Ovorubin

Ovorubin (PcOvo or PcPV1) is the most abundant perivitellin (>60 % total protein) of the perivitelline fluid from Pomacea canaliculata snail eggs. This glyco-lipo-caroteno protein complex is a approx. 300 kDa multimer of a combination of multiple copies of six different ~30 kDa subunits.[1]

Ovorubin
Identifiers
OrganismPomacea canaliculata (golden apple snail)
SymbolPcOvo
Alt. symbolsPcPV1
PDBJ7HZ90; J7I5Z5
UniProtJ7I2T6

Together with the other perivitellins from Pomacea canaliculata eggs, ovorubin serves a nutrient source for developing embryos, notably to the intermediate and late stages.[2] Moreover, after hatching, the protein is still detected in the lumen of the digestive gland ready to be endocytosed, therefore, acting as a nutrient source for the newly hatched snail.[2]

Ovorubin contains carbohydrates and carotenoid pigments as main prosthetic groups, [3] which are related to many physiological roles on Pomacea aerial egg-laying strategy. Given that carbohydrates tend to retain water, the high glycosylation of ovorubin (~17 % w/w) was proposed as an embryo defense against water loss.[3] The carotenoid pigments stabilized by ovorubin also provide the eggs of antioxidant and photoprotective capacities, crucial roles to cope with the harsh conditions of the aerial environment.[2][4][5][6][7] The presence of carotenoid pigments is also responsible for the brightly reddish coloration of Ovorubin, and therefore snail eggs, which was related to a warning coloration (aposematism) advertising predators about the presence of deterrents.[8][9] In fact, field evidence of egg unpalatability is provided by the fact that most animals foraging in habitats where the apple snails live ignore these eggs.[10]

Like most other studied perivitellins from Pomacea snails, ovorubin 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.[11][12]

References

  1. Garin CF, Heras H, Pollero RJ (December 1996). "Lipoproteins of the egg perivitelline fluid of Pomacea canaliculata snails (Mollusca: Gastropoda)". The Journal of Experimental Zoology. 276 (5): 307–14. doi:10.1002/(SICI)1097-010X(19961201)276:5<307::AID-JEZ1>3.0.CO;2-S. PMID 8972583.
  2. Heras H, Garin CF, Pollero RJ (1998). "Biochemical composition and energy sources during embryo development and in early juveniles of the snail Pomacea canaliculata (Mollusca: Gastropoda)". Journal of Experimental Zoology. 280 (6): 375–383. doi:10.1002/(SICI)1097-010X(19980415)280:63.0.CO;2-K (inactive 2021-01-31). ISSN 1097-010X.CS1 maint: DOI inactive as of January 2021 (link)
  3. Dreon MS, Heras H, Pollero RJ (July 2004). "Characterization of the major egg glycolipoproteins from the perivitellin fluid of the apple snail Pomacea canaliculata". Molecular Reproduction and Development. 68 (3): 359–64. doi:10.1002/mrd.20078. PMID 15112330. S2CID 22032382.
  4. Cheesman DF (December 1958). "Ovorubin, a chromoprotein from the eggs of the gastropod mollusc Pomacea canaliculata". Proceedings of the Royal Society of London. Series B, Biological Sciences. 149 (937): 571–87. doi:10.1098/rspb.1958.0093. PMID 13623805. S2CID 44905224.
  5. Dreon MS, Heras H, Pollero RJ (January 2003). "Metabolism of ovorubin, the major egg lipoprotein from the apple snail". Molecular and Cellular Biochemistry. 243 (1–2): 9–14. doi:10.1023/A:1021616610241. PMID 12619883. S2CID 6345962.
  6. Dreon MS, Schinella G, Heras H, Pollero RJ (February 2004). "Antioxidant defense system in the apple snail eggs, the role of ovorubin". Archives of Biochemistry and Biophysics. 422 (1): 1–8. doi:10.1016/j.abb.2003.11.018. PMID 14725852.
  7. Dreon MS, Ceolín M, Heras H (April 2007). "Astaxanthin binding and structural stability of the apple snail carotenoprotein ovorubin". Archives of Biochemistry and Biophysics. 460 (1): 107–12. doi:10.1016/j.abb.2006.12.033. PMID 17324373.
  8. Heras H, Dreon MS, Ituarte S, Pollero RJ (2007-07-01). "Egg carotenoproteins in neotropical Ampullariidae (Gastropoda: Arquitaenioglossa)". Comparative Biochemistry and Physiology. Toxicology & Pharmacology. 146 (1–2): 158–67. doi:10.1016/j.cbpc.2006.10.013. PMID 17320485.
  9. Hayes KA, Burks RL, Castro-Vazquez A, Darby PC, Heras H, Martín PR, et al. (2015). "Insights from an Integrated View of the Biology of Apple Snails (Caenogastropoda: Ampullariidae)". Malacologia. 58 (1–2): 245–302. doi:10.4002/040.058.0209. ISSN 0076-2997. S2CID 85707576.
  10. Snyder NF, Snyder HA (1971-01-01). "Defenses of the Florida Apple Snail Pomacea Paludosa". Behaviour. 40 (3–4): 175–214. doi:10.1163/156853971X00384. ISSN 0005-7959.
  11. Dreon MS, Ituarte S, Ceolín M, Heras H (September 2008). "Global shape and pH stability of ovorubin, an oligomeric protein from the eggs of Pomacea canaliculata". The FEBS Journal. 275 (18): 4522–30. doi:10.1111/j.1742-4658.2008.06595.x. PMID 18673387. S2CID 22611520.
  12. Dreon MS, Ituarte S, Heras H (December 2010). "The role of the proteinase inhibitor ovorubin in apple snail eggs resembles plant embryo defense against predation". PLOS ONE. 5 (12): e15059. doi:10.1371/journal.pone.0015059. PMC 2997075. PMID 21151935.
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