Abstract
Six closely related antibacterial proteins, attacins A-F, were isolated from the hemolymph of immunized pupae of the Cecropia moth, Hyalophora cecropia. Chromatofocusing separated attacins A-F, with isoelectric points between 5.7 and 8.3. Immunological experiments show that the attacins constitute antibacterially active forms of the previously isolated inducible immune protein P5. Their mol. wts., 20-23 K, are similar to that of protein P5, but significantly lower than 28 K found for preP5 synthesized in vitro (see accompanying paper). The six attacins can be divided into two groups according to their amino acid composition and amino-terminal sequences, attacins A-D constitute a basic group and attacins E and F an acidic one. Within each group the forms are very similar. The attacins efficiently killed Escherichia coli and two other Gram-negative bacteria isolated from the gut of a silk worm but they did not act on other Gram-positive and Gram-negative bacteria tested. Only growing cells of E. coli were attacked; cells suspended in phosphate buffer were inert. Besides the cecropins and lysozyme, the attacins represent a third class of antibacterial proteins in the humoral immune system of H. cecropia.
MeSH Terms
Amino Acid Sequence
Animals
Anti-Bacterial Agents/isolation & purification,pharmacology
Bacteria/drug effects
Hemolymph/analysis
Insect Hormones/isolation & purification,pharmacology
Insect Proteins
Lepidoptera/immunology
Moths/immunology
Pupa/immunology
Chemicals
Anti-Bacterial Agents
Insect Hormones
Insect Proteins
attacin antibacterial protein, insect
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hultmark D
Engström A
Andersson K
Steiner H
Bennich H
Boman H G
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