ĐÁNH GIÁ THỰC TRẠNG SỨC KHỎE - DINH DƯỠNG CỦA CÁN BỘ THUỘC DIỆN TỈNH ỦY TỈNH THÁI BÌNH QUẢN LÝ NĂM 2019

Nghiên cứu nhằm đánh giá tình trạng dinh dưỡng của các cán bộ thuộc diện Ban thường vụ Tỉnh ủy tỉnh Thái Bình quản lý. Đối tượng được điều tra bao gồm các cán bộ đương chức và các cán bộ đã nghỉ hưu. Thiết kế nghiên cứu mô tả cắt ngang điều tra 800 cán bộ. Đánh giá tình trạng dinh dưỡng bằng chỉ số khối cơ thể (BMI), chỉ số WHR và xét nghiệm định lượng Hemoglobin máu, Albumin huyết thanh, Cholesterol máu, Triglycerid, LDL-cholesterol, HDL-cholesterol. Kết quả cho thấy tỉ lệ CED chung là 0,6 %. Tỉ lệ thừa cân - béo phì chung là 14,4%, tỷ lệ thừa cân nữ là 7,3% thấp hơn nam là 15,8 %. Tỷ lệ cán bộ có nguy cơ thừa cân, béo phì tính theo chỉ số vòng eo/vòng mông là 43,1%, trong đó cán bộ nữ là 44,5% cao hơn cán bộ nam là 42,8%. Nhóm cán bộ có sức khỏe phân loại B1 cao nhất chiếm tỷ lệ 88,9%, loại A chiếm 7,1%, loại B2 chiếm 3,2%, loại C chiếm 0,8%. Chỉ số Albumin huyết thanh trung bình là 43,6 ± 4,6 g/l; Protein huyết thanh trung bình là 70,0 ± 8,1 g/l, Glucose máu trung bình là 6,7 ± 1,5 mmol/l. Chỉ số Cholesterol máu trung bình là 5,29±0,66 mmol/; chỉ số Triglycerid máu trung bình là 2,26±0,9 mmol/l; chỉ số H-DLC trung bình là 1,96 ± 0,68 (mmol/l). L-DLC là 2,91±0,56 mmol/l.

Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity

Lassa virus is endemic in West Africa and can cause severe hemorrhagic fever. The viral L protein transcribes and replicates the RNA genome via its RNA-dependent RNA polymerase activity. Here, we present nine cryo-EM structures of the L protein in the apo-, promoter-bound pre-initiation and active RNA synthesis states. We characterize distinct binding pockets for the conserved 3’ and 5’ promoter RNAs and show how full-promoter binding induces a distinct pre-initiation conformation. In the apo- and early elongation states, the endonuclease is inhibited by two distinct L protein peptides, whereas in the pre-initiation state it is uninhibited. In the early elongation state, a template-product duplex is bound in the active site cavity together with an incoming non-hydrolysable nucleotide and the full C-terminal region of the L protein, including the putative cap-binding domain, is well-ordered. These data advance our mechanistic understanding of how this flexible and multifunctional molecular machine is activated.

Subcellular localization of nucleocapsid protein of SFTSV and its assembly into the ribonucleoprotein complex with L protein and viral RNA

Severe fever with thrombocytopenia syndrome virus (SFTSV) is an emerging bunyavirus that causes novel zoonotic diseases in Asian countries including China, Japan, South Korea, and Vietnam. In phleboviruses, viral proteins play a critical role in viral particle formation inside the host cells. Viral glycoproteins (GPs) and RNA-dependent RNA polymerase (RdRp) are colocalized in the Golgi apparatus and endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The nucleocapsid (N) protein was widely expressed in the cytoplasm, even in cells coexpressing GP. However, the role of SFTSV N protein remains unclear. The subcellular localization of SFTSV structural proteins was investigated using a confocal microscope. Subsequently, minigenome and immunoprecipitation assays were carried out. The N protein interacts with viral RNA (vRNA) and further shows translational activity with RdRp which is L protein and localized in the ERGIC and Golgi apparatus when co-expressed with GP. On the other hand, mutant N protein did not interact with vRNA either localized in the ERGIC or Golgi apparatus. The interaction between the N protein of SFTSV and vRNA is important for the localization of viral proteins and viral assembly. This study provides useful insights into the life cycle of SFTSV, which will lead to the detection of antiviral targets.

Structure of Rift Valley fever virus RNA-dependent RNA polymerase

Rift Valley fever virus (RVFV) belongs to the order Bunyavirales and is the type species of genus Phlebovirus , which accounts for over 50% of family Phenuiviridae species. RVFV is mosquito-borne and causes severe diseases in both humans and livestock, and consists of three segments (S, M, L) in the genome. The L segment encodes an RNA-dependent RNA polymerase (RdRp, L protein) that is responsible for facilitating the replication and transcription of the virus. It is essential for the virus and has multiple drug targets. Here, we established an expression system and purification procedures for full-length L protein, which is composed of an endonuclease domain, RdRp domain, and cap-binding domain. A cryo-EM L protein structure was reported at 3.6 Å resolution. In this first L protein structure of genus Phlebovirus , the priming loop of RVFV L protein is distinctly different from those of other L proteins and undergoes large movements related to its replication role. Structural and biochemical analyses indicate that a single template can induce initiation of RNA synthesis, which is notably enhanced by 5’ viral RNA. These findings help advance our understanding of the mechanism of RNA synthesis and provide an important basis for developing antiviral inhibitors. Importance The zoonosis RVF virus (RVFV) is one of the most serious arbovirus threats to both human and animal health. RNA-dependent RNA polymerase (RdRp) is a multifunctional enzyme catalyzing genome replication as well as viral transcription, so the RdRp is essential for studying the virus and has multiple drug targets. In our study, we report the structure of RVFV L protein at 3.6 Å resolution by cryo-EM. This is the first L protein structure of genus Phlebovirus. Strikingly, a single template can initiate RNA replication. The structure and assays provide a comprehensive and in-depth understanding of the catalytic and substrate recognition mechanism of RdRp.

