Molluscan attractins, a family of water-borne protein pheromones with interspecific attractiveness

Scott F. Cummins, Catherine H. Schein, Yuan Xu, Werner Braun, Gregg T. Nagle

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

The marine mollusk Aplysia releases the water-borne pheromone attractin during egg laying. This small protein stimulates the formation and maintenance of mating and egg-laying aggregations. Attractin has been characterized from five Aplysia species: A. californica, A. brasiliana, A. fasciata, A. vaccaria, and A. depilans. We describe here the isolation of attractin from Bursatella leachii, and show that it belongs to the same protein family. The pattern of residue conservation, especially the six invariant cysteines, suggests that all of these attractins have a common fold. The nuclear magnetic resonance solution structure of A. californica attractin contains two antiparallel α-helices, the second of which contains the heptapeptide sequence IEECKTS that has been implicated in attractin function. Synthetic peptides containing this IEECKTS region are attractive, and mutating surface exposed charged residues within this region of attractin abolishes attractin activity. This suggests that the second helix is an essential part of the receptor-binding interface. In contrast to the peptide pheromonal attractants in amphibians, which are species specific, the attractins are, to our knowledge, the first water-borne peptide or protein pheromone family in invertebrates and vertebrates that are not species specific.

Original languageEnglish (US)
Pages (from-to)121-129
Number of pages9
JournalPeptides
Volume26
Issue number1
DOIs
StatePublished - Jan 2005

Fingerprint

Pheromones
Aplysia
Peptides
Vaccaria
Ovum
Water
Proteins
Mollusca
Amphibians
Invertebrates
Cysteine
Vertebrates
Conservation
Magnetic Resonance Spectroscopy
Agglomeration
Maintenance
Nuclear magnetic resonance

Keywords

  • Albumen gland
  • Aplysia
  • Attractin
  • Bursatella leachii
  • Mollusk
  • Protein pheromone

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

Cite this

Molluscan attractins, a family of water-borne protein pheromones with interspecific attractiveness. / Cummins, Scott F.; Schein, Catherine H.; Xu, Yuan; Braun, Werner; Nagle, Gregg T.

In: Peptides, Vol. 26, No. 1, 01.2005, p. 121-129.

Research output: Contribution to journalArticle

Cummins, Scott F. ; Schein, Catherine H. ; Xu, Yuan ; Braun, Werner ; Nagle, Gregg T. / Molluscan attractins, a family of water-borne protein pheromones with interspecific attractiveness. In: Peptides. 2005 ; Vol. 26, No. 1. pp. 121-129.
@article{ed7468776def4376a1964bfd5107b662,
title = "Molluscan attractins, a family of water-borne protein pheromones with interspecific attractiveness",
abstract = "The marine mollusk Aplysia releases the water-borne pheromone attractin during egg laying. This small protein stimulates the formation and maintenance of mating and egg-laying aggregations. Attractin has been characterized from five Aplysia species: A. californica, A. brasiliana, A. fasciata, A. vaccaria, and A. depilans. We describe here the isolation of attractin from Bursatella leachii, and show that it belongs to the same protein family. The pattern of residue conservation, especially the six invariant cysteines, suggests that all of these attractins have a common fold. The nuclear magnetic resonance solution structure of A. californica attractin contains two antiparallel α-helices, the second of which contains the heptapeptide sequence IEECKTS that has been implicated in attractin function. Synthetic peptides containing this IEECKTS region are attractive, and mutating surface exposed charged residues within this region of attractin abolishes attractin activity. This suggests that the second helix is an essential part of the receptor-binding interface. In contrast to the peptide pheromonal attractants in amphibians, which are species specific, the attractins are, to our knowledge, the first water-borne peptide or protein pheromone family in invertebrates and vertebrates that are not species specific.",
keywords = "Albumen gland, Aplysia, Attractin, Bursatella leachii, Mollusk, Protein pheromone",
author = "Cummins, {Scott F.} and Schein, {Catherine H.} and Yuan Xu and Werner Braun and Nagle, {Gregg T.}",
year = "2005",
month = "1",
doi = "10.1016/j.peptides.2004.07.017",
language = "English (US)",
volume = "26",
pages = "121--129",
journal = "Peptides",
issn = "0196-9781",
publisher = "Elsevier Inc.",
number = "1",

}

TY - JOUR

T1 - Molluscan attractins, a family of water-borne protein pheromones with interspecific attractiveness

AU - Cummins, Scott F.

AU - Schein, Catherine H.

AU - Xu, Yuan

AU - Braun, Werner

AU - Nagle, Gregg T.

PY - 2005/1

Y1 - 2005/1

N2 - The marine mollusk Aplysia releases the water-borne pheromone attractin during egg laying. This small protein stimulates the formation and maintenance of mating and egg-laying aggregations. Attractin has been characterized from five Aplysia species: A. californica, A. brasiliana, A. fasciata, A. vaccaria, and A. depilans. We describe here the isolation of attractin from Bursatella leachii, and show that it belongs to the same protein family. The pattern of residue conservation, especially the six invariant cysteines, suggests that all of these attractins have a common fold. The nuclear magnetic resonance solution structure of A. californica attractin contains two antiparallel α-helices, the second of which contains the heptapeptide sequence IEECKTS that has been implicated in attractin function. Synthetic peptides containing this IEECKTS region are attractive, and mutating surface exposed charged residues within this region of attractin abolishes attractin activity. This suggests that the second helix is an essential part of the receptor-binding interface. In contrast to the peptide pheromonal attractants in amphibians, which are species specific, the attractins are, to our knowledge, the first water-borne peptide or protein pheromone family in invertebrates and vertebrates that are not species specific.

AB - The marine mollusk Aplysia releases the water-borne pheromone attractin during egg laying. This small protein stimulates the formation and maintenance of mating and egg-laying aggregations. Attractin has been characterized from five Aplysia species: A. californica, A. brasiliana, A. fasciata, A. vaccaria, and A. depilans. We describe here the isolation of attractin from Bursatella leachii, and show that it belongs to the same protein family. The pattern of residue conservation, especially the six invariant cysteines, suggests that all of these attractins have a common fold. The nuclear magnetic resonance solution structure of A. californica attractin contains two antiparallel α-helices, the second of which contains the heptapeptide sequence IEECKTS that has been implicated in attractin function. Synthetic peptides containing this IEECKTS region are attractive, and mutating surface exposed charged residues within this region of attractin abolishes attractin activity. This suggests that the second helix is an essential part of the receptor-binding interface. In contrast to the peptide pheromonal attractants in amphibians, which are species specific, the attractins are, to our knowledge, the first water-borne peptide or protein pheromone family in invertebrates and vertebrates that are not species specific.

KW - Albumen gland

KW - Aplysia

KW - Attractin

KW - Bursatella leachii

KW - Mollusk

KW - Protein pheromone

UR - http://www.scopus.com/inward/record.url?scp=11144314747&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=11144314747&partnerID=8YFLogxK

U2 - 10.1016/j.peptides.2004.07.017

DO - 10.1016/j.peptides.2004.07.017

M3 - Article

C2 - 15626512

AN - SCOPUS:11144314747

VL - 26

SP - 121

EP - 129

JO - Peptides

JF - Peptides

SN - 0196-9781

IS - 1

ER -