title: Intravenous immunoglobulin reduces β amyloid and abnormal tau formation caused by herpes simplex virus type 1.
abstract: Intravenous immunoglobulin (IVIG) treatment of Alzheimer's disease (AD) has been encouraging. Its mechanism of action might be via anti-β-amyloid (Aβ) antibodies which facilitate Aβ clearance. However, IVIG's benefits might result from its antiviral activity, particularly against herpes simplex virus type 1 (HSV1), a virus implicated in AD. We investigated IVIG's effect on HSV1, specifically on the accumulation of Aβ and abnormally phosphorylated tau which it causes. We show that IVIG is effective at reducing the accumulation of these abnormal molecules and that it acts synergistically with the antiviral acyclovir, suggesting that their combined use would be beneficial for treating AD.
authors: Faculty of Life Sciences, The University of Manchester, Manchester, M13 9PT, UK.
authors: Matthew A
authors: MA
authors: Wozniak
authors: Ruth F
authors: RF
authors: Itzhaki
mesh_terms: D016229:Amyloid beta-Peptides / Q000009:adverse effects / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D000818:Animals; D002522:Chlorocebus aethiops; D018259:Herpesvirus 1, Human / Q000472:pathogenicity*; D016756:Immunoglobulins, Intravenous / Q000008:administration & dosage*; D014709:Vero Cells; D015678:Viral Structural Proteins / Q000037:antagonists & inhibitors / Q000096:biosynthesis; D016875:tau Proteins / Q000009:adverse effects / Q000037:antagonists & inhibitors* / Q000096:biosynthesis
chemical_list: D016229:Amyloid beta-Peptides; D016756:Immunoglobulins, Intravenous; D015678:Viral Structural Proteins; D016875:tau Proteins