Supplementary Materials

Supplementary Material for:

Amyloid-β peptide protects against microbial infection in mouse and worm models of Alzheimer's disease

Deepak Kumar Vijaya Kumar, Se Hoon Choi, Kevin J. Washicosky, William A. Eimer, Stephanie Tucker, Jessica Ghofrani, Aaron Lefkowitz, Gawain McColl, Lee E. Goldstein, Rudolph E. Tanzi,* Robert D. Moir*

*Corresponding author. Email: moir{at}helix.mgh.harvard.edu (R.D.M.); tanzi{at}helix.mgh.harvard.edu (R.E.T.)

Published 25 May 2016, Sci. Transl. Med. 8, 340ra72 (2016)
DOI: 10.1126/scitranslmed.aaf1059

This PDF file includes:

  • Materials and Methods
  • Fig. S1. Aβ deposition and inflammation in 5XFAD mice before infection and criteria used for assessing clinical performance after infection.
  • Fig. S2. Aβ42 localizes to gut and muscle in GMC101 nematodes.
  • Fig. S3. Aβ expression protects GMC101 nematodes and CHO-CAB cells against S. Typhimurium.
  • Fig. S4. Confirmation of increased Candida resistance among transformed host cells using three independent assays.
  • Fig. S5. Transformed cell lines generate Aβ oligomers at levels found in the soluble fraction of human brain.
  • Fig. S6. Transformed H4-Aβ40 and CHO-CAB host cells resist Candida colonization and agglutinate yeast.
  • Fig. S7. Birefringence of Congo red–stained yeast aggregates from H4-Aβ42 medium.
  • Fig. S8. Anti-Aβ antibodies do not label CL2122 tissues or yeast.
  • Fig. S9. β-Amyloid colocalizes with S. Typhimurium cells in 5XFAD brain.
  • Fig. S10. Model for antimicrobial activities of soluble Aβ oligomers.
  • Table S1. Figure micrographs are representative of data from multiple repeat experiments and image fields.
  • Legend for video S1

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Other Supplementary Material for this manuscript includes the following:

  • Video S1 (.mov format). Z-section projection of 5XFAD mouse brain showing β-amyloid entrapment of S. Typhimurium cells.

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