Therapeutic efficacy of an E. coli strain carrying an ovalbumin allergenic peptide as a fused protein to OMPC in a murine model of allergic airway inflammation

Yepez, Sara Huerta; Hernández-Pando, Rogelio; Santos-Argumedo, Leopoldo; Paredes, Mario Vega; Cueto, Angeles Hernández; Isibasí, Armando; Bonilla, César R.González

doi:10.1016/s0264-410x(02)00244-x

Cited by 7 publications

(4 citation statements)

References 37 publications

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“…2c, lanes 2 and 4). This result is consistent with a similar fusion protein in which a foreign sequence was inserted in the fifth loop of OmpC, 42 and may be explained by low efficiency in codon usage, but this issue needs to be further analysed. However, the Western blot using a cocktail of monoclonal antibodies against OmpC was consistent with the electrophoretic pattern (Fig.…”

Section: Resultssupporting

confidence: 86%

“…These permissive sites are located in the external loops, and that porins in solution have the property to aggregate as trimers. OmpC and other porins have been used for the expression of foreign ‘passenger’ antigens and we have reported that an allergenic peptide fused to the external loop five of OmpC is able to modulate the lung inflammatory response in a mouse model of allergy to ovalbumin 42 …”

Section: Discussionmentioning

confidence: 99%

“…OmpC and other porins have been used for the expression of foreign`passenger' antigens and we have reported that an allergenic peptide fused to the external loop ®ve of OmpC is able to modulate the lung in¯ammatory response in a mouse model of allergy to ovalbumin. 42 The assumption that a fusion protein bearing a small CD154 amino acid strand is able to bind CD40 and induce activation is inconsistent with the model of a trimeric structure as necessary for CD154/CD40 function. Nevertheless, it has been demonstrated that CD154 engages and clusters CD40 in a similar way to other cellular surface receptors, moving through the cell membrane in rafts constituted by detergent insensitive glycosphingolipid rich domains.…”

Section: Discussionmentioning

confidence: 99%

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A Salmonella typhi OmpC fusion protein expressing the CD154 Trp140–Ser149 amino acid strand binds CD40 and activates a lymphoma B‐cell line

et al. 2003

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SUMMARYCD154 is a type II glycoprotein member of the tumour necrosis factor (TNF) ligand family, which is expressed mainly on the surface of activated T lymphocytes. The interaction with its receptor CD40, plays a central role in the control of several functions of the immune system. Structural models based on the homology of CD154 with TNF and lymphotoxin indicate that binding to CD40 involves three regions surrounding amino acids K143, R203 and Q220, and that strands W140±S149 and S198±A210 are critical for such interactions. Also, it has been reported that two recombinant CD154 fragments, including amino acid residues Y45±L261 or E108±L261 are biologically active, whereas other polypeptides, including S149±L261, are not. Therefore, we decided to construct a fusion protein inserting the W140-S149 amino acid strand (WAEKGYYTMS) in an external loop of the outer membrane protein C (OmpC) from Salmonella enterica serovar Typhi and assess its ability to bind CD40 and activate B cells. The sodium dodecyl sulphate±polyacrylamide gel electrophoresis demonstrated that the chimeric OmpC±gp39 protein conserved its ability to form trimers. Binding to CD40 was established by three variants of enzyme-linked immunosorbent assay, a direct binding assay by coating plates with a recombinant CD40±Fc protein and through two competition assays between OmpC±gp39 and recombinant CD154 or soluble CD40±Fc. Flow cytometry analysis demonstrated that OmpC±gp39 increased the expression levels of major histocompatibility complex II, CD23, and CD80, in Raji human B-cell lymphoma similarly to an antibody against CD40. These results further support that the CD154/CD40 interaction is similar to the TNF/TNF receptor. This is the ®rst report of a bacterial fusion protein containing a small amino acid strand form a ligand that is able to activate its cognate receptor.

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Section: Resultssupporting

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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A Salmonella typhi OmpC fusion protein expressing the CD154 Trp140–Ser149 amino acid strand binds CD40 and activates a lymphoma B‐cell line

et al. 2003

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“…Previous studies have shown that the insertions into these long loops did not affect the trimerization or the insertion of these porins into the cell membrane . An allergenic peptide of 16 amino acids from ovalbumin and a rotavirus epitope comprising 18 amino acids have been successfully displayed on the loops of S. typhi OmpC . Short epitopes inserted into the long surface accessible loops induce epitope‐specific immune responses and are thus appealing candidates for live recombinant vaccines.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Salmonella typhi OmpC and OmpF porins engineered with HIV‐gp41 epitope on the surface loops

et al. 2017

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Porins form trimers in the outer membrane and help transport nutrients and waste products across the bacterial cell membrane. Porin loops are suitable candidates as display systems due to their high immunogenicity and presentation at the bacterial cell surface. In this study, Salmonella typhi porins (OmpC and OmpF) engineered with the Kennedy peptide from gp41 of HIV were characterised. The chimeric OmpC carrying the Kennedy peptide in loop7 did not trimerise, whereas the chimeric OmpF with the epitope in loop5 formed trimers and also was recognised by the antibodies in the HIV patient serum. The results suggest that chimeric S. typhi OmpF may be taken further as a potential candidate to develop as an epitope display system. Proteins 2017; 85:657-664. © 2016 Wiley Periodicals, Inc.

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2-Methoxyestradiol (2-ME) reduces the airway inflammation and remodeling in an experimental mouse model

Huerta-Yépez

Baay-Guzmán

Garcia-Zepeda

et al. 2008

Clinical Immunology

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Therapeutic efficacy of an E. coli strain carrying an ovalbumin allergenic peptide as a fused protein to OMPC in a murine model of allergic airway inflammation

Cited by 7 publications

References 37 publications

A Salmonella typhi OmpC fusion protein expressing the CD154 Trp140–Ser149 amino acid strand binds CD40 and activates a lymphoma B‐cell line

A Salmonella typhi OmpC fusion protein expressing the CD154 Trp140–Ser149 amino acid strand binds CD40 and activates a lymphoma B‐cell line

Characterization of Salmonella typhi OmpC and OmpF porins engineered with HIV‐gp41 epitope on the surface loops

2-Methoxyestradiol (2-ME) reduces the airway inflammation and remodeling in an experimental mouse model

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