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Biological Characterization of Commercial Recombinantly Expressed Immunomodulating Proteins Contaminated with Bacterial Products in the Year 2020: The SAA3 Case
Joint Authors
Oliveira, Vívian Louise S. de
Abouelasrar Salama, Sara
De Bondt, Mirre
Berghmans, Nele
Gouwy, Mieke
Oliveira, Sergio C.
Amaral, Flavio A.
Proost, Paul
Van Damme, Jo
Struyf, Sofie
De Buck, Mieke
Source
Issue
Vol. 2020, Issue 2020 (31 Dec. 2020), pp.1-17, 17 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2020-07-06
Country of Publication
Egypt
No. of Pages
17
Main Subjects
Abstract EN
The serum amyloid A (SAA) gene family is highly conserved and encodes acute phase proteins that are upregulated in response to inflammatory triggers.
Over the years, a considerable amount of literature has been published attributing a wide range of biological effects to SAAs such as leukocyte recruitment, cytokine and chemokine expression and induction of matrix metalloproteinases.
Furthermore, SAAs have also been linked to protumorigenic, proatherogenic and anti-inflammatory effects.
Here, we investigated the biological effects conveyed by murine SAA3 (mu rSAA3) recombinantly expressed in Escherichia coli.
We observed the upregulation of a number of chemokines including CCL2, CCL3, CXCL1, CXCL2, CXCL6 or CXCL8 following stimulation of monocytic, fibroblastoid and peritoneal cells with mu rSAA3.
Furthermore, this SAA variant displayed potent in vivo recruitment of neutrophils through the activation of TLR4.
However, a major problem associated with proteins derived from recombinant expression in bacteria is potential contamination with various bacterial products, such as lipopolysaccharide, lipoproteins and formylated peptides.
This is of particular relevance in the case of SAA as there currently exists a discrepancy in biological activity between SAA derived from recombinant expression and that of an endogenous source, i.e.
inflammatory plasma.
Therefore, we subjected commercial recombinant mu rSAA3 to purification to homogeneity via reversed-phase high-performance liquid chromatography (RP-HPLC) and re-assessed its biological potential.
RP-HPLC-purified mu rSAA3 did not induce chemokines and lacked in vivo neutrophil chemotactic activity, but retained the capacity to synergize with CXCL8 in the activation of neutrophils.
In conclusion, experimental results obtained when using proteins recombinantly expressed in bacteria should always be interpreted with care.
American Psychological Association (APA)
Abouelasrar Salama, Sara& De Bondt, Mirre& Berghmans, Nele& Gouwy, Mieke& Oliveira, Vívian Louise S. de& Oliveira, Sergio C.…[et al.]. 2020. Biological Characterization of Commercial Recombinantly Expressed Immunomodulating Proteins Contaminated with Bacterial Products in the Year 2020: The SAA3 Case. Mediators of Inflammation،Vol. 2020, no. 2020, pp.1-17.
https://search.emarefa.net/detail/BIM-1191865
Modern Language Association (MLA)
Abouelasrar Salama, Sara…[et al.]. Biological Characterization of Commercial Recombinantly Expressed Immunomodulating Proteins Contaminated with Bacterial Products in the Year 2020: The SAA3 Case. Mediators of Inflammation No. 2020 (2020), pp.1-17.
https://search.emarefa.net/detail/BIM-1191865
American Medical Association (AMA)
Abouelasrar Salama, Sara& De Bondt, Mirre& Berghmans, Nele& Gouwy, Mieke& Oliveira, Vívian Louise S. de& Oliveira, Sergio C.…[et al.]. Biological Characterization of Commercial Recombinantly Expressed Immunomodulating Proteins Contaminated with Bacterial Products in the Year 2020: The SAA3 Case. Mediators of Inflammation. 2020. Vol. 2020, no. 2020, pp.1-17.
https://search.emarefa.net/detail/BIM-1191865
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1191865