Molasses as a new nutrition medium for Scenedsmus quadricauda growth and production of some bio compounds

Algae comprise a large group of Thallophyta, which may be used as direct nutrition of human beings. Molasses is the by-product of the sugar manufacturing facility. In this study, a locally isolated Scendsmus quadricauda from the environment of Mosul in the Shalalat region was obtained. Biomass of Scenedsmus was measurement by carried out and filtration then drying in an oven for 24 h and weighed, Estimation of chlorophyll and protein and carbohydrate content of Scenedsmus. The research has proved that the best growing period for Scendsmue quadricauda is 15 days when using sugar factory waste as a carbon source, the growth reached (1.42 nm) as optical density, biomass (1525 mg /L), chlorophyll (green), pigment (18 mg /l) protein content (396 mg /l ) and carbohydrates ( 501 mg / l ). The research showed that the use of sugar factory waste as a nutritional medium for algal growth in the dark (11.5%) achieved good growth of Scendesmues quadricauda ( 0.632 nm), biomass (820 mg / L), green pigment (Chlorophyll) (18 mg /L) protein content (235 mg / L ) and carbohydrates (401 mg/L). while using phosphor (0.018%) of K2HPO4 in dark medium achieved highest growth rate (0.91 nm) , biomass (1110 mg / L) chlorophyll ( 22 mg/L) protein (301mg/L) and carbohydrate (461 mg/L) . It is noted too , that using IAA (0.5 g/L) in dark medium support best growth (0.888 nm) , biomass (1010 mg/L) chlorophyll (25 mg/L) , protein (230mg/L) and carbohydrate (440 mg//L) . The study showed that thiamine (1 g/L) in dark medium achieved highest growth (0.750 nm) biomass (218 mg/L), chlorophyll (29mg/L), protein (220 mg/L), carbohydrate (340mg/L). Therefore, using Molasses can enhance the growth, biomass, chlorophyll, protein, and carbohydrate content in the S. quadricauda.

THIẾT LẬP KHOẢNG NỒNG ĐỘ CỦA SÁU THÔNG SỐ THƯỜNG QUY AST, ALT, CHOLESTEROL, TRIGLYCERIDE, GLUCOSE VÀ PROTEIN TRONG CHẾ TẠO MẪU NGOẠI KIỂM HÓA SINH

Xét nghiệm hóa sinh là một trong những chỉ định cận lâm sàng thường quy nhất tại các đơn vị y tế, các xét nghiệm này là căn cứ góp phần giúp các nhà lâm sàng đưa ra quyết định quan trọng cho công tác điều trị, chẩn đoán sớm và dự phòng bệnh, nghiên cứu khoa học trong y học,... Một trong những công tác nhằm đảm bảo độ tin cậy và chất lượng của xét nghiệm hóa sinh là ngoại kiểm tra chất lượng xét nghiệm [1,2,3]. Để chế tạo mẫu ngoại kiểm cần có khoảng nồng độ cao, thấp, bình thường của các thông số để sử dụng trong quá trình pha chế mẫu. Sáu thông số hóa sinh thường quy được khảo sát gồm protein, glucose, cholesterol, triglyceride, AST, ALT. Kết quả thu được khoảng nồng độ cao của glucose là 9,50 – 24,00mmol/L, protein là 95-115 g/L, cholesterol là 6,20–9,00mmol/L, triglyceride là 2,70 – 9,50mmol/L, AST là 95 - 350 U/L, ALT là 95 - 300 U/L; khoảng nồng độ thấp của glucose là 2,49 - 3,90 mmol/L, protein là 10 - 40 g/L, cholesterol là 2,50 – 3,70 mmol/L, triglyceride là 0,20 – 1,00 mmol/L, AST là 7 - 24 U/L, ALT là 7 - 24 U/L; khoảng nồng độ bình thường của glucose là 4,00 – 9,00 mmol/L, protein là 45-90g/L, cholesterol là 3,80–6,10 mmol/L, triglyceride là 1,10-2,60mmol/L, AST là 25-94U/L, ALT là 25-94 U/L.

Potential efficacy of existing drug molecules against severe fever with thrombocytopenia syndrome virus: an in silico study

Severe fever with thrombocytopenia syndrome (SFTS) is a zoonotic disease caused by the SFTS virus (SFTSV). SFTS can be considered a life-threatening notifiable infectious disease. The unavailability of specific therapeutics encourages the investigation of potential efficacy of existing drugs against this infection. Drug repurposing was done by performing virtual screening of already established drug molecules followed by 100 ns molecular dynamics simulations and molecular mechanics Poisson–Boltzmann surface area–based binding-energy calculation by targeting the SFTS L protein. On the basis of binding energy and protein–ligand interactions, top 10 promising hits were identified, showing stable binding with SFTS L protein. Further 100 ns atomistic MD simulation refined the hits from top 10 to top 4 with docking-based binding energy lesser than −8.0 kcal/mol toward the SFTS L protein and engaged in π–π interactions with pivotal amino acid residues. Various parameters and binding affinity of top 4 ligands towards L protein was computed. Ligand zaltoprofen exhibited best binding energy −220.095 kJ/mol. The present work is the first in silico study to assess bromfenac, cinchophen, elliptinium, and zaltoprofen; four promising hits against SFTS. Nonetheless, further proper biological evaluation is necessary to determine their efficacy against SFTS.