PVA) matrices and elucidating antibacterial mechanisms through in-silico docking, advancing bio-based packaging for food safety. Box-Behnken Design optimized CSO-loaded films for chemical, physical, and mechanical properties. Films were characterized using SEM, FTIR spectroscopy, and TGA, then tested for antioxidant activity, water vapor permeability, transparency, and mechanical properties including tensile strength and elongation at break. CSO release from the matrix followed a biphasic profile at pH 7.4, with 20 % burst release within 12 h followed by sustained release over 72 h, governed by Hixson-Crowell matrix degradation mechanisms. To understand binding interactions, in-silico docking studies were conducted between 4-vinylguaiacol (key CSO component) and target proteins (DNA Gyrase, Sortase A, and SPI4) from Escherichia coli (E. coli), Staphylococcus aureus (S. aureus), and Salmonella Typhi (S. Typhi), respectively, revealing strong binding affinities (-5 to -8.1 Kcal/mol). The developed CSO-loaded films demonstrated significant antibacterial enhancement compared to unloaded films: 30-fold against gram-positive S. aureus, 13.4-fold and 7-fold against gram-negative S. Typhi and E. coli, respectively, confirming optimal CSO incorporation substantially improved food packaging safety and effective antibacterial protection.

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SrtA

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