Does the Amazon suffer from BSE prevention?

In the last decade, large-scale production of soybeans has been a major driver of the enhanced deforestation in the Brazilian Amazon. We show that these soybeans are mainly exported to the EU to substitute for the BSE related banned meat and bone meal in livestock feed. This strongly suggests a link between Brazilian rainforest disappearance and BSE prevention. (c) 2006 Elsevier B.V. All rights reserved

Fc galactosylation of anti-platelet human IgG1 alloantibodies enhances complement activation on platelets

Approximately 20% of patients receiving multiple platelet transfusions develop platelet alloantibodies, which can be directed against human leukocyte antigens (HLA) and, to a lesser extent, against human platelet antigens (HPA). These anti-bodies can lead to the rapid clearance of donor platelets, presumably through IgG-Fc receptor (Fc gamma R)-mediated phagocytosis or via complement activation, resulting in platelet refractoriness. Strikingly, not all patients with anti-HLA or-HPA antibodies develop platelet refractoriness upon unmatched platelet transfusions. Previously, we found that IgG Fc glycosylation of anti-HLA antibodies was highly variable between patients with platelet refractoriness, especially with respect to galactosylation and sialylation of the Fc-bound sugar moiety. Here, we produced recombinant glycoengineered anti-HLA and anti-HPA-1a monoclonal antibodies with varying Fc galactosylation and sialylation levels and studied their ability to activate the classical complement pathway. We observed that anti-HLA monoclonal antibodies with different specificities, binding simultaneously to the same HLA-molecules, or anti-HLA in combination with anti-HPA-1a monoclonal antibodies interacted synergistically with C1q, the first component of the classical pathway. Elevated Fc galactosylation and, to a lesser extent, sialylation significantly increased the complement-activating properties of anti-HLA and anti-HPA-1a monoclonal antibodies. We propose that both the breadth of the polyclonal immune response, with recognition of different HLA epitopes and in some cases HPA antigens, and the type of Fc glycosylation can provide an optimal stoichiometry for C1q binding and sub-sequent complement activation. These factors can shift the effect of a platelet alloimmune response to a clinically relevant response, leading to complement-mediated clearance of donor platelets, as observed in platelet refractoriness.Proteomic

Fc galactosylation of anti-platelet hIgG1 alloantibodies enhance complement activation on platelets

Transplantation and autoimmunit