โ Scribed by T. R. Kyriakides; J. L. McKillip; K. D. Spence
No coin nor oath required. For personal study only.
The immune protein, scolexin, a bacteria-induced, larva-specific protein from Manduca sexta, was shown to exist in the hemolymph in two isoelectric forms designated herein as scolexin-1 and scolexin-2 (native M, -72 kd). These two charge isomers appeared to share the same amino acid composition. Scolexin is composed of two subunits (peptide M, -36 kd) that possess the same Nterminus. Scolexin-2 was subjected to glycosyl composition analysis, revealing the presence of galactose, glucose, mannose, xylose, and sialic acid residues.
Hybridization of epidermal RNA with oligonucleotides deduced from the scolexin N-terminal sequence showed a continuous decline in mRNA following day 0 of the 5th larval instar. By employing in vitro protein labelling, it was found that organ cultures of the epidermis from immune larvae showed a greater ability over that of naive epidermal cultures to synthesize scolexin; these data reflected the inducible response seen i n the hemolymph, and confirm other data indicating that the epidermis is an important site of scolexin biosynthesis. Q 1995 WiIey-Liss, Inc.
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