Let It Beat: How Lifestyle and Psychosocial Factors Affect the Risk of Sudden Cardiac Death—A 10-Year Follow-Up Study

(1) Background: The aim of this study was to evaluate the lifestyle and occurrence of psychosocial factors in patients with a high risk of sudden cardiac death (SCD) and to explore their effect on the occurrence of the adequate therapy of an Implantable Cardioverter Defibrillator (ICD). (2) Methods: In this retro-prospective single-centre study, a group of patients aged 18–65 years old, who underwent the first ICD implantation for primary (PP) or secondary (SP) prevention between 2010–2014, was studied. The control group consisted of pair-matched (age ± 5 years, gender) respondents without a high risk of SCD. Information was obtained using a self-reported questionnaire and hospital electronic health records. The adequacy of ICD therapy was evaluated regularly until 31 January 2020. Multivariate logistic regression models were employed to assess the risk of SCD. (3) Results: A family history of SCD, coronary artery disease, diabetes mellitus and depression significantly aggravated the odds of being at a high risk of SCD. The occurrence of an appropriate ICD therapy was significantly associated with being in the SP group, BMI, education level and TV/PC screen time. (4) Conclusions: Lifestyle and psychosocial factors have been confirmed to affect the risk of SCD. Early identification and treatment of coronary artery disease and its risk factors remain the cornerstones of preventive effort. Further research is needed to evaluate the complex nature of psychosocial determinants of cardiac health

Preliminary Study of Sars-Cov-2 Occurrence in Wastewater in the Czech Republic

The virus SARS-CoV-2, which has caused the recent COVID-19 pandemic, may be present in the stools of COVID-19 patients. Therefore, we aimed to detect SARS-CoV-2 in wastewater for surveillance of SARS-CoV-2 in the population. Samples of untreated wastewater were collected from 33 wastewater treatment plants (WWTPs) of different sizes within the Czech Republic. SARS-CoV-2 RNA was concentrated from wastewater and viral RNA was determined using real-time reverse transcription polymerase chain reaction (RT-qPCR). SARS-CoV-2 RNA was detected in 11.6% of samples and more than 27.3% of WWTPs; in some of them, SARS-CoV-2 was detected repeatedly. Our preliminary results indicate that an epidemiology approach that focuses on the determination of SARS-CoV-2 in wastewater could be suitable for SARS-CoV-2 surveillance in the population

Raman Spectroscopy Adds Complementary Detail to the High-Resolution X-Ray Crystal Structure of Photosynthetic PsbP from Spinacia oleracea

PLoS ONE. Volume 7, Issue 10, 5 October 2012, Article number e46694.Raman microscopy permits structural analysis of protein crystals in situ in hanging drops, allowing for comparison with Raman measurements in solution. Nevertheless, the two methods sometimes reveal subtle differences in structure that are often ascribed to the water layer surrounding the protein. The novel method of drop-coating deposition Raman spectropscopy (DCDR) exploits an intermediate phase that, although nominally "dry," has been shown to preserve protein structural features present in solution. The potential of this new approach to bridge the structural gap between proteins in solution and in crystals is explored here with extrinsic protein PsbP of photosystem II from Spinacia oleracea. In the high-resolution (1.98 Å) x-ray crystal structure of PsbP reported here, several segments of the protein chain are present but unresolved. Analysis of the three kinds of Raman spectra of PsbP suggests that most of the subtle differences can indeed be attributed to the water envelope, which is shown here to have a similar Raman intensity in glassy and crystal states. Using molecular dynamics simulations cross-validated by Raman solution data, two unresolved segments of the PsbP crystal structure were modeled as loops, and the amino terminus was inferred to contain an additional beta segment. The complete PsbP structure was compared with that of the PsbP-like protein CyanoP, which plays a more peripheral role in photosystem II function. The comparison suggests possible interaction surfaces of PsbP with higher-plant photosystem II. This work provides the first complete structural picture of this key protein, and it represents the first systematic comparison of Raman data from solution, glassy, and crystalline states of a protein. © 2012 Kopecky Jr

Raman Spectroscopy Adds Complementary Detail to the High-Resolution X-Ray Crystal Structure of Photosynthetic PsbP from <em>Spinacia oleracea</em>

<div><p>Raman microscopy permits structural analysis of protein crystals <em>in situ</em> in hanging drops, allowing for comparison with Raman measurements in solution. Nevertheless, the two methods sometimes reveal subtle differences in structure that are often ascribed to the water layer surrounding the protein. The novel method of drop-coating deposition Raman spectropscopy (DCDR) exploits an intermediate phase that, although nominally “dry,” has been shown to preserve protein structural features present in solution. The potential of this new approach to bridge the structural gap between proteins in solution and in crystals is explored here with extrinsic protein PsbP of photosystem II from <em>Spinacia oleracea</em>. In the high-resolution (1.98 Å) x-ray crystal structure of PsbP reported here, several segments of the protein chain are present but unresolved. Analysis of the three kinds of Raman spectra of PsbP suggests that most of the subtle differences can indeed be attributed to the water envelope, which is shown here to have a similar Raman intensity in glassy and crystal states. Using molecular dynamics simulations cross-validated by Raman solution data, two unresolved segments of the PsbP crystal structure were modeled as loops, and the amino terminus was inferred to contain an additional beta segment. The complete PsbP structure was compared with that of the PsbP-like protein CyanoP, which plays a more peripheral role in photosystem II function. The comparison suggests possible interaction surfaces of PsbP with higher-plant photosystem II. This work provides the first complete structural picture of this key protein, and it represents the first systematic comparison of Raman data from solution, glassy, and crystalline states of a protein.</p> </div

Secondary structure content of PsbP.

<p>The amide I band was analyzed from Raman spectra acquired on protein samples in solution, glassy state (DCDR), and crystals. Spectra were deconvoluted using the pattern recognition least-squares method (LSA) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0046694#pone.0046694-Overman1" target="_blank">[38]</a> and two reference intensity profile methods (3-RIP and 4-RIP) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0046694#pone.0046694-Tuma1" target="_blank">[39]</a>. Secondary structure content is given as % of residues ± standard deviation calculated from the standard deviations for each respective reference set. All % values are based on the full sequence of 190 residues; the number of residues in each secondary structure type is given in parentheses. The 4-RIP method does not normalize to 100%. The categories α-ordered and α-disordered structures reflect helix mobility. In the model, the 15 native and 4 remaining His-tag residues were assigned as unordered, and added to the 48 residues observed in that conformation.</p

X-ray data collection and refinement statistics.

<p>Values in parentheses are for the highest-resolution shell.</p

Pair alignment of spinach and tobacco PsbP sequences.

<p>Sequences are numbered starting with 1 at the first residue of the mature protein. Asterisks mark identities (149 of 186 residues, 78%). Residues present in the crystalline protein but unresolved in the electron density are bold (spinach) or underlined (tobacco); residues 1 to 9 of the tobacco structure were missing due to partial degradation <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0046694#pone.0046694-Ifuku4" target="_blank">[33]</a>.</p

Raman spectra of spinach PsbP.

<p>Spectra acquired on samples of protein in solution (<b>A</b>), DCDR glassy deposit (<b>B</b>), and crystal (<b>C</b>). Difference spectra are depicted below the figure: DCDR minus solution (<b>B – A</b>); crystal minus solution (<b>C – A</b>); crystal minus DCDR (<b>C – B</b>). The frequencies indicated by vertical dashed lines mark band positions in solution. Band assignments are presented in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0046694#pone-0046694-t002" target="_blank">Table 2</a>.</p