Amyloids protect the silkmoth oocyte and embryo.
Chorion is the major component of silkmoth eggshell. More than 95% of its dry mass consists of proteins that have remarkable mechanical and chemical properties protecting the oocyte and the developing embryo from a wide range of environmental hazards. We present data from electron microscopy (negative staining and shadowing), X-ray diffraction and modeling studies of synthetic peptide analogues of silkmoth chorion proteins indicating that chorion is a natural amyloid. The folding and self-assembly models of chorion peptides strongly support the beta-sheet helix model of amyloid fibrils proposed recently by Blake and Serpell [Structure 4 (1996) 989-998].
Iconomidou
V A
VA
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Greece.
Vriend
G
G
Hamodrakas
S J
SJ
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry* / Q000502:physiology / Q000648:ultrastructure; D000818:Animals; D012831:Bombyx / Q000196:embryology*; D002823:Chorion / Q000737:chemistry; D004625:Embryo, Nonmammalian / Q000737:chemistry*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009865:Oocytes / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D000682:Amyloid; D010455:Peptides