Listar por autoría "d6cfa6a6-3f5c-44f7-a8e2-76e55cf0c274"
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Amphiphilic COSAN and I2-COSAN crossing synthetic lipid membranes: planar bilayers and liposomes
Verdiá Báguena, Carmen; Alcaraz, Antonio; Aguilella, Vicente; Cioran, Ana M.; Tachikawa, Shoji; Nakamura, Hiroyuki; Teixidor, Francesc; Viñas, Clara Royal Society of Chemistry (2014-03)The boron-rich cobaltabisdicarbollide (COSAN) and its 8,80-I2 derivative (I2-COSAN), both of purely inorganic nature, are shown to cross through synthetic lipid membranes. These results reveal unexpected properties at the ... -
Analysis of SARS-CoV E protein ion channel activity by tuning the protein and lipid charge
Verdiá Báguena, Carmen; Nieto Torres, José L.; Alcaraz, Antonio; De Diego, Marta L.; Enjuanes, Luis; Aguilella, Vicente Elsevier (2013-05-18)A partial characterization of the ion channels formed by the SARS coronavirus (CoV) envelope (E) protein was previously reported (C. Verdiá-Báguena et al., 2012 [12]). Here, we provide new significant insights on the ... -
Channel-Inactivating Mutations and Their Revertant Mutants in the Envelope Protein of Infectious Bronchitis Virus
To, Janet; Surya, Wahyu; To, Sing Fung; Li, Yan; Verdiá Báguena, Carmen; Queralt-Martín, María; Aguilella, Vicente; Ding, Xiang Liu; Torres, Jaume American Society for Microbiology (2016-12)It has been shown previously in the severe acute respiratory syndrome coronavirus (SARS-CoV) that two point mutations, N15A and V25F, in the transmembrane domain (TMD) of the envelope (E) protein abolished channel activity ... -
Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids
Aguilella, Vicente; Alcaraz, Antonio; Verdiá Báguena, Carmen; Nieto Torres, José L.; De Diego, Marta L.; Torres, Jaume; Enjuanes, Luis Elsevier (2012-10)Coronavirus (CoV) envelope (E) protein ion channel activity was determined in channels formed in planar lipid bilayers by peptides representing either the transmembrane domain of severe acute respiratory syndrome CoV ... -
Energy transduction and signal averaging of fluctuating electric fields by a single protein ion channel
Verdiá Báguena, Carmen; Gómez, V.; Cervera, Javier; Ramírez, Patricio; Mafe, Salvador Royal Society of Chemistry (2017)We demonstrate the electrical rectification and signal averaging of fluctuating signals using a biological nanostructure in aqueous solution: a single protein ion channel inserted in the lipid bilayer characteristic of ... -
Entropy–enthalpy compensation at the single protein level: pH sensing in the bacterial channel OmpF
Alcaraz, Antonio; Queralt-Martín, María; Verdiá Báguena, Carmen; Aguilella, Vicente; Mafe, Salvador The Royal Society of Chemistry (2014)The pH sensing mechanism of the OmpF channel operates via ligand modification: increasing acidity induces the replacement of cations with protons in critical binding sites decreasing the channel conductance. Aside from the ... -
Inhibition of the human respiratory syncytial virus small hydrophobic protein and structural variations in a bicelle environment
Li, Yan; To, Janet; Verdiá Báguena, Carmen; Dossena, Silvia; Surya, Wahyu; Huang, Mei; Paulmichl, Markus; Liu, Ding Xiang; Aguilella, Vicente; Torres, Jaume American Society for Microbiology (2014)The small hydrophobic (SH) protein is a 64-amino-acid polypeptide encoded by the human respiratory syncytial virus (hRSV). SH protein has a single α-helical transmembrane (TM) domain that forms pentameric ion channels. ... -
Ion channel activity of the CSFV p7 viroporin in surrogates of the ER lipid bilayer
