Visualization 1: Digital polarization holography advancing geometrical phase optics

Polarized image of an “invisible” cat revealed by inserting and removing a polarizer. Originally published in Optics Express on 08 August 2016 (oe-24-16-18297

The photograph of the whole shell and the SEM images of cross-section of <i>M</i>. <i>galloprovincialis</i> shell.

<p>A: the exterior side of <i>M</i>. <i>galloprovincialis</i> shell; B: the interior side of <i>M</i>. <i>galloprovincialis</i> shell, the white line represents the cutting plane; “AMS”, “AMS-A”, and “AMS-P” represent the area of adductor muscle scar (AMS), anterior side of AMS, and posterior side of AMS, respectively. C: the cross-sectional SEM image of AMS-A, showed nacre (N) on the top layer and fibrous prism (FP) at the bottom of this area; D: enlarged image of nacre from AMS-A; E: the cross-sectional SEM image of central AMS, showed myostracum (M) at the top, nacre (N) at the middle, and fibrous prism (FP) at the bottom of this area; F: the cross-sectional SEM image of AMS-P, showed fibrous prism at this area.</p

Table_3_Physiological and transcriptome analysis of Mytilus coruscus in response to Prorocentrum lima and microplastics.docx

Nowadays, diarrheic shellfish toxicity (DSP) toxin and microplastics (MPs) are commonly found in coastal waters worldwide. Due to their widespread use, their persistence and toxicity, they may induce adverse effects on Mytilus coruscus. However, the underlying toxic mechanisms of DSP and MPs on M. coruscus remain unclear. This study explored the physiological index and transcriptome change of the digestive gland of adult M. coruscus exposed for 3 days to polystyrene (PS) MPs (0.2 mg/L, 90-100 μm) and Prorocentrum lima alone or in combination. The results showed that the CAT activity and MDA content significantly increased, respiration rate and feeding rate significantly decreased. The combination of MPs and P. lima caused more structural damage to the rough surface endoplasmic reticulum and mitochondria in the digestive glands of M. coruscus. The transcriptome analysis showed that 485 and 220 genes were up- and down-regulated, respectively, after exposure to P. lima; 1,989 up-regulated DEGs and 1,098 down-regulated DEGs were identified after exposure to MP treatment, and 1,004 up-regulated DEGs and 664 down-regulated DEGs were identified after exposure to the combination of P. lima and MPs. The DEGs were mainly enriched in the lysosome, mRNA surveillance pathway, carbon metabolism, the mTOR signaling pathway, the complement and coagulation cascades, and the TNF signaling pathway. The MP, P. lima exposure mainly induced the expression of RNA-binding protein musashi, serine/arginine repetitive matrix protein 1, low affinity immunoglobulin epsilon Fc receptor, toll-like receptor 2, caspase 7, calmodulin, E3 ubiquitin-protein ligase, serine/threonine-protein kinase PRP4, glutathione S-transferase, and heat shock 70 kDa protein. MPs and P. lima poison mainly influence the expression of RNA transport, immune related gene, apoptosis, signal related gene, and antioxidant gene change. The combination of MPs and P. lima has a synergistic toxic effect. This study provides a new insights into its physiological and molecular responses of M. coruscus to MPs and P. lima toxic exposure.</p

The photograph of the whole shell and the SEM images of cross-section of <i>M</i>. <i>galloprovincialis</i> shell.

<p>A: the exterior side of <i>M</i>. <i>galloprovincialis</i> shell; B: the interior side of <i>M</i>. <i>galloprovincialis</i> shell, the white line represents the cutting plane; “AMS”, “AMS-A”, and “AMS-P” represent the area of adductor muscle scar (AMS), anterior side of AMS, and posterior side of AMS, respectively. C: the cross-sectional SEM image of AMS-A, showed nacre (N) on the top layer and fibrous prism (FP) at the bottom of this area; D: enlarged image of nacre from AMS-A; E: the cross-sectional SEM image of central AMS, showed myostracum (M) at the top, nacre (N) at the middle, and fibrous prism (FP) at the bottom of this area; F: the cross-sectional SEM image of AMS-P, showed fibrous prism at this area.</p

A representative MS/MS spectrum for the two peptides matching with EST gi|58308563, an AGL-rich protein of <i>M</i>. <i>galloprovincialis</i>.

