Identification of sex, age and species-specific proteins on the surface of the harpacticoid copepod Tigriopus japonicus |
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Authors: | J H Ting L S Kelly T W Snell |
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Institution: | (1) School of Biology, Georgia Institute of Technology, Atlanta, GA, 30332-0230, USA Fax: 001 (0)404 894-0519 e-mail: gt4017a@prism.gatech.edu, GE |
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Abstract: | Behavioral experiments have shown that male copepods of the species Tigriopus japonicus (Nori) can distinguish species, sex, and developmental stage of potential mates using contact chemoreception. Lectin-binding
patterns on the body surface of females have indicated that surface-bound glycoproteins may be important signals in mate choice.
In the present study, the proteolytic enzyme trypsin was used to cleave surface proteins from females, reducing their attractiveness
to males. The protein fragments released were used to make monoclonal antibodies. Three levels of screening were used to identify
monoclonal antibodies that recognized proteins involved in mate recognition. One monoclonal antibody bound to the terminal
urosome and lateral prosome of CV females, and its binding significantly decreased female attractiveness to males. Western
blotting showed that this antibody bound the trypsin-cleaved fragment and proteins of homogenized CV females and virgin adult
females, but did not bind proteins of homogenized males, CIII females, or females of T. californicus or T. fulvus. This antibody recognized proteins on the surface of females that may enable males to discriminate conspecifics, sex, and
age. It is likely that this molecule has a central role in the evolution of reproductive isolation in this group.
Received: 22 July 1999 / Accepted: 21 March 2000 |
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