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773 results on '"Hytönen, Vesa"'

1. Progression of herpesvirus infection remodels mitochondrial organization and metabolism

Author

Leclerc, Simon, Gupta, Alka, Ruokolainen, Visa, Chen, Jian-Hua, Kunnas, Kari, Ekman, Axel A, Niskanen, Henri, Belevich, Ilya, Vihinen, Helena, Turkki, Paula, Perez-Berna, Ana J, Kapishnikov, Sergey, Mäntylä, Elina, Harkiolaki, Maria, Dufour, Eric, Hytönen, Vesa, Pereiro, Eva, McEnroe, Tony, Fahy, Kenneth, Kaikkonen, Minna U, Jokitalo, Eija, Larabell, Carolyn A, Weinhardt, Venera, Mattola, Salla, Aho, Vesa, and Vihinen-Ranta, Maija

Subjects
Medical Microbiology, Biochemistry and Cell Biology, Biomedical and Clinical Sciences, Biological Sciences, Infectious Diseases, Sexually Transmitted Infections, 2.1 Biological and endogenous factors, 2.2 Factors relating to the physical environment, Aetiology, Infection, Mitochondria, Herpesvirus 1, Human, Humans, Herpes Simplex, Animals, Herpesviridae Infections, Disease Progression, Chlorocebus aethiops, Microbiology, Immunology, Virology, Medical microbiology
Abstract

Viruses target mitochondria to promote their replication, and infection-induced stress during the progression of infection leads to the regulation of antiviral defenses and mitochondrial metabolism which are opposed by counteracting viral factors. The precise structural and functional changes that underlie how mitochondria react to the infection remain largely unclear. Here we show extensive transcriptional remodeling of protein-encoding host genes involved in the respiratory chain, apoptosis, and structural organization of mitochondria as herpes simplex virus type 1 lytic infection proceeds from early to late stages of infection. High-resolution microscopy and interaction analyses unveiled infection-induced emergence of rough, thin, and elongated mitochondria relocalized to the perinuclear area, a significant increase in the number and clustering of endoplasmic reticulum-mitochondria contact sites, and thickening and shortening of mitochondrial cristae. Finally, metabolic analyses demonstrated that reactivation of ATP production is accompanied by increased mitochondrial Ca2+ content and proton leakage as the infection proceeds. Overall, the significant structural and functional changes in the mitochondria triggered by the viral invasion are tightly connected to the progression of the virus infection.

Published
2024

7. DNA-origami-directed virus capsid polymorphism

Author

Seitz, Iris, Saarinen, Sharon, Kumpula, Esa-Pekka, McNeale, Donna, Anaya-Plaza, Eduardo, Lampinen, Vili, Hytönen, Vesa P., Sainsbury, Frank, Cornelissen, Jeroen J. L. M., Linko, Veikko, Huiskonen, Juha T., and Kostiainen, Mauri A.

Published
2023
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10. Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A

Author

Pavic, Karolina, Gupta, Nikhil, Omella, Judit Domènech, Derua, Rita, Aakula, Anna, Huhtaniemi, Riikka, Määttä, Juha A., Höfflin, Nico, Okkeri, Juha, Wang, Zhizhi, Kauko, Otto, Varjus, Roosa, Honkanen, Henrik, Abankwa, Daniel, Köhn, Maja, Hytönen, Vesa P., Xu, Wenqing, Nilsson, Jakob, Page, Rebecca, Janssens, Veerle, Leitner, Alexander, and Westermarck, Jukka

Published
2023
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11. Crystal structure of the FERM-folded talin head reveals the determinants for integrin binding

Author

Zhang, Pingfeng, Azizi, Latifeh, Kukkurainen, Sampo, Gao, Tong, Baikoghli, Mo, Jacquier, Marie-Claude, Sun, Yijuan, Määttä, Juha AE, Cheng, R Holland, Wehrle-Haller, Bernhard, Hytönen, Vesa P, and Wu, Jinhua

Subjects
Biochemistry and Cell Biology, Biological Sciences, Amino Acid Motifs, Animals, Binding Sites, Humans, Integrin beta3, Leucine, Mice, Microscopy, Electron, Transmission, Models, Molecular, Mutagenesis, Polylysine, Protein Domains, Protein Folding, Talin, talin, integrin, FERM domain, cell adhesion, NPxY motif
Abstract

Binding of the intracellular adapter proteins talin and its cofactor, kindlin, to the integrin receptors induces integrin activation and clustering. These processes are essential for cell adhesion, migration, and organ development. Although the talin head, the integrin-binding segment in talin, possesses a typical FERM-domain sequence, a truncated form has been crystallized in an unexpected, elongated form. This form, however, lacks a C-terminal fragment and possesses reduced β3-integrin binding. Here, we present a crystal structure of a full-length talin head in complex with the β3-integrin tail. The structure reveals a compact FERM-like conformation and a tightly associated N-P-L-Y motif of β3-integrin. A critical C-terminal poly-lysine motif mediates FERM interdomain contacts and assures the tight association with the β3-integrin cytoplasmic segment. Removal of the poly-lysine motif or disrupting the FERM-folded configuration of the talin head significantly impairs integrin activation and clustering. Therefore, structural characterization of the FERM-folded active talin head provides fundamental understanding of the regulatory mechanism of integrin function.

