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A conserved heptapeptide sequence in the waterborne attractin pheromone stimulates mate attraction in Aplysia

  • Scott F. Cummins
    ,
  • Amy E. Nichols
    ,
  • Krishna Rajarathnam
    ,
  • Gregg T. Nagle(corresponding author)
*Corresponding author for this work
  • University of Texas Medical Branch at Galveston
Scholary Output:
Contribution to journal
Article
Peer-review

Open access

Sustainable Development Goals

  • SDG 14 - Life Below Water
    SDG 14 Life Below Water

Abstract

Mate attraction in the marine mollusk Aplysia involves long-distance waterborne chemical signaling via the release of the peptide pheromone attractin during egg laying. Aplysia californica attractin attracts conspecifics, reduces the latency to mating, and stimulates hermaphroditic mating. Four additional members of the Aplysia attractin family have recently been characterized from Aplysia brasiliana, Aplysia fasciata, Aplysia depilans, and Aplysia vaccaria. The five sequences differ significantly, but share six cysteine residues and the strictly conserved sequence Ile30-Glu-Glu- Cys-Lys-Thr-Ser36. Attractin is attractive to geographically and evolutionarily distant species, suggesting that the conserved heptapeptide region may be important for mate attraction. Consistent with this prediction, a synthetic constrained cyclic peptide that contains the conserved heptapeptide sequence is significantly attractive in T-maze bioassays. The attractins are the first family of waterborne peptide pheromones characterized in invertebrates and are unique in that family members are not species-specific pheromonal attractants.

Publication Information

Output type

Scholary Output:
Contribution to journal
Article
Peer-review

Original language

English (US)

Pages from-to (Number of pages)

Pages 185-189 (5 pages)

Journal (Volume, Issue Number)

Peptides (Volume 25, Issue 2)

Publication milestones

  • Published - 02/2004

Publication status

Published - 02/2004

ISSN

0196-9781

Publication IDs

  • Scopus: 1942451963
  • PubMed: 15062999

Publication metrics

Metrics

Scopus
citations
SciVal
FWCI
0.91
SciVal
Author count
4
SciVal
citations
14
SciVal
Paper percentile
64
Fractional count
1
Fractional count
0.25
Fractional count
3
Fractional count
0.75
Fractional count
1
Fractional count
1

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Citation count
15
Captures
23

Funding Details

Supported by the National Science Foundation (IBN-0314377). We thank C.H. Schein, W. Braun, and S.D. Painter for helpful discussions, and the UTMB Protein Chemistry Lab and Mass Spectrometry Facility for performing amino acid compositional analyses and MALDI-MS.