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Order Bunyavirales
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
Regarding structural proteins, as illustrated in Figure 32.2, the M RNA encodes a single open reading frame that is processed into the viral glycoproteins Gn and Gc, which are embedded into the lipid bilayer envelope of the virion, but the S RNA segment encodes the protein N, which, in addition to encapsidation of the genomic RNAs, functions as an RNA chaperone (for references see a review of Soldan and González-Scarano 2014). Unlike arenaviruses, the hantaviruses do not encode a matrix protein as a possible analogue of the protein Z that played the central role in the generation of arenaviral VLPs. It was speculated that the function of matrix protein in this case is carried out by the cytoplasmic tail of glycoprotein Gn that interacts with the nucleocapsid protein and/or genomic RNA (Strandin et al. 2013).
Infections
Published in Evelyne Jacqz-Aigrain, Imti Choonara, Paediatric Clinical Pharmacology, 2021
Evelyne Jacqz-Aigrain, Imti Choonara
The Human Inmmunodeficiency Virus (HIV) is a retrovirus. The virus contains 2 identical copies of a positive sense (i.e. mRNA) single-stranded RNA strand about 9,500 nucleotides long. These may be linked to each other to form a genomic RNA dimer. The RNA dimer is in turn associated with a basic nucleocapsid (NC) protein (p9/6). The ribonucleoprotein particle is encapsidated by a capsid made up of a capsid protein (CA), p24. The capsid environment also contains other viral proteins such as integrase and reverse transcriptase. It also contains a wide variety of other macromolecules derived from the cell including tRNAlys3, which serves as a primer for reverse transcription. The capsid has an icosahedral structure. The capsid is in turn encapsidated by a layer of matrix protein (MA), p17. This matrix protein is associated with a lipid bilayer or envelope.
Introduction and Review of Biological Background
Published in Luke R. Bucci, Nutrition Applied to Injury Rehabilitation and Sports Medicine, 2020
Other matrix proteins found in cartilage and connective tissues that are associated with GAGs are anchorin, chondronectin, fibronectin, entactin, fibrillin, integrins, laminins, sparc (osteonectin), tenascin, undulin, and cartilage matrix protein.79,83 These proteins are believed to help attach and bind chondrocytes and fibroblasts to their extracellular matrices. Roles in cell adhesion and regulation of matrix organization or assembly have been presented for these accessory matrix proteins.79,83
Expression of cartilage oligomeric matrix protein in periampullary adenocarcinoma is associated with pancreatobiliary-type morphology, higher levels of fibrosis and immune cell exclusion
Published in OncoImmunology, 2022
Konstantinos S. Papadakos, Sebastian Lundgren, Chrysostomi Gialeli, Patrick Micke, Artur Mezheyeuski, Jacob Elebro, Karin Jirström, Anna M. Blom
Cartilage oligomeric matrix protein (COMP) is a large pentameric protein that under normal conditions is almost exclusively expressed in the cartilage. COMP is a regulator of the extracellular matrix (ECM) assembly.1 Fibrosis is characterized by excessive production of ECM proteins, which leads to stiffening of the tissue causing cellular stress and organ malfunction.2 COMP is highly expressed in fibrotic diseases, such as scleroderma,3 idiopathic pulmonary fibrosis,4 and liver fibrosis.5,6 Under fibrotic conditions, COMP plays a vital role in the organization of ECM and regulates type I and II collagen7 production and fibrillogenesis.8 Moreover, in COMP knockout mice, the organization of collagen fibers is unraveled, and development of fibrosis attenuated. Moreover, fibroblasts lacking expression of COMP are unable to secret and deposit collagens into the ECM, leading to intracellular stress due to collagen accumulation in the endoplasmic reticulum.9
Combining locoregional CAR-T cells, autologous + allogeneic tumor lysate vaccination and levamisole in treatment of glioblastoma
Published in Immunopharmacology and Immunotoxicology, 2022
Meric A. Altinoz, Alp Ozpinar, Emily Hacker, Aysel Ozpinar
Malignant cells reside in a complex 3-dimensional microenvironment called tumor microenvironment, where physical cues are recently described as novel cancer hallmarks [16]. The swift tumor growth destroys the microarchitecture of surrounding tissues causing enhanced stiffness, increased interstitial fluid pressure, solid stress and vascular shear stress, and a modified structure of extracellular matrix. Physical cues also interfere with cancer immunosurveillance; for instance, increased solid stress hampers dendritic cell recruitment and enhanced matrix stiffness blocks the capability of dendritic cells to bind and internalize cancer antigens [16]. Enhanced solid stress also compresses blood vessels within tumors which leads to hypoxia and lactic acidosis in cancerous micromillieu which further hinders the immune cell activity and the exogenous delivery of immunotherapeutic cells and medicines through the narrowed vessel cavities [16]. Matrix protein crosslinking inhibitors and vasodilatator agents can bu utilized to reduce matrix stiffness and to overcome vessel narrowing, respectively. Also, nanomaterials including nanogels, polylactate glycolic acid-encapsulations and macroporous alginate scaffolds may be employed for locoregional delivery of immune cells and immunotherapeutics to handle with the obstacles of tumor microenvironment [16]. A short and elegant review regarding overcoming physical barriers against immunotherapy is recently published by Guo et al. [16].
Photoprotective effect of solid lipid nanoparticles of rutin against UVB radiation damage on skin biopsies and tissue-engineered skin
Published in Journal of Microencapsulation, 2022
Rodrigo Molina Martins, Silvia de Siqueira Martins, Gustavo Luis Ferreira Barbosa, Maria José Vieira Fonseca, Patrick J. Rochette, Véronique J. Moulin, Luis Alexandre Pedro de Freitas
UV irradiation increases MMP expression. that can degrade all components of extracellular matrix protein, including collagen and elastin, resulting in wrinkling and photoaging (Ma et al. 2018, Souza et al. 2018). We have measured the activity of MMPs in UVB irradiated and non-irradiated skin samples after treatment with rutin or the formulation containing SLNs of rutin. UVB irradiation of the skin increased the MMP content by 4-fold compared with the non-irradiated skins (Figure 5(b)). The formulation containing rutin or SLNs of rutin decreased the MMP content to the non-irradiated skin level. Those results suggest that the photochemopreventive effect of SLNs of rutin incorporated in topical formulation could balance the establishment of oxidative stress by decreasing lipid peroxidation and the activity of MMPs.