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PLoS One
2015 Apr 16;104:e0119427. doi: 10.1371/journal.pone.0119427.
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Preparation and representation of recombinant Mn-ferritin flower-like spherical aggregates from marine invertebrates.
Chen L
,
Zhou J
,
Zhang Y
,
Chu S
,
He W
,
Li Y
,
Su X
.
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Ferritin has important functions in the transition and storage of toxic metal ions, but its regulation and function in many invertebrate species are still largely unknown. In our previous work, the cDNA sequence of Sinonovacula constricta, Apostichopus japonicas and Acaudina leucoprocta were constructed and efficiently expressed in E. Coli BL21 under IPTG induction. In this follow-up study, the recombinant ferritins were exposed to heavy metal manganese. The manganese concentration levels in three recombinant ferritins were greater than horse spleen ferritin (HSF). Compared with HSF, the amount of manganese enrichment in the three recombinant ferritins was 1.75-fold, 3.25-fold and 2.42-fold increases in ScFER, AjFER, and AlFER, respectively. After phosphate stimulation, the concentration of manganese increased and was higher than the ordinary dialysis control groups. The ScFER was four times its baseline value. The AjFER and AlFER were 1.4- and 8-fold higher, respectively. The AlFER sample stimulated by phosphate was 22-fold that of HSF. The morphologies of the resulting Mn-Ferritin from different marine invertebrates were characterized with scanning electron microscopy. Surface morphologies were lamella flower-like and are consistent with changes in surface morphologies of the standard Mn-HSF. Invertebrate recombinant ferritin and HSF both can uptake manganese. We found that the structure of A. leucoproctarecombinant Mn-Ferritin aggregate changed over time. The surface formed lamella flower-like aggregate, but gradually merged to create a relatively uniform plate-like phase of aggregate spherically and fused without clear boundaries.
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25879665
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Fig 1. Expression and purification of pET-FER recombinant ScFER, AjFER, AlFER protein in E. coli strain BL21.Lanes 8, 13, and 17: middle molecular marker; lanes 1 and 2: negative control; lanes 3–7: ScFER induce expression at 1, 2, 3, 4, and 5 h; lanes 9 and 10: AjFER expression at 4 and 5 h; lanes 11 and 12: AlFER induce expression at 4 and 5h; lanes 14–16: AlFER, AjFER, and ScFER purified expression products.
Fig 2. EDS results of different ferritin treatment groups.Peaks of manganese for each ferritin can be clearly detected in the same position (0.56 and 5.91 keV) in the manganese treatment groups (a, c, e, g). No manganese peak was detected in the negative controls (b, d, f, h). a: ScFER with manganese treatment; b: the negative control of ScFER without manganese treatment; c: AjFER with manganese treatment; d: the negative control of AjFER without manganese treatment; e: AlFER with manganese treatment; f: the negative control of AlFER without manganese treatment; g: HSF with manganese treatment; h: the negative control of HSF without manganese treatment.
Fig 4. SEM of different treatment groups of ferritin.a: ScFER aggregates morphology; b: Mn-ScFER aggregates; c: AjFER aggregates morphology; d: Mn-AjFER aggregates; e: AlFER aggregates morphology; f: Mn-AlFER aggregates; g: HSF aggregates morphology; and h: Mn-HSF aggregates.
Fig 5. The surface characteristics of Mn-AlFER aggregates.a: surface observed after 1 day; 5: surface observed after 2 days; c and d: surface observed after 5 days; e: surface observed after 6 days; f and g: surface observed after 7 days; h and i: surface observed after 9 days; j and k: surface observed after 12 days; l: surface observed after 15 days.
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