Published
2020

12. Structural Insight into CVB3-VLP Non-Adjuvanted Vaccine

Author

Hankaniemi, Minna M, Baikoghli, Mo A, Stone, Virginia M, Xing, Li, Väätäinen, Outi, Soppela, Saana, Sioofy-Khojine, Amirbabak, Saarinen, Niila VV, Ou, Tingwei, Anson, Brandon, Hyöty, Heikki, Marjomäki, Varpu, Flodström-Tullberg, Malin, Cheng, R Holland, Hytönen, Vesa P, and Laitinen, Olli H

Subjects
Biomedical and Clinical Sciences, Immunology, Biotechnology, Immunization, Prevention, Heart Disease, Vaccine Related, Infectious Diseases, Cardiovascular, 3.4 Vaccines, Prevention of disease and conditions, and promotion of well-being, Infection, Good Health and Well Being, Coxsackievirus B, vaccine, virus-like particle, Microbiology, Medical microbiology
Abstract

Coxsackievirus B (CVB) enteroviruses are common pathogens that can cause acute and chronic myocarditis, dilated cardiomyopathy, aseptic meningitis, and they are hypothesized to be a causal factor in type 1 diabetes. The licensed enterovirus vaccines and those currently in clinical development are traditional inactivated or live attenuated vaccines. Even though these vaccines work well in the prevention of enterovirus diseases, new vaccine technologies, like virus-like particles (VLPs), can offer important advantages in the manufacturing and epitope engineering. We have previously produced VLPs for CVB3 and CVB1 in insect cells. Here, we describe the production of CVB3-VLPs with enhanced production yield and purity using an improved purification method consisting of tangential flow filtration and ion exchange chromatography, which is compatible with industrial scale production. We also resolved the CVB3-VLP structure by Cryo-Electron Microscopy imaging and single particle reconstruction. The VLP diameter is 30.9 nm on average, and it is similar to Coxsackievirus A VLPs and the expanded enterovirus cell-entry intermediate (the 135s particle), which is ~2 nm larger than the mature virion. High neutralizing and total IgG antibody levels, the latter being a predominantly Th2 type (IgG1) phenotype, were detected in C57BL/6J mice immunized with non-adjuvanted CVB3-VLP vaccine. The structural and immunogenic data presented here indicate the potential of this improved methodology to produce highly immunogenic enterovirus VLP-vaccines in the future.

Published
2020

20. Molecular dynamics simulations reveal how vinculin refolds partially unfolded talin rod helices to stabilize them against mechanical force.

Author

Mykuliak, Vasyl V., Rahikainen, Rolle, Ball, Neil J., Bussi, Giovanni, Goult, Benjamin T., and Hytönen, Vesa P.

Subjects
MECHANICAL loads, DENATURATION of proteins, VINCULIN, MOLECULAR dynamics, SINGLE molecules
Abstract

Vinculin binds to specific sites of mechanically unfolded talin rod domains to reinforce the coupling of the cell's exterior to its force generation machinery. Force-dependent vinculin–talin complexation and dissociation was previously observed as contraction or extension of the unfolded talin domains respectively using magnetic tweezers. However, the structural mechanism underlying vinculin recognition of unfolded vinculin binding sites (VBSs) in talin remains unknown. Using molecular dynamics simulations, we demonstrate that a VBS dynamically refolds under force, and that vinculin can recognize and bind to partially unfolded VBS states. Vinculin binding enables refolding of the mechanically strained VBS and stabilizes its folded α-helical conformation, providing resistance against mechanical stress. Together, these results provide an understanding of a recognition mechanism of proteins unfolded by force and insight into the initial moments of how vinculin binds unfolded talin rod domains during the assembly of this mechanosensing meshwork. Author summary: Cells attach to and interact with their surroundings, and sense mechanical signals from the microenvironment. Vinculin and talin are classical examples of mechanosensitive proteins that complex in a force-dependent manner. Talin domains unfold under mechanical loads exposing buried vinculin binding sites, namely single α-helices. Such mechanical stretching enables recognition by vinculin, however, the structural states of vinculin's binding site when under force and the complexation mechanisms are poorly understood. We used molecular dynamics simulations to study the behavior of a single vinculin binding helix under mechanical load and during the initial moments of the vinculin–talin binding process. Our results reveal the highly dynamic nature of a vinculin binding helix under mechanical load. Depending on the force magnitude, the helix frequently reforms to a partially folded conformation on the nanosecond to microsecond timescale. Crucially, vinculin recognizes such partially folded helices in talin and promotes their refolding against force. Our findings are beyond the resolution limits imposed by experimental single molecule methods, suggesting a model which may be useful as a general mechanism for protein-protein binding under mechanical load. [ABSTRACT FROM AUTHOR]

