In this paper we have engineered the targeting of ScFv fragments to mitochondria and demonstrated that this can occur efficiently. This extends the range of subcellular compartments where antibody domains can be targeted in order to interfere with the action of the corresponding antigen. Moreover, we have compared the redox state of ScFv fragments targeted to the secretory compartment, the cytosol and the mitochondria, and demonstrated that cysteine residues in ScFv targeted to the secretory compartments and to the mitochondria are oxidized. On the contrary, cytosolic antibody domains are expressed in a reduced state, which is probably the reason for their lower expression levels. These pitfalls, however, do not prevent their successful utilization for intracellular immunization.

Biocca, S., Ruberti, F., Tafani, M., Pierandrei Amaldi, P., Cattaneo, A. (1995). Redox state of single chain Fv fragments targeted to the endoplasmic reticulum, cytosol and mitochondria. BIO/TECHNOLOGY, 13(10), 1110-1115.

Redox state of single chain Fv fragments targeted to the endoplasmic reticulum, cytosol and mitochondria

BIOCCA, SILVIA;
1995-10-01

Abstract

In this paper we have engineered the targeting of ScFv fragments to mitochondria and demonstrated that this can occur efficiently. This extends the range of subcellular compartments where antibody domains can be targeted in order to interfere with the action of the corresponding antigen. Moreover, we have compared the redox state of ScFv fragments targeted to the secretory compartment, the cytosol and the mitochondria, and demonstrated that cysteine residues in ScFv targeted to the secretory compartments and to the mitochondria are oxidized. On the contrary, cytosolic antibody domains are expressed in a reduced state, which is probably the reason for their lower expression levels. These pitfalls, however, do not prevent their successful utilization for intracellular immunization.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/12
Settore BIO/13
English
Amino Acid Sequence; Animals; COS Cells; Cysteine; Cytosol; Disulfides; Dithiothreitol; Electron Transport Complex IV; Endoplasmic Reticulum; Fluorescent Antibody Technique; Gene Expression; Immunoglobulin Fragments; Mitochondria; Molecular Sequence Data; Oxidation-Reduction; Protein Sorting Signals; Proto-Oncogene Proteins p21(ras); Recombinant Fusion Proteins; Transfection; ras Proteins
Biocca, S., Ruberti, F., Tafani, M., Pierandrei Amaldi, P., Cattaneo, A. (1995). Redox state of single chain Fv fragments targeted to the endoplasmic reticulum, cytosol and mitochondria. BIO/TECHNOLOGY, 13(10), 1110-1115.
Biocca, S; Ruberti, F; Tafani, M; Pierandrei Amaldi, P; Cattaneo, A
Articolo su rivista
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/129912
Citazioni
  • ???jsp.display-item.citation.pmc??? 33
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact