Characterization of Aplysia attractin, the first water-borne peptide pheromone in invertebrates

Sherry D. Painter, Bret Clough, Rebecca W. Garden, Jonathan V. Sweedler, Gregg Thomas Nagle

Research output: Contribution to journalArticle

79 Citations (Scopus)

Abstract

Although animals in the genus Aplysia are solitary during most of the year, they form breeding aggregations during the reproductive season. The aggregations contain both mating and egg-laying animals and are associated with masses of egg cordons. The egg cordons are a source of pheromones that establish and maintain the aggregation, but none of the pheromonal factors have been chemically characterized. In these studies, specimens of Aplysia were induced to lay eggs, the egg cordons collected and eluted, and the eluates fractionated by C18 reversed-phase HPLC. Four peak fractions were bioassayed in a T-maze. All four increased the number of animals attracted to a nonlaying conspecific and were thus subjected to compositional and microsequence analysis. Each contained the same NH2-terminal peptide sequence. The full-length peptide ('attractin') was isolated from the albumen gland, a large exocrine organ that packages the eggs into a cordon. The complete 58-residue sequence was obtained, and it matched that predicted by an albumen gland cDNA. Mass spectrometry showed that attractin is 21 wt. % carbohydrate as the result of N-linked glycosylation. T-maze bioassays confirmed that the full-length peptide is attractive. Attractin is the first water-borne peptide pheromone characterized in molluscs, and the first in invertebrates.

Original languageEnglish (US)
Pages (from-to)120-131
Number of pages12
JournalBiological Bulletin
Volume194
Issue number2
DOIs
StatePublished - Jan 1 1998

Fingerprint

Aplysia
Pheromones
Invertebrates
pheromones
Ovum
invertebrates
peptides
Peptides
Water
Eggs
water
animals
Mollusca
reversed-phase high performance liquid chromatography
glycosylation
Glycosylation
Biological Assay
egg masses
molluscs
Breeding

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)

Cite this

Characterization of Aplysia attractin, the first water-borne peptide pheromone in invertebrates. / Painter, Sherry D.; Clough, Bret; Garden, Rebecca W.; Sweedler, Jonathan V.; Nagle, Gregg Thomas.

In: Biological Bulletin, Vol. 194, No. 2, 01.01.1998, p. 120-131.

Research output: Contribution to journalArticle

Painter, Sherry D. ; Clough, Bret ; Garden, Rebecca W. ; Sweedler, Jonathan V. ; Nagle, Gregg Thomas. / Characterization of Aplysia attractin, the first water-borne peptide pheromone in invertebrates. In: Biological Bulletin. 1998 ; Vol. 194, No. 2. pp. 120-131.
@article{7b7404b88eca4686b847504b28fb37eb,
title = "Characterization of Aplysia attractin, the first water-borne peptide pheromone in invertebrates",
abstract = "Although animals in the genus Aplysia are solitary during most of the year, they form breeding aggregations during the reproductive season. The aggregations contain both mating and egg-laying animals and are associated with masses of egg cordons. The egg cordons are a source of pheromones that establish and maintain the aggregation, but none of the pheromonal factors have been chemically characterized. In these studies, specimens of Aplysia were induced to lay eggs, the egg cordons collected and eluted, and the eluates fractionated by C18 reversed-phase HPLC. Four peak fractions were bioassayed in a T-maze. All four increased the number of animals attracted to a nonlaying conspecific and were thus subjected to compositional and microsequence analysis. Each contained the same NH2-terminal peptide sequence. The full-length peptide ('attractin') was isolated from the albumen gland, a large exocrine organ that packages the eggs into a cordon. The complete 58-residue sequence was obtained, and it matched that predicted by an albumen gland cDNA. Mass spectrometry showed that attractin is 21 wt. {\%} carbohydrate as the result of N-linked glycosylation. T-maze bioassays confirmed that the full-length peptide is attractive. Attractin is the first water-borne peptide pheromone characterized in molluscs, and the first in invertebrates.",
author = "Painter, {Sherry D.} and Bret Clough and Garden, {Rebecca W.} and Sweedler, {Jonathan V.} and Nagle, {Gregg Thomas}",
year = "1998",
month = "1",
day = "1",
doi = "10.2307/1543042",
language = "English (US)",
volume = "194",
pages = "120--131",
journal = "Biological Bulletin",
issn = "0006-3185",
publisher = "Marine Biological Laboratory",
number = "2",

}

TY - JOUR

T1 - Characterization of Aplysia attractin, the first water-borne peptide pheromone in invertebrates

AU - Painter, Sherry D.

AU - Clough, Bret

AU - Garden, Rebecca W.

AU - Sweedler, Jonathan V.

AU - Nagle, Gregg Thomas

PY - 1998/1/1

Y1 - 1998/1/1

N2 - Although animals in the genus Aplysia are solitary during most of the year, they form breeding aggregations during the reproductive season. The aggregations contain both mating and egg-laying animals and are associated with masses of egg cordons. The egg cordons are a source of pheromones that establish and maintain the aggregation, but none of the pheromonal factors have been chemically characterized. In these studies, specimens of Aplysia were induced to lay eggs, the egg cordons collected and eluted, and the eluates fractionated by C18 reversed-phase HPLC. Four peak fractions were bioassayed in a T-maze. All four increased the number of animals attracted to a nonlaying conspecific and were thus subjected to compositional and microsequence analysis. Each contained the same NH2-terminal peptide sequence. The full-length peptide ('attractin') was isolated from the albumen gland, a large exocrine organ that packages the eggs into a cordon. The complete 58-residue sequence was obtained, and it matched that predicted by an albumen gland cDNA. Mass spectrometry showed that attractin is 21 wt. % carbohydrate as the result of N-linked glycosylation. T-maze bioassays confirmed that the full-length peptide is attractive. Attractin is the first water-borne peptide pheromone characterized in molluscs, and the first in invertebrates.

AB - Although animals in the genus Aplysia are solitary during most of the year, they form breeding aggregations during the reproductive season. The aggregations contain both mating and egg-laying animals and are associated with masses of egg cordons. The egg cordons are a source of pheromones that establish and maintain the aggregation, but none of the pheromonal factors have been chemically characterized. In these studies, specimens of Aplysia were induced to lay eggs, the egg cordons collected and eluted, and the eluates fractionated by C18 reversed-phase HPLC. Four peak fractions were bioassayed in a T-maze. All four increased the number of animals attracted to a nonlaying conspecific and were thus subjected to compositional and microsequence analysis. Each contained the same NH2-terminal peptide sequence. The full-length peptide ('attractin') was isolated from the albumen gland, a large exocrine organ that packages the eggs into a cordon. The complete 58-residue sequence was obtained, and it matched that predicted by an albumen gland cDNA. Mass spectrometry showed that attractin is 21 wt. % carbohydrate as the result of N-linked glycosylation. T-maze bioassays confirmed that the full-length peptide is attractive. Attractin is the first water-borne peptide pheromone characterized in molluscs, and the first in invertebrates.

UR - http://www.scopus.com/inward/record.url?scp=0032051672&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032051672&partnerID=8YFLogxK

U2 - 10.2307/1543042

DO - 10.2307/1543042

M3 - Article

C2 - 9604313

AN - SCOPUS:0032051672

VL - 194

SP - 120

EP - 131

JO - Biological Bulletin

JF - Biological Bulletin

SN - 0006-3185

IS - 2

ER -