Published
2024
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25. Thrombus Aspirates From Patients With Acute Ischemic Stroke Are Infiltrated by Viridans Streptococci

Author

Patrakka, Olli, primary, Tuomisto, Sari, additional, Pienimäki, Juha‐Pekka, additional, Ollikainen, Jyrki, additional, Oksala, Niku, additional, Lampinen, Vili, additional, Ojanen, Markus J. T., additional, Huhtala, Heini, additional, Hytönen, Vesa P., additional, Lehtimäki, Terho, additional, Martiskainen, Mika, additional, and Karhunen, Pekka J., additional

Published
2023
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32. Quantitative pigment extraction analysis for human pluripotent stem cell derived retinal pigment epithelial cells

Author

Rieck, Jochen, Juuti-Uusitalo, Kati, Autio, Reija, Hytönen, Vesa, Skottman, Heli, Magjarevic, Ratko, Editor-in-chief, Ładyżyński, Piotr, Series editor, Ibrahim, Fatimah, Series editor, Lacković, Igor, Series editor, Rock, Emilio Sacristan, Series editor, Eskola, Hannu, editor, Väisänen, Outi, editor, Viik, Jari, editor, and Hyttinen, Jari, editor

Published
2018
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34. Growth of immobilized DNA by polymerase: bridging nanoelectrodes with individual dsDNA molecules

Author

Linko, Veikko, Leppiniemi, Jenni, Shen, Boxuan, Niskanen, Einari, Hytönen, Vesa P., and Toppari, J. Jussi

Subjects
Physics - Biological Physics, Condensed Matter - Other Condensed Matter, Condensed Matter - Soft Condensed Matter
Abstract

We present a method for controlled connection of gold electrodes with dsDNA molecules (locally on a chip) by utilizing polymerase to elongate single-stranded DNA primers attached to the electrodes. Thiol-modified oligonucleotides are directed and immobilized to nanoscale electrodes by means of dielectrophoretic trapping, and extended in a procedure mimicking PCR, finally forming a complete dsDNA molecule bridging the gap between the electrodes. The technique opens up opportunities for building from the bottom-up, for detection and sensing applications, and also for molecular electronics., Comment: 5 pages, 3 figures; Nanoscale (2011)

Published
2011
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47. ConFERMing the role of talin in integrin activation and mechanosignaling

Author

Bachmann, Michael, Su, Baihao, Rahikainen, Rolle, Hytönen, Vesa P., Wu, Jinhua, Wehrle-Haller, Bernhard, Tampere University, BioMediTech, and Fimlab Laboratories PLC

Subjects
3111 Biomedicine
Abstract

Talin (herein referring to the talin-1 form), is a cytoskeletal adapter protein that binds integrin receptors and F-actin, and is a key factor in the formation and regulation of integrin-dependent cell-matrix adhesions. Talin forms the mechanical link between the cytoplasmic domain of integrins and the actin cytoskeleton. Through this linkage, talin is at the origin of mechanosignaling occurring at the plasma membrane-cytoskeleton interface. Despite its central position, talin is not able to fulfill its tasks alone, but requires help from kindlin and paxillin to detect and transform the mechanical tension along the integrin-talin-F-actin axis into intracellular signaling. The talin head forms a classical FERM domain, which is required to bind and regulate the conformation of the integrin receptor, as well as to induce intracellular force sensing. The FERM domain allows the strategic positioning of protein-protein and protein-lipid interfaces, including the membrane-binding and integrin affinityregulating F1 loop, as well as the interaction with lipid-anchored Rap1 (Rap1a and Rap1b in mammals) GTPase. Here, we summarize the structural and regulatory features of talin and explain how it regulates cell adhesion and force transmission, as well as intracellular signaling at integrin-containing cell-matrix attachment sites. publishedVersion

Published
2023

49. Thermoresponsive and biocompatible poly(N-isopropylacrylamide)–cellulose nanocrystals hydrogel for cell growth

Author

Trubetskaya, Anna, primary, Leppiniemi, Jenni, additional, Lipponen, Sami, additional, Lombardo, Salvatore, additional, Thielemans, Wim, additional, Maloney, Thaddeus, additional, Pääkkönen, Timo, additional, Kesari, Kavindra Kumar, additional, Ruokolainen, Janne, additional, Hytönen, Vesa P., additional, and Kontturi, Eero, additional

Published
2023
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