News Column

Reports Outline Immunoglobulins Findings from M. Woisetschlager and Colleagues [In vivo and in vitro activity of an immunoglobulin Fc fragment (Fcab)...

August 20, 2014



Reports Outline Immunoglobulins Findings from M. Woisetschlager and Colleagues [In vivo and in vitro activity of an immunoglobulin Fc fragment (Fcab) with engineered Her-2/neu binding sites]

By a News Reporter-Staff News Editor at Biotech Week -- New research on Immunology is the subject of a report. According to news reporting from Vienna, Austria, by NewsRx journalists, research stated, "Antigen-binding Fc fragments (Fcabs) are a new unique class of immunotherapeutics. They are small (50 kD) fully functional antibody alternatives that bind antigen and elicit effector functions such as antibody-dependent cytotoxicity (ADCC) and complement-dependent cytotoxicity."

The news correspondents obtained a quote from the research, "Since Fcabs carry the natural FcRn binding site of antibodies, they have very favorable pharmacokinetics. We showed recently that Fcab H10-03-6 is a high-affinity binder of Her-2/neu (ErbB2/neu) mediating killing of Her-2/neu-overexpressing tumor cells in the presence of immune effector cells, strongly suggesting that the mechanism of killing is due to ADCC. The present study further confirms ADCC as the mechanism by which H10-03-6 mediates tumor cell killing, since H10-03-6 was shown to interact simultaneously with Her-2/neu and the Fc receptor CD16a. The epitope recognized by H10-03-6 overlaps with that of the clinically used monoclonal antibody trastuzumab. However, unlike trastuzumab, Fcab H10-03-6 did not inhibit proliferation of human tumor cells in vitro even under conditions favoring Her-2/neu crosslinking. Treatment of mice harboring human BT-474 cell xenograft tumors with Fcab H10-03-6 led to statistically significant retardation of tumor growth."

According to the news reporters, the research concluded: "For the first time, in vivo properties of an Fcab are presented, supporting the view that Fcabs could become highly efficacious immunotherapeutics for human use."

For more information on this research see: In vivo and in vitro activity of an immunoglobulin Fc fragment (Fcab) with engineered Her-2/neu binding sites. Biotechnology Journal, 2014;9(6):844-51. (Wiley-Blackwell - www.wiley.com/; Biotechnology Journal - onlinelibrary.wiley.com/journal/10.1002/(ISSN)1860-7314)

Our news journalists report that additional information may be obtained by contacting M. Woisetschlager, F-star GmbH, Vienna, Austria. Additional authors for this research include B. Antes, R. Borrowdale, S. Wiederkum, M. Kainer, H. Steinkellner, G. Wozniak-Knopp, K. Moulder, F. Ruker and G.C Mudde (see also Immunology).

Keywords for this news article include: Antibodies, Vienna, Europe, Austria, Immunology, Engineering, Blood Proteins, Immunoproteins, Serum Globulins, Immunoglobulin Fragments, Immunoglobulin Fc Fragments, Immunoglobulin Constant Regions.

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


For more stories covering the world of technology, please see HispanicBusiness' Tech Channel



Source: Biotech Week


Story Tools






HispanicBusiness.com Facebook Linkedin Twitter RSS Feed Email Alerts & Newsletters