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Isolation and characterization of bacteria‐induced protein P4 from hemolymph of Manduca sexta
Author(s) -
Ladendorff Noma E.,
Kanost Michael R.
Publication year - 1990
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940150104
Subject(s) - manduca sexta , hemolymph , biology , biochemistry , isoelectric point , sphingidae , prophenoloxidase , bacteria , microbiology and biotechnology , insect , enzyme , botany , innate immune system , genetics , receptor
Insects synthesize several types of hemolymph proteins in response to bacterial infection. The objective of this study was to characterize a 48,000 dalton hemolymph protein induced in larvae of Manduca sexta after injection of bacteria. The protein, isolated by cation exchange and gel filtration chromatography from hemolymph of larvae injected with Micrococcus lysodeikticus , was found to be a glycoprotein with pl = 8.4. The molecular weight, isoelectric point, amino acid composition, and NH 2 terminal sequence of the protein are similar to bacteria‐induced protein P4 from Hyalophora cecropia , and the M. sexta protein is also designated P4. The hemolymph concentration of M. sexta P4 (35 ± 7 μg/ml in day 3 fifth instar larvae) increases 30‐ to 45‐fold by 48 h after injection of bacteria, but it does not increase in response to injection of distilled water. Lower levels of induction occur after injection of peptidoglycan fragments, zymosan, and lipopolysaccharide. The properties of M. sexta P4 are very similar to those of a previously characterized M. sexta hemolymph protein known as postlarval protein , and antibodies against P4 bind to postlarval protein.