Influenza epidemiology and risk factors for severe acute respiratory infection in Morocco during the 2016/2017 and 2017/2018 seasons.

INTRODUCTION: in order to implement an influenza vaccination program for high-risk-groups in Morocco, as recommended by the World Health Organization, an epidemiological study indicating the influenza virus effect in the development of complicated influenza for subjects with co-morbidity was required. The present study aims to evaluate the risk factors for severe acute respiratory infections caused by influenza in risk groups. METHODS: this research is based on the epidemiological and virological surveillance data of severe acute respiratory infections and influenza-like illness during the 2016/2017 and 2017/2018 seasons. It was realized using a retrospective series study with a descriptive and analytical purpose. RESULTS: the over-recruitment of pediatric cases with a severe acute respiratory infection has been significantly rectified because cases of severe acute respiratory infections under 15 years old in the 2017/2018 season represent only 57.9%, whereas they represented 75.9% of the total cases of severe acute respiratory infections during the 2016/2017 season. The influenza positivity rate has increased globally and specifically by age group, clinical service and co-morbidity. The risk factors considered were significantly associated with hospitalization for influenza-associated severe acute respiratory infections. The multivariate logistic regression analysis considers male sex (OR=2.1), age ≥65 years (OR=5.4), presence of influenza cases in the surroundings (OR=0.1), diabetes (OR=7.5) and chronic respiratory disease (OR=10.9) as risk factors influenza-associated severe acute respiratory infections. CONCLUSION: the risk assessment of influenza-associated severe acute respiratory infections in high-risk groups revealed national epidemiological findings, particularly for diabetics and the elderly. An influenza vaccination program for these high-risk-groups becomes much recommended in Morocco.

Insight into the mechanism of lipids binding and uptake by CD36 receptor.

The membrane protein CD36 is a member of the class B scavenger receptor family. It plays a crucial role in some cardiovascular pathologies and metabolic diseases. Studying the mechanism of action of CD36 receptor is limited due to the absence of its tridimensional crystallized structure. The molecular docking method has allowed us to perform various simulation of the CD36 receptor interaction with their ligands involved in the development of some diseases. In this work, we predicted a tridimensional structure model of CD36 extracellular domain. In addition, we have achieved several tests of rigid and flexible docking by acting on residues proposed in previous experimental researches as essential in fixing of LFCAs. Furthermore, we have acted on regions that appear a key binding site of LFCAs. The physicoc hemical evaluation indicated the reliability of the proposed CD36 structure used for different molecular docking tests. Based on the docking outcome, we were able to propose the different steps of the mechanism allowing the interaction of fatty acids on CD36 receptor and their penetration into the cell cytoplasm. The obtained results and taking in consideration CD36 receptor as a therapeutic target will help us to suggest the mechanism by which an antagonist may inhibit this receptor by acting on its extracellular domain.

Affinity comparison of different THCA synthase to CBGA using modeling computational approaches.

The Δ(9-)Tetrahydrocannabinol (THCA) is the primary psychoactive compound of Cannabis Sativa. It is produced by Δ(1-) Tetrahydrocannabinolic acid synthase (THCA) which catalyzes the oxidative cyclization of cannabigerolic acid (CBGA) the precursor of the THCA. In this study, we were interested by the three dimensional structure of THCA synthase protein. Generation of models were done by MODELLER v9.11 and homology modeling with Δ1-tetrahydrocannabinolic acid (THCA) synthase X ray structure (PDB code 3VTE) on the basis of sequences retrieved from GenBank. Procheck, Errat, and Verify 3D tools were used to verify the reliability of the six 3D models obtained, the overall quality factor and the Prosa Z-score were also used to check the quality of the six modeled proteins. The RMSDs for C-alpha atoms, main-chain atoms, side-chain atoms and all atoms between the modeled structures and the corresponding template ranged between 0.290 Å-1.252 Å, reflecting the good quality of the obtained models. Our study of the CBGA-THCA synthase docking demonstrated that the active site pocket was successfully recognized using computational approach. The interaction energy of CBGA computed in 'fiber types' proteins ranged between -4.1 95 kcal/mol and -5.95 kcal/mol whereas in the 'drug type' was about -7.02 kcal/mol to -7.16 kcal/mol, which maybe indicate the important role played by the interaction energy of CBGA in the determination of the THCA level in Cannabis Sativa L. varieties. Finally, we have proposed an experimental design in order to explore the binding energy source of ligand-enzyme in Cannabis Sativa and the production level of the THCA in the absence of any information regarding the correlation between the enzyme affinity and THCA level production. This report opens the doors to more studies predicting the binding site pocket with accuracy from the perspective of the protein affinity and THCA level produced in Cannabis Sativa.

Three Dimensional Structure Prediction of Fatty Acid Binding Site on Human Transmembrane Receptor CD36.

CD36 is an integral membrane protein which is thought to have a hairpin-like structure with alpha-helices at the C and N terminals projecting through the membrane as well as a larger extracellular loop. This receptor interacts with a number of ligands including oxidized low density lipoprotein and long chain fatty acids (LCFAs). It is also implicated in lipid metabolism and heart diseases. It is therefore important to determine the 3D structure of the CD36 site involved in lipid binding. In this study, we predict the 3D structure of the fatty acid (FA) binding site [127-279 aa] of the CD36 receptor based on homology modeling with X-ray structure of Human Muscle Fatty Acid Binding Protein (PDB code: 1HMT). Qualitative and quantitative analysis of the resulting model suggests that this model was reliable and stable, taking in consideration over 97.8% of the residues in the most favored regions as well as the significant overall quality factor. Protein analysis, which relied on the secondary structure prediction of the target sequence and the comparison of 1HMT and CD36 [127-279 aa] secondary structures, led to the determination of the amino acid sequence consensus. These results also led to the identification of the functional sites on CD36 and revealed the presence of residues which may play a major role during ligand-protein interactions.