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Original article
Gholamreza Ahmadian
National Institute of Genetic Engineering and Biotechnology, Tehran, Iran
Corresponding Author
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This work is licensed under a CC BY 4.0 License. Read Full License
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 analysiswas 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.
Keywords
Protein A- IgG interaction, Surface-displayed OmpA, Protein interaction, Molecular dynamics
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CURRENT STATUS: Published
View the published article at AMB Express.
Version 2
Posted 24 Aug, 2020
No community comments so far
Reviewer #2 agreed
On 23 Aug, 2020
Review #1 received
Received 23 Aug, 2020
Review #2 received
Received 23 Aug, 2020
Editorial decision: Accept
On 23 Aug, 2020
Reviewers invited
Invitations sent on 19 Aug, 2020
Reviewer #1 agreed
On 19 Aug, 2020
Editor assigned
On 18 Aug, 2020
Submission checks complete
On 17 Aug, 2020
Editor invited
On 17 Aug, 2020
No comments provided
Review #1 received
Received 09 Aug, 2020
Editorial decision: Minor Revision
On 09 Aug, 2020
Review #4 received
Received 03 Aug, 2020
Review #2 received
Received 31 Jul, 2020
Reviewer #3 agreed
On 31 Jul, 2020
Reviewer #4 agreed
On 31 Jul, 2020
Review #3 received
Received 31 Jul, 2020
Reviewer #2 agreed
On 28 Jul, 2020
Reviewers invited
Invitations sent on 27 Jul, 2020
Reviewer #1 agreed
On 27 Jul, 2020
Editor assigned
On 22 Jul, 2020
Editor invited
On 21 Jul, 2020
Submission checks complete
On 15 Jul, 2020
First submitted
On 11 Jul, 2020
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Subject Areas
Applied & Industrial Microbiology
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A new preprint design is coming!
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See the published version of this preprint at AMB Express.
This is a preprint, a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Original article
Gholamreza Ahmadian
National Institute of Genetic Engineering and Biotechnology, Tehran, Iran
Corresponding Author
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Published
View the published article at AMB Express.
Version 2
Posted 24 Aug, 2020
No community comments so far
Reviewer #2 agreed
On 23 Aug, 2020
Review #1 received
Received 23 Aug, 2020
Review #2 received
Received 23 Aug, 2020
Editorial decision: Accept
On 23 Aug, 2020
Reviewers invited
Invitations sent on 19 Aug, 2020
Reviewer #1 agreed
On 19 Aug, 2020
Editor assigned
On 18 Aug, 2020
Submission checks complete
On 17 Aug, 2020
Editor invited
On 17 Aug, 2020
No comments provided
Review #1 received
Received 09 Aug, 2020
Editorial decision: Minor Revision
On 09 Aug, 2020
Review #4 received
Received 03 Aug, 2020
Review #2 received
Received 31 Jul, 2020
Reviewer #3 agreed
On 31 Jul, 2020
Reviewer #4 agreed
On 31 Jul, 2020
Review #3 received
Received 31 Jul, 2020
Reviewer #2 agreed
On 28 Jul, 2020
Reviewers invited
Invitations sent on 27 Jul, 2020
Reviewer #1 agreed
On 27 Jul, 2020
Editor assigned
On 22 Jul, 2020
Editor invited
On 21 Jul, 2020
Submission checks complete
On 15 Jul, 2020
First submitted
On 11 Jul, 2020
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
Subject Areas
Applied & Industrial Microbiology
License:
This work is licensed under a CC BY 4.0 License. Read Full License
View the published article at AMB Express.
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 analysiswas 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.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
This is a list of supplementary files associated with this preprint. Click to download.
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