On the primary structures of lysozyme, cecropins and attacins from Hyalophora cecropia

H G Boman; I Faye; P von Hofsten; K Kockum; J Y Lee; K G Xanthopoulos; H Bennich; A Engström; R B Merrifield; D Andreu

doi:10.1016/0145-305x(85)90018-7

On the primary structures of lysozyme, cecropins and attacins from Hyalophora cecropia

Dev Comp Immunol. 1985 Summer;9(3):551-8. doi: 10.1016/0145-305x(85)90018-7.

Authors

H G Boman, I Faye, P von Hofsten, K Kockum, J Y Lee, K G Xanthopoulos, H Bennich, A Engström, R B Merrifield, D Andreu

PMID: 3840100
DOI: 10.1016/0145-305x(85)90018-7

Abstract

Diapausing pupae of Cecropia respond to a bacterial infection by the selective synthesis of RNA and 15-20 hemolymph proteins. Of these we have purified lysozyme and two classes of antibacterial proteins called cecropins and attacins. The primary structure has been determined for the lysozyme, one attacin and five cecropins. We have also prepared a cDNA bank, isolated and sequenced clones corresponding to the lysozyme, the two main attacins and one cecropin. The results of these structural studies are briefly summarized. Finally we review the solid phase synthesis of cecropin A and B and 9 analogs of cecropin A.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Sequence
Animals
Antimicrobial Cationic Peptides*
DNA / genetics
Insect Hormones / genetics
Insect Hormones / isolation & purification*
Insect Proteins*
Lepidoptera / analysis*
Moths / analysis*
Moths / genetics
Muramidase / genetics
Muramidase / isolation & purification*
Sequence Homology, Nucleic Acid

Substances

Antimicrobial Cationic Peptides
Insect Hormones
Insect Proteins
attacin antibacterial protein, insect
cecropin A
cecropin B protein, Insecta
cecropin D protein, Hyalophora cecropia
DNA
Muramidase