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Weed pollen allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Michael Hauser, Gabriele Gadermaier, Sabrina Wildner, Lisa Pointner, Michael Wallner, Fatima Ferreira
The members of the profilin family are small proteins (14 kDa) expressed in all eukaryotic cells and some viruses, sharing greater than 75% sequence identities [64,65]. Their conformation displays a central antiparallel β-sheet core surrounded by α helices representative of α/β proteins. Profilins are actin-monomer-binding proteins promoting the polymerization of actin filaments for the cytoskeleton's turnover and are, therefore, involved in cell motility, cytokinesis, and outgrowth of the pollen tube [66–69]. Additional binding partners have been identified, including phosphatidylinositols and L-proline-rich proteins, suggesting the contribution of profilins in other essential cellular processes, such as exocytosis-endocytosis and in signaling pathways [70].
Cytoskeletons (F-actin) and spermatogenesis
Published in C. Yan Cheng, Spermatogenesis, 2018
Liza O’Donnell, Peter G. Stanton
Actin monomers are relatively flat proteins with a cleft that binds tightly to ATP, which is hydrolyzed during polymerization. Monomers spontaneously dimerize then polymerize into a helical single-stranded filament (Figure 15.1a). Due to the orientation of actin monomers at each end, F-actin has a “pointy end,” which is slow to polymerize, and a “barbed end,” which rapidly polymerizes and grows in length (Figure 15.1). Profilin is a small protein that plays a major role in actin polymerization via binding to monomers (Figure 15.1a) and to the polymerized filament and cytoskeletal proteins.4 Once polymerized, actin filaments can be cross-linked into higher-order structures via association with various microtubule-associated proteins (Figure 15.1b), (reviewed in Pollard 2016).1 The complexity of actin structures is further increased by branching, facilitated by the Arp2/3 complex. The Arp2/3 complex, in association with nucleation promoting factors such as WASH and WASP, binds to the side of a filament and nucleates a daughter branch,5 whereas cortactin stabilizes the branches (Figure 15.1b).
Biomolecular and Clinical Aspects of Food Allergy
Published in Andreas L. Lopata, Food Allergy, 2017
The profilin-like superfamily comprises four member families. One of them, the profilin family, are proteins that are highly conserved in higher plants with sequence identities of at least 75% (Radauer et al. 2006). Profilins are cytoplasmic proteins of 12-15 kDa and are present in all eukaryotic cells. They bind monomeric actin (Schutt et al. 1993) and are involved in the dynamic turnover and restructuring of the actin cytoskeleton (Witke 2004). Profilin from birch pollen was the first profilin that was described as allergenic (Valenta et al. 1991). Subsequently, a large number of cross-reactive profilin allergens were described in pollen of trees, grasses and weeds (Gadermaier et al. 2014, Hauser et al. 2010). As profilin-specific IgE cross-reacts with practically all plant profilins, a profilin sensitization is regarded as a risk factor for allergic reactions to various plant pollen (Mari 2001) and plant foods (Asero et al. 2003, Fernandez-Rivas 2015). However, the clinical relevance of a profilin sensitization is still under discussion (Santos and Van Ree 2011). The clinical relevance of a profilin sensitization was shown for profilins from cantaloupe, watermelon, tomato, banana, pineapple, orange and kaki (Anliker et al. 2001, Asero et al. 2008, Lopez-Torrejon et al. 2005). Recently, profilins were shown to be complete food allergens capable of eliciting severe reactions in plant food allergic patients that had been exposed to high levels of grass pollen (Alvarado et al. 2014).
Development of a novel anti-biofilm peptide derived from profilin of Spodoptera frugiperda
Published in Biofouling, 2020
Amanda Carolina Borges da Silva, Janaina de Cassia Orlandi Sardi, Daniella Gorete Lourenço de Oliveira, Caio Fernando Ramalho de Oliveira, Helder Freitas dos Santos, Edson Lucas dos Santos, Edson Crusca, Marlon Henrique Cardoso, Octávio Luiz Franco, Maria Lígia Rodrigues Macedo
In this study, the profilin protein sequence from Spodoptera frugiperda was selected as a template to design a new synthetic AMP, named PEP-IA18. Profilin is a protein involved in the dynamics and restructuring of the actin cytoskeleton, which is essential for tissue regeneration and pathogen capture by immune cells (Mahoney et al. 1997; Krishnan and Moens 2009). To reduce the molecular size, to improve the selectivity for microorganism cells and to reduce the cytotoxicity of PEP-IA18 for human cells, modifications in the original profilin sequence were carried out with the aid of the Antimicrobial Peptide Database (APD3) and Collection of Anti-Microbial Peptides (CAMPr3) algorithms. As a result, PEP-IA18 showed antifungal activity against Candida spp., demonstrating potential as an alternative in the treatment of yeast infections.
Construction of dual nanomedicines for the imaging and alleviation of atherosclerosis
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2020
Shuihua Zhang, Wan Xu, Peng Gao, Wenli Chen, Quan Zhou
Profilin-1, a small actin-binding protein, regulates the dynamics of actin polymerization, which is key for cell motility in vivo [35]. Profilin-1 expression and dysfunction play an important role in the development of cardiovascular diseases [36,37]. Western blot analysis revealed that the expression of profilin-1 in the arterial wall of ApoE−/− mice was significantly higher than that in the normal group (Figure 4(c,d)). This result was consistent with the upregulated expression of profilin-1 in MOVAS cells treated with oxidized low-density lipoprotein (Figure S6). These results suggest that profilin-1 can be used as a targeted molecule for atherosclerosis; this is consistent with previous studies [6,8]. Thus, profilin-1 may be a potential new target for the diagnosis and treatment of cardiovascular diseases.