A comprehensive review on staphylococcal protein A (SpA): Its production and applications

Rigi, Garshasb; Ghaedmohammadi, Samira; Ahmadian, Gholamreza

doi:10.1002/bab.1742

Cited by 49 publications

(28 citation statements)

References 76 publications

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“…Antibody purification using Protein A (SpA), immobilized to different solid surfaces, is commonly used in research laboratories or commercial antibody manufacturing. Increasing the stability of SpA protein under harsh treatment/washing conditions is an important factor to increase the yield and quality of purified antibodies (Rigi et al 2019 ; Cherf and Cochran 2015 ). One of the major strategies to increase proteins stability is display of proteins on the surface of a live cell as an alternative to classic protein immobilization approach (Lozančić et al 2019 ; Grewal, et al 2016 ).…”

Section: Discussionmentioning

confidence: 99%

Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

et al. 2020

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Staphylococcal protein A (SpA) is a major virulence factor of Staphylococcus aureus. S. aureus is able to escape detection by the immune system by the surface display of protein A. The SpA protein is broadly used to purify immunoglobulin G (IgG) antibodies. This study investigates the fusion ability of Lpp′-OmpA (46-159) to anchor and display five replicate domains of protein A with 295 residues length (SpA295) of S. aureus on the surface of Escherichia coli to develop a novel bioadsorbent. First, the binding between Lpp'-OmpA-SPA295 and IgGFc and the three-dimensional structure was investigated using molecular dynamics simulation. Then high IgG recovery from human serum by the surface-displayed system of Lpp′-OmpA-SPA295 performed experimentally. In silico analysis was demonstrated the binding potential of SPA295 to IgG after expression on LPP-OmpA surface. Surface-engineered E. coli displaying SpA protein and IgG-binding assay with SDS-PAGE analysis exhibited high potential of the expressed complex on the E. coli surface for IgG capture from human serum which is applicable to conventional immune precipitation.

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Section: Discussionmentioning

confidence: 99%

Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

et al. 2020

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“…One of the most common antibody puri cation techniques used SpA immobilized on various solid supports that can be used in industrial application. Changes in SpA immobility methods for improving antibody extraction is still ongoing (Rigi, G. et al 2019).…”

Section: Discussionmentioning

confidence: 99%

Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

Vahed

Ramezani

Tafakori

et al. 2020

Preprint

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Staphylococcal protein A (SpA) is a major bacterial virulence factor of Staphylococcus aureus. S. aureus is capable of escaping from immune system recognition by the surface display of protein A. The SpA protein is broadly used to purify immunoglobulin G (IgG) antibodies. This study investigates the ability of the fusion of Lpp’-OmpA (46 − 159) to anchor and display five repeat domains of protein A with 295 residues length (SpA295) of S. aureus on the Escherichia coli cell surface to develop a novel bioadsorbent. First, the binding between Lpp’-OmpA-SPA295 and IgGFc and anticipation of this structure was investigated using molecular dynamics simulation. Then high IgG recovery from human serum by the surface-displayed system of Lpp’-OmpA-SPA295 performed experimentally. In silico analysis showed the binding potential of SPA295 to IgG after surface expression on LPP-OmpA. Surface-engineered E. coli displaying SpA protein and IgG-binding assay with SDS-PAGE analysis exhibited the high potential of the expressed complex on the surface of E. coli for IgG recapture from human serum which is applicable to conventional immune precipitation.

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“…High specificity for the Fc region of antibodies, Large binding constants [29] Cost effective due to continuous rounds of the reaction [30] High efficiency in purification [30] Effective in the large-scale purification of monoclonal IgG [31] High cost [31] Poor stability [31] Harsh product release conditions [31] Requirement for accurate analytical test to assure the absence of contaminants [32] Process throughput Problems with leaching of Protein A ligand [33] Requirement for efficient cleaning [33] Lack of alkaline stability [33] (Continues) TA B L E 1 (Continued)…”

Section: Techniquesmentioning

confidence: 99%

“…Here, the basic interactions between the target biomolecule and the affinity sorbent are also listed for each chromatographic method. The most common advantages and disadvantages of these methods are comparatively documented in Table 1 [9,12–41]. The information presented in Figure 2 and Table 1 can be used as a starting point for the selection of an appropriate chromatographic method for a certain biomolecule that is isolated or enriched from a complex biological sample.…”

Section: Bioaffinity Chromatography Techniquesmentioning

confidence: 99%

Recent trends in sorbents for bioaffinity chromatography

Kip

Hamaloğlu

Demir

et al. 2021

J of Separation Science

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Isolation or enrichment of biological molecules from complex biological samples is mostly a prerequisite in proteomics, genomics, and glycomics. Different techniques have been used to advance the efficiency of the purification of biological molecules. Bioaffinity chromatography is one of the most powerful technique that plays an important role in the isolation of target biological molecules by the specific interactions with ligands that are immobilized on different support materials. This review examines the recent developments in bioaffinity chromatography particularly over the past 5 years in the literature. Also properties of supports, immobilization techniques, types of binding agents, and methods used in bioaffinity chromatography applications are summarized.

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A comprehensive review on staphylococcal protein A (SpA): Its production and applications

Cited by 49 publications

References 76 publications

Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG

Recent trends in sorbents for bioaffinity chromatography

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