<p>A: protein sequence derived from EST gi|58308563. The matched peptides from MS/MS spectra were underlined; B: MS/MS spectrum of the peptide “-AAAAAGASAAAGGSGGTLR-” with <i>m/z</i> of 1486.90 Da; C: MS/MS spectrum of the peptide “-LISRIIAR-” with <i>m/z</i> of 940.71 Da.</p

HPLC elution profiles and SDS-PAGE analysis of shell matrices from nacre, myostracum, and fibrous prism, respectively.

<p>A: HPLC elution profiles of acid-soluble matrices from nacre (N-A), myostracum (M-A), and fibrous prism (FP-A). The bold line represents the concentration of acetonitrile. B: HPLC elution profiles of urea-soluble matrices from nacre (N-U), myostracum (M-U), and fibrous prism (FP-U). The bold line represents the concentration of acetonitrile. C: PAGE comparison of acid-soluble (ASM), urea-soluble (USM), and insoluble matrices (IM) of nacre (N), myostracum (M), and fibrous prism (FP).</p

Domain organization and sequence alignment of representative novel proteins of <i>M</i>. <i>galloprovincialis</i> shell with their homologous from other shell.

<p>A: protease inhibitor-like protein of <i>M</i>. <i>galloprovincialis</i> (gi|238643545) and NSPI2 of <i>P</i>. <i>maxima</i> (sp|P86964.1); B: EGF-domain containing protein of <i>M</i>. <i>galloprovincialis</i> (gi|145890922) and Gigasin-2 of <i>C</i>. <i>gigas</i> (sp|P86785.1); C: alveoline-like protein of <i>M</i>. <i>galloprovincialis</i> (gi|212821271) and alveoline-like protein of <i>P</i>. <i>margaritifera</i> (sp|H2A0K6.1); D: chitinase-like proteins of <i>M</i>. <i>galloprovincialis</i> (gi|58308904 and gi|58307961) and acidic mammalian chitinase isoform X4 of <i>Saimiri boliviensis</i> (gi|72558135)<i>;</i> E: EP proteins of <i>M</i>. <i>galloprovincialis</i> (gi|145893971 and gi|34304719) and EP protein of <i>M</i>. <i>edulis</i> (gb|AAQ63463.1); F: Cathepsin-like protein of <i>M</i>. <i>galloprovincialis</i> (gi|238641522) and Cathepsin of <i>C</i>. <i>gigas</i> (gi|405966499). Signal peptides are underlined; “*”represents identical amino acids; “:” and “.” represent similar amino acids; “-”represents the gaps inserted in the sequence.</p

Layer-by-Layer Proteomic Analysis of <i>Mytilus galloprovincialis</i> Shell

<div><p>Bivalve shell is a biomineralized tissue with various layers/microstructures and excellent mechanical properties. Shell matrix proteins (SMPs) pervade and envelop the mineral crystals and play essential roles in biomineralization. Despite that <i>Mytilus</i> is an economically important bivalve, only few proteomic studies have been performed for the shell, and current knowledge of the SMP set responsible for different shell layers of <i>Mytilus</i> remains largely patchy. In this study, we observed that <i>Mytilus galloprovincialis</i> shell contained three layers, including nacre, fibrous prism, and myostracum that is involved in shell-muscle attachment. A parallel proteomic analysis was performed for these three layers. By combining LC-MS/MS analysis with <i>Mytilus</i> EST database interrogations, a whole set of 113 proteins was identified, and the distribution of these proteins in different shell layers followed a mosaic pattern. For each layer, about a half of identified proteins are unique and the others are shared by two or all of three layers. This is the first description of the protein set exclusive to nacre, myostracum, and fibrous prism in <i>Mytilus</i> shell. Moreover, most of identified proteins in the present study are novel SMPs, which greatly extended biomineralization-related protein data of <i>Mytilus</i>. These results are useful, on one hand, for understanding the roles of SMPs in the deposition of different shell layers. On the other hand, the identified protein set of myostracum provides candidates for further exploring the mechanism of adductor muscle-shell attachment.</p></div

The distribution pattern of identified proteins in three shell layers of <i>M</i>. <i>galloprovincialis</i>.

<p>The proteomic data comprises identifications occurring in both soluble fraction and insoluble fraction from all three layers. N, M, and FP represent nacre, myostracum, and fibrous prism, respectively.</p

Visualization 3: Digital polarization holography advancing geometrical phase optics

Sample with the invisible photo of George Washington (the background is The New York Times homepage) Originally published in Optics Express on 08 August 2016 (oe-24-16-18297