PmPV1
| Pomacea maculata perivitellin-1 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | PmPV1 | ||||||
| Alt. symbols | PV1 | ||||||
| UniProt | A0A1L6BRS1 | ||||||
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Pomacea maculata perivitellin-1 (PmPV1) is the most abundant perivitellin found in the perivitelline fluid from Pomacea maculata snail eggs. This glyco-lipo-caroteno protein is an approx. 294 kDa multimer of a combination of multiple copies of six different ~30 kDa subunits. [1] PmPV1 account >60% of the total proteins found in the Pomacea maculata eggs. [2]
PmPV1 is an orthologous of ovorubin and scalarin, sharing most of the structural features with the former protein and cross-reacting with anti-ovorubin polyclonal antibodies. [1][3] Like ovorubin and scalarin, PmPV1 is highly glycosylated (~13% w/w) and carries carotenoid pigments, indicating that this perivitellin would probably have the antioxidant, photoprotective, aposematic and water retention functions described for its orthologous. [1]
PmPV1 is a kinetically stable protein that, like most other studied perivitellins from Pomacea snails, is highly stable in a wide range of pH values and withstands gastrointestinal digestion, characteristics associated with an antinutritive defense system that deters predation by lowering the nutritional value of the eggs. [3] Remarkably, and in agreement with this antinutritive activity, PmPV1 withstands in vivo digestion, being recovered structurally unaltered from mice feces after trespassing the whole digestive system. [3]
References
- ^ a b c Pasquevich MY, Dreon MS, Heras H (March 2014). "The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 169: 63–71. doi:10.1016/j.cbpb.2013.11.008. PMID 24291422.
- ^ Giglio ML, Ituarte S, Pasquevich MY, Heras H (2016-09-12). "The eggs of the apple snail Pomacea maculata are defended by indigestible polysaccharides and toxic proteins". Canadian Journal of Zoology. 94 (11): 777–785. doi:10.1139/cjz-2016-0049. hdl:1807/74381. ISSN 0008-4301.
- ^ a b c Pasquevich MY, Dreon MS, Qiu JW, Mu H, Heras H (November 2017). "Convergent evolution of plant and animal embryo defences by hyperstable non-digestible storage proteins". Scientific Reports. 7 (1): 15848. Bibcode:2017NatSR...715848P. doi:10.1038/s41598-017-16185-9. PMC 5696525. PMID 29158565.
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