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Evolutionary Proteomics Reveals Distinct Patterns of Complexity and Divergence between Lepidopteran Sperm Morphs
Emma Whittington1, Timothy L Karr2, Andrew J Mongue3
1Center for Reproductive Evolution, Department of Biology, Syracuse University.
Genome Biology and Evolution
|July 4, 2019
Summary
Sperm diversity includes non-fertilizing parasperm. Comparing butterfly and moth sperm reveals shared proteins in both types, but parasperm have fewer proteins and evolve faster, possibly due to sexual selection.
Area of Science:
- Evolutionary biology
- Reproductive biology
- Proteomics
Background:
- Spermatozoa exhibit remarkable diversity, including sperm heteromorphism, where males produce multiple sperm morphs.
- Sperm heteromorphism involves fertilizing sperm and non-fertilizing parasperm, whose functions are poorly understood.
- In Lepidoptera, males produce fertilizing eupyrene sperm and non-fertilizing apyrene sperm lacking DNA.
Purpose of the Study:
- To conduct a comparative proteomic analysis of eupyrene and apyrene sperm in two lepidopteran species.
- To identify shared and unique proteins between fertilizing and non-fertilizing sperm morphs.
- To investigate the evolutionary dynamics of sperm proteomes in relation to sperm heteromorphism.
Main Methods:
- Comparative proteomic analysis of eupyrene and apyrene sperm from Danaus plexippus (monarch butterfly) and Manduca sexta (Carolina sphinx moth).
- Mass spectrometry-based identification and quantification of sperm proteins.
- Gene ontology (GO) analysis to determine protein functions and cellular localizations.
Main Results:
- Approximately 700 sperm proteins were identified in each species, with about half shared between eupyrene and apyrene sperm.
- Apyrene sperm exhibited a less complex proteome compared to eupyrene sperm.
- Shared proteins were associated with canonical sperm structures and metabolism, while morph-specific proteins suggested roles in female neurobiology and reflected structural differences.
Conclusions:
- Proteins shared between sperm morphs are highly conserved, whereas morph-specific proteins, particularly in apyrene sperm, evolve rapidly.
- The rapid divergence of apyrene sperm proteomes may result from relaxed selection pressures related to fertilization.
- Parasperm's evolutionary lability suggests adaptive responses to sexual selection dynamics.
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