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Journal of Neuroscience, Vol 9, 3332-3346, Copyright © 1989 by Society for Neuroscience
Expression of pheromone binding proteins during antennal development in the gypsy moth Lymantria dispar
RG Vogt, AC Kohne, JT Dubnau and GD Prestwich
Department of Chemistry, State University of New York, Stony Brook 11794.
We have identified 2 olfactory specific proteins in the gypsy moth
Lymantria dispar that are uniquely associated with the male antennae, the
principal olfactory organs of this animal. These proteins were the major
soluble protein components of the olfactory sensilla, present in equivalent
amounts. Both proteins comigrated on SDS-PAGE, showing an apparent
molecular mass of 15,000 Da but migrated separately on non-SDS- PAGE,
indicating differences in net charge. N-terminal amino acid sequence
analysis showed that the 2 proteins share 50% identity, indicating that
they are genetically distinct homologs. Both proteins bound the L. dispar
sexpheromone, associated with antisera prepared against the previously
identified phermone-binding protein (PBP) of the moth Antheraea polyphemus,
and shared sequence identity with the A. polyphemus PBP. These 2 proteins
are therefore identified as L. dispar PBPs and are termed PBP1 and PBP2
based on their migration differences on non-SDS-PAGE. It is estimated that
PBP1 and PBP2 are present in the sensilla lumen at a combined concentration
of 13.4 mM. The expression of the L. dispar PBPs was examined during the 11
d development of the adult antenna. PBP1 and PBP2 were first detected by
non-SDS-PAGE analysis and Coomassie blue staining 3 d before adult
eclosion, on day A-3. Levels increased, reaching a plateau on day A-1 that
continued into adult life. In vivo labeling studies indicated that the rate
of PBP synthesis increased from A-3 to a plateau on A-2, where it remained
into adult life. In vitro translations of antennal mRNAs indicated that
translatable PBP mRNA was available at a very low level on day A-4,
increased slightly on A-3 and dramatically on A-2, and remained at a high
level into adult life. PBP mRNA represented the major translatable mRNA in
the antenna during this period. It was estimated that the PBPs undergo a
combined steady-state turnover of 8 x 10(7) molecules/hr/sensillum. Cursory
in vivo and in vitro translation studies of antennal mRNA from A.
polyphemus and Manduca sexta showed similar temporal patterns of PBP
expression, suggesting that the L. dispar observations are general.
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