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Erratum

Erratum

Page 1037 | Published online: 12 Jun 2008

In the review “Antibody–cytokine fusion proteins: applications in cancer therapy”, published in the May 2008 issue of Expert Opinion on Biological Therapy (Expert Opin. Biol. Ther. (2008) 8(5):609-32), should have been printed in colour in order to help the audience to properly understand the important concept that this figure describes. Due to a printing error, this figure appeared in black and white; the lack of colour resulted in the loss of critical information and lack of accuracy. The online version was correct. Please see the colour version of below.

Informa Healthcare would like to apologise for this mistake, which was caused by an oversight by the printing company. The authors (Elizabeth Ortiz-Sánchez, Gustavo Helguera, Tracy R Daniels & Manuel L Penichet) had paid the corresponding fee for colour printing.

Figure 5. Schematic model of the mechanism involved in the antitumor effect of vaccination with complexes consisting of ECDHER2 and anti-HER2/neu IgG3-(IL-2) in DC. Anti-HER2/neu IgG3-(IL-2) can bind HER2/neu expressed as soluble antigen ECDHER2. This soluble antigen is poorly processed because of its high level of glycosylation that results in its binding to the mannose receptor, early endosomal retention, and recycling back to the cell surface. However, the interaction between the complex of ECDHER2 plus anti-HER2/neu IgG3-(IL-2) with IL-2 receptor (IL-2R) expressed on the cell surface induces ECDHER2 internalization and trafficking to the late endosome/lysosome MHC class II pathway facilitating the processing and presentation to CD4+ T cells via MHC class II molecules in order to stimulate the immune response against HER2/neu positive tumor cells.
Figure 5. Schematic model of the mechanism involved in the antitumor effect of vaccination with complexes consisting of ECDHER2 and anti-HER2/neu IgG3-(IL-2) in DC. Anti-HER2/neu IgG3-(IL-2) can bind HER2/neu expressed as soluble antigen ECDHER2. This soluble antigen is poorly processed because of its high level of glycosylation that results in its binding to the mannose receptor, early endosomal retention, and recycling back to the cell surface. However, the interaction between the complex of ECDHER2 plus anti-HER2/neu IgG3-(IL-2) with IL-2 receptor (IL-2R) expressed on the cell surface induces ECDHER2 internalization and trafficking to the late endosome/lysosome MHC class II pathway facilitating the processing and presentation to CD4+ T cells via MHC class II molecules in order to stimulate the immune response against HER2/neu positive tumor cells.

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