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

Pasquevich, María Yanina; Dreon, Marcos Sebastián; Heras, Horacio

doi:10.1016/j.cbpb.2013.11.008

Cited by 30 publications

(83 citation statements)

References 53 publications

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“…The perivitelline fluid of P. maculata is also similar, with two major perivitellins, PmPV1 and PmPV2 (Pasquevich et al, 2014). PcOvo, PsSC and PmPV1 act as carriers of antioxidant carotenoid cofactors, notably astaxanthin, which are extremely labile in solution but are not degraded when bound to the perivitellins Pasquevich et al, 2014).…”

Section: Perivitellin Structure and Synthesismentioning

confidence: 97%

“…In spite of the central role of perivitellins in reproduction and development, there is little information on their structural features in invertebrates. Studies in molluscs are limited essentially to the perivitellins of Pomacea, mostly in P. canaliculata but also P. scalaris and P. maculata (Ituarte et al, 2012;Pasquevich et al, 2014).…”

Section: Egg Proteins: Structure and Role In Defensementioning

confidence: 99%

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Insights from an Integrated View of the Biology of Apple Snails (Caenogastropoda: Ampullariidae)

et al. 2015

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Section: Perivitellin Structure and Synthesismentioning

confidence: 97%

Section: Egg Proteins: Structure and Role In Defensementioning

confidence: 99%

Insights from an Integrated View of the Biology of Apple Snails (Caenogastropoda: Ampullariidae)

et al. 2015

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“…5,6 These perivitellins serve as stores of nutrients that fuel the embryonic development and are involved in embryo protection in some Pomacea. 6,7 Although previous proteomic studies named the major perivitellin protein PV1 as PcOvo for P. canaliculata, 8 PmPV1 for P. maculata 9 and PsSC for P. scalaris, 10 to avoid confusion of the major protein in PVF, we used "PV1" throughout this study. Among two major perivitelline groups, PV1 is an oligomer composed of several subunits and plays several critical roles: photoprotection, antioxidant, and nutrient provision in P. canaliculata and P. maculate, 4,8,11,12 and immune response in P. scalaris.…”

mentioning

confidence: 99%

Egg perivitelline fluid proteome of a freshwater snail: Insight into the transition from aquatic to terrestrial egg deposition

Zhang

et al. 2020

Rapid Comm Mass Spectrometry

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Rationale Proteins from the egg perivitelline fluid (PVF) are assumed to play critical roles in embryonic development, but for many groups of animals their identities remain unknown. Identifying egg PVF proteins is a critical step towards understanding their functions including their roles in evolutionary transition in habitats. Methods We applied proteomic and transcriptomic analysis to investigate the PVF proteome of the eggs of Pomacea diffusa, an aerial ovipositing freshwater snail in the family Ampullariidae. The PVF proteins were separated with the sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) method, and proteomic analysis was conducted using an LTQ Velos ion trap mass spectrometer coupled with liquid chromatography. Comparison of PVF proteomes and evolution analyses was performed between P. diffusa and other ampullariids. Results In total, 32 egg PVF proteins were identified from P. diffusa. They were categorized as PV1‐like subunits, immune‐responsive proteins, protein degradation, signaling and binding, transcription and translation, metabolism, oxidation–reduction and proteins with unknown function. Interestingly, the proteome includes a calcium‐binding protein important in forming the hard eggshell that enabled the terrestrial transition. However, it does not include PV2, a neurotoxic protein that was assumed to be present in all Pomacea species. Conclusions The PVF proteome data from P. diffusa can help us better understand the roles that reproductive proteins played during the transition from underwater to terrestrial egg deposition. Moreover, they could be useful in comparative studies of the terrestrialization in several groups of animals that occurred independently during their evolution.

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“…PmPV2 was obtained following the method described for PcPV2 (Pasquevich, Dreon, & Heras, 2014). Briefly, PVF was ultracentrifuged in a NaBr (density = 1.28 g/ml) gradient at 207,000 xg for 22 h at 4 °C.…”

Section: Methodsmentioning

confidence: 99%

Exaptation of two ancient immune proteins into a new dimeric pore-forming toxin in snails

Giglio

Ituarte

Milesi

et al. 2019

Preprint

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The Membrane Attack Complex-Perforin (MACPF) family is ubiquitously found in all kingdoms. They have diverse cellular roles but MACPF but pore-forming toxic function are very rare in animals. Here we present the structure of PmPV2, a MACPF toxin from the poisonous apple snail eggs, that can affect the digestive and nervous systems of potential predators. We report the three-dimensional structure of PmPV2, at 15 Å resolution determined by negative stain electron microscopy (NS-EM) and its solution structure by small angle X-ray scattering (SAXS). We found that PV2s differ from nearly all MACPFs in two respects: it is a dimer in solution and protomers combine two immune proteins into an AB toxin. MACPF chain is linked by a single disulfide bond to a tachylectin chain, and two heterodimers are arranged head-to-tail by non-covalent forces in the native protein. MACPF domain is fused with a putative new Ct-accessory domain exclusive to invertebrates. Tachylectin is a six-bladed β-propeller, similar to animal tectonins. We experimentally validated the predicted functions of both subunits and demonstrated for the first time that PV2s are true pore-forming toxins. The tachylectin ..B.. delivery subunit would bind to target membranes, and then its MACPF ..A.. toxic subunit disrupt lipid bilayers forming large pores altering the plasma membrane conductance. These results indicate that PV2s toxicity evolved by linking two immune proteins where their combined preexisting functions give rise to a new toxic entity with a novel role in defense against predation. This structure is an unparalleled example of protein exaptation.

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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

Cited by 30 publications

References 53 publications

Insights from an Integrated View of the Biology of Apple Snails (Caenogastropoda: Ampullariidae)

Insights from an Integrated View of the Biology of Apple Snails (Caenogastropoda: Ampullariidae)

Egg perivitelline fluid proteome of a freshwater snail: Insight into the transition from aquatic to terrestrial egg deposition

Exaptation of two ancient immune proteins into a new dimeric pore-forming toxin in snails

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