Dataset for the proteomic and transcriptomic analyses of perivitelline fluid proteins in Pomacea snail eggs

Mu, Huawei; Sun, Jin; Heras, Horacio; Chu, Ka Hou; Qiu, Jian

doi:10.1016/j.dib.2017.09.020

Cited by 7 publications

(5 citation statements)

References 9 publications

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“…N-terminal sequences of PmPV1 subunits 25 were used to pick up the corresponding protein and DNA sequences. The presence of PmPV1 subunits were further identified by mass spectrometric data obtained by proteomic analysis of P. maculata perivitelline fluid 51 . Other potential subunits were identified by homology searching P. maculata albumen gland transcriptome.…”

Section: Methodsmentioning

confidence: 99%

Convergent evolution of plant and animal embryo defences by hyperstable non-digestible storage proteins

Pasquevich

Dreon

Qiu

et al. 2017

Sci Rep

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Plants have evolved sophisticated embryo defences by kinetically-stable non-digestible storage proteins that lower the nutritional value of seeds, a strategy that have not been reported in animals. To further understand antinutritive defences in animals, we analysed PmPV1, massively accumulated in the eggs of the gastropod Pomacea maculata, focusing on how its structure and structural stability features affected its capacity to withstand passage through predator guts. The native protein withstands >50 min boiling and resists the denaturing detergent sodium dodecyl sulphate (SDS), indicating an unusually high structural stability (i.e., kinetic stability). PmPV1 is highly resistant to in vitro proteinase digestion and displays structural stability between pH 2.0–12.0 and 25–85 °C. Furthermore, PmPV1 withstands in vitro and mice digestion and is recovered unchanged in faeces, supporting an antinutritive defensive function. Subunit sequence similarities suggest a common origin and tolerance to mutations. This is the first known animal genus that, like plant seeds, lowers the nutritional value of eggs by kinetically-stable non-digestible storage proteins that survive the gut of predators unaffected. The selective pressure of the harsh gastrointestinal environment would have favoured their appearance, extending by convergent evolution the presence of plant-like hyperstable antinutritive proteins to unattended reproductive stages in animals.

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Section: Methodsmentioning

confidence: 99%

Convergent evolution of plant and animal embryo defences by hyperstable non-digestible storage proteins

Pasquevich

Dreon

Qiu

et al. 2017

Sci Rep

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“…Protein sequences translated from the combined transcriptomes of albumen gland and other tissues can be found in a Data in Brief paper (Mu et al, submitted) [62].…”

Section: Abbreviationsmentioning

confidence: 99%

An integrated proteomic and transcriptomic analysis of perivitelline fluid proteins in a freshwater gastropod laying aerial eggs

Sun

Heras

et al. 2017

Journal of Proteomics

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“…However, another role regulating endogenous proteolytic activities cannot be discarded. These inhibitors are conserved in other members of the genus like the sympatric species P. maculata (Mu et al 2017a).…”

Section: R a F Tmentioning

confidence: 99%

Non-digestible proteins and protease inhibitors: implications for defense of the colored eggs of the freshwater apple snailPomacea canaliculata

et al. 2019

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Apple snails (Pomacea Perry, 1810) are successful invaders that cause ecological perturbations, economic losses, and medical issues. A peculiar trait of this snail is a high biological potential, related to the absence of predators of their eggs. Eggs show protease inhibitor (PI) activity, originally ascribed to PcOvo perivitellin in the apple snail Pomacea canaliculata (Lamarck, 1822) but absent in PmPV1, the orthologoue of PcOvo, in eggs of the apple snail Pomacea maculata Perry, 1810. As egg fluid diminishes rat growth rate, an antidigestive effect, similar to plant defenses against herbivory, was hypothesized. However, PI activity has not been characterized in apple snail eggs. Here we identify and partially characterize P. canaliculata egg PI and improve our knowledge of the quaternary structure and evolution of PcOvo. Through N-terminal, transcriptomic or proteomic sequencing, and biochemical validation, we identified a Kunitz-type and a Kazal-type inhibitor that, though at low concentration in the egg, exhibit strong PI activity against trypsin, chymotrypsin, elastase, and subtilisin. Additionally, we report three new subunits for the non-digestible storage protein PcOvo. They are likely products of ancient gene duplication, as their sequences exhibit moderate similarity (30%). To our knowledge, this is the first report of Kazal-type inhibition among invertebrate eggs. Inhibiting varied proteases, PI seems an efficient adaptive trait that limits predator’s capacity to digest egg nutrients.

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Dataset for the proteomic and transcriptomic analyses of perivitelline fluid proteins in Pomacea snail eggs

Cited by 7 publications

References 9 publications

Convergent evolution of plant and animal embryo defences by hyperstable non-digestible storage proteins

Convergent evolution of plant and animal embryo defences by hyperstable non-digestible storage proteins

An integrated proteomic and transcriptomic analysis of perivitelline fluid proteins in a freshwater gastropod laying aerial eggs

Non-digestible proteins and protease inhibitors: implications for defense of the colored eggs of the freshwater apple snailPomacea canaliculata

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