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Role of Microbial Biofilm in Agriculture and Their Impact on Environment
Published in Bakrudeen Ali Ahmed Abdul, Microbial Biofilms, 2020
Asma Rehman, Lutfur Rahman, Ata Ullah, Muhammad Bilal Yazdani, Muhammad Irfan, Waheed S. Khan
The formation of biofilms from cellular adhesion to the substrate and to the mature biofilm development is a well-regulated established process (Prüß et al. 2006). Gene expression in biofilm formation is influenced by highly regulated and complex pathways (Prigent-Combaret et al. 2001). A cyclic diguanylate /cyclic di- Guanosine monophosphate (GMP) (c-di-GMP) has a critical role in the determination of bacterial cell’s position as to remain free in the environment or in biofilm (Römling, Gomelsky, and Galperin 2005, Wolfe and Visick 2008). It has the capability to regulate transcription by the attachment to the effector proteins (Weber et al. 2006, Hickman and Harwood 2008) and involve in adhesin secretion and localization (Monds et al. 2007). Moreover function and motility of flagella and EPS synthesis can also depend on c-di-GMP activity (Weinhouse et al. 1997, Merighi et al. 2007). It has been reported that enzyme histidine kinase (Chen et al. 2012) and sRNA (small noncoding RNA) also have a significant effect on biofilm formation (Chambers and Sauer 2013). Moreover, gene expression regulation is very much important in microbial cells due to the that their occur synthesis and secretion of cellular polymeric substances, which play significant role in the attachment of cells to the surfaces. However, it is also notable that genes which are involved in the synthesis of chemotaxis proteins and proteins for the development of flagella are also regulated to ensure the movement of microbes (Barraud et al. 2006, Rollet, Gal, and Guzzo 2009).
Optogenetic Modulation of Neural Circuits
Published in Francesco S. Pavone, Shy Shoham, Handbook of Neurophotonics, 2020
Mathias Mahn, Oded Klavir, Ofer Yizhar
Plant, bacterial, and fungal proteins utilize light-oxygen-voltage-sensing (LOV) domains (Christie et al., 1999) as light sensor (Herrou and Crosson, 2011; Losi and Gärtner, 2012; Christie et al., 2015). Their small size (~120 amino acids) and flavin-based cofactors, which are abundantly available in animal tissues, make these blue-light sensors especially suitable for optogenetic approaches. Several studies successfully utilized LOV domains fused to effector proteins to accomplish light-based control of subcellular protein concentrations (Guntas et al., 2015; Kawano et al., 2015; Wang et al., 2016; Niopek et al., 2016), gene expression (Wang et al., 2012; Ma et al., 2013), DNA manipulation (Kawano et al., 2016), calcium signaling (Pham et al., 2011), or protein stability (Bonger et al., 2014). Different LOV domain proteins were engineered to achieve changes in the dimerization state of the protein upon illumination. Vivid (VVD) is one such protein, which homodimerizes upon light absorption (Zoltowski et al., 2007). This dimerization is well-characterized and mutants spanning a wide range of inactivation kinetics are available (Zoltowski et al., 2009). A heterodimerizing version of VVD has been generated (Kawano et al., 2015), and was utilized to reconstitute a split Cre recombinase enzyme, leading to the generation of an efficient light-activatable Cre-dependent expression system (Kawano et al., 2016).
The Role of Nanoparticles in Cancer Therapy through Apoptosis Induction
Published in Hala Gali-Muhtasib, Racha Chouaib, Nanoparticle Drug Delivery Systems for Cancer Treatment, 2020
Marveh Rahmati, Saeid Amanpour, Hadiseh Mohammadpour
TNFα is induced by cytokines which are released by inflammatory cells and particularly activated macrophages. TNFα is the main extrinsic stimulus of extrinsic apoptosis. TNFR1 and TNFR2 are two receptors for TNFα in most cells. After the binding of TNFα to TNFR1, CASP-8 is activated in DICS complex, which contains the intermediate membrane proteins TNF receptor-associated death domain (TRADD). TRADD subsequently recruits other effector proteins such as FADD/MORT1 (FAS-Associated Death Domain Protein) into DISC complex. Regardless of apoptosis, the TNFα-TNFR pathway can also indirectly activate some of the transcription factors involved in cell survival and inflammatory responses [34]. In response to TNF induction, the transcription factor NF-κB and MAP kinases, including ERK, p38, and JNK, are activated in most cell types. Apoptosis or necrosis could also be initiated.
Involvement of Pseudomonas aeruginosa in the occurrence of community and hospital acquired diarrhea, and its virulence diversity among the stool and the environmental samples
Published in International Journal of Environmental Health Research, 2022
Parisa Fakhkhari, Elahe Tajeddin, Masoumeh Azimirad, Siavosh Salmanzadeh-Ahrabi, Ahya Abdi-Ali, Bahram Nikmanesh, Babak Eshrati, Mohammad Mehdi Gouya, Parviz Owlia, Mohammad Reza Zali, Masoud Alebouyeh
Although P. aeruginosa is an agent linked to the gastrointestinal infections, it generally causes diseases in exraintestinal sites. P. aeruginosa exploits some virulence factors to establish its infection in the lung (Ballok and O’Toole 2013). P. aeruginosa exotoxins have several functions, including Adenosine diphosphate (ADP)-ribosyltransferase (such as Exotoxin A), cytotoxic (such as pyocyanin), and proteolytic (such as elastase that degrades host defenses) activities (Shi et al. 2012). This bacterium encodes a type III secretions system, a system that can inject toxic effector proteins into the cytoplasm of eukaryotic cells. Currently, four effector proteins are defined in P. aeruginosa: ExoU, ExoS, ExoT, and ExoY. These effector proteins modulate host cell functions, change cytoskeletal organization, and signal transduction. While most of P. aeruginosa strains carry exoT and exoY genes, exoS and exoU show diversity among the isolates.