Preparation and Representation of Recombinant Mn-Ferritin Flower-Like Spherical Aggregates from Marine Invertebrates

Abstract

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.

Atomic resolution studies detect new biologic evidences on the Turin Shroud

“…EDXS experiments performed on individual large particles, as the one shown in Fig 3, reveal the presence of Ca, O, C, N, Fe, S, K, Cl (see S3 Fig), which are compatible with ferritin-based proteins [31,32]. Nevertheless, the high contamination rate [19] due to the century exposure of the TS to the environment does not permit to have enough statistics to discriminate and quantify the EDXS signal coming from the small dark particles with respect to those coming from the big particles embedding them.…”

Adaptation and evolution of the sea anemone Alvinactis sp. to deep‐sea hydrothermal vents: A comparison using transcriptomes

“…The detoxification system can be highly efficient because no free sulfide can be found in cells (Vetter et al, 1987 ). Heavy metals can be sequestrated by metallothionein, phytochelatin, or ferritin to avoid their toxicity (Chen et al, 2015 ; Wong et al, 2015 ; Zapata et al, 2009 ). The in vivo effect of metals (like reactive oxygen species [ROS]) causes these organisms to respond by the function of detoxification of superoxide dismutase (SOD), catalase, or glutathione peroxidase (Genard et al, 2013 ; Marie et al, 2006 ).…”