Largo, Eneko; Verdiá Báguena, Carmen; Aguilella, Vicente; Nieva, José L.; Alcaraz, Antonio Elsevier (2016-01)Viroporins comprise a family of non-structural proteins that play significant and diverse roles during the replication cycle of many animal viruses. Consequently, they have become promising targets for inhibitory drug and ... -
Lipid charge regulation of non-specific biological ion channels
Aguilella, Vicente; Verdiá Báguena, Carmen; Alcaraz, Antonio Royal Society of Chemistry (2014)Ion channels are specialized proteins that enable the movement of charges through otherwise impermeable lipidic membranes. Their action is essential in living organisms facilitating electric signaling, muscle contraction ... -
MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
Surya, Wahyu; Li, Yan; Verdiá Báguena, Carmen; Aguilella, Vicente; Torres, Jaume Elsevier (2015-04)The Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly identified pathogen able of human transmission that causes a mortality of almost 40%. As in the case of SARS-CoV, MERS virus lacking E protein represents ... -
Protein Ion Channels as Molecular Ratchets. Switchable Current Modulation in Outer Membrane Protein F Porin Induced by Millimolar La3+ Ions
Verdiá Báguena, Carmen; Queralt-Martín, María; Aguilella, Vicente; Alcaraz, Antonio American Chemical Society (2012)The quest for innovative tunable nanodevices has mainly focused on switches that modulate their properties through engineered conformational changes. We propose here an alternative route that takes advantage of the crucial ... -
Relevance of Viroporin Ion Channel Activity on Viral Replication and Pathogenesis
Nieto Torres, José L.; Verdiá Báguena, Carmen; Castaño Rodríguez, Carlos; Aguilella, Vicente; Enjuanes, Luis MDPI (2015-07)Modification of host-cell ionic content is a significant issue for viruses, as several viral proteins displaying ion channel activity, named viroporins, have been identified. Viroporins interact with different cellular ... -
Role of Severe Acute Respiratory Syndrome Coronavirus Viroporins E, 3a, and 8a in Replication and Pathogenesis
Castaño Rodríguez, Carlos; Honrubia, José M.; Gutiérrez-Álvarez, Javier; De Diego, Marta L.; Nieto Torres, José L.; Jiménez Guardeño, José M.; Regla Nava, José A.; Fernández Delgado, Raúl; Verdiá Báguena, Carmen; Queralt-Martín, María; Kochan, Grazyna; Perlman, Stanley; Aguilella, Vicente; Sola, Isabel; Enjuanes, Luis American Society for Microbiology (2018)Viroporins are viral proteins with ion channel (IC) activity that play an important role in several processes, including virus replication and pathogenesis. While many coronaviruses (CoVs) encode two viroporins, severe ... -
Severe acute respiratory syndrome coronavirus E protein transports calcium ions and activates the NLRP3 inflammasome
Nieto Torres, José L.; Verdiá Báguena, Carmen; Jiménez Guardeño, José M.; Regla Nava, José A.; Castaño Rodríguez, Carlos; Fernández Delgado, Raúl; Torres, Jaume; Aguilella, Vicente; Enjuanes, Luis Elsevier (2015-11)Severe acute respiratory syndrome coronavirus (SARS-CoV) envelope (E) protein is a viroporin involved in virulence. E protein ion channel (IC) activity is specifically correlated with enhanced pulmonary damage, edema ... -
Severe Acute Respiratory Syndrome Coronavirus Envelope Protein Ion Channel Activity Promotes Virus Fitness and Pathogenesis
Nieto Torres, José L.; De Diego, Marta L.; Verdiá Báguena, Carmen; Jiménez Guardeño, José M.; Regla Nava, José A.; Fernández Delgado, Raúl; Castaño Rodríguez, Carlos; Alcaraz, Antonio; Torres, Jaume; Aguilella, Vicente; Enjuanes, Luis Public Library of Science (2014)Deletion of Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) envelope (E) gene attenuates the virus. E gene encodes a small multifunctional protein that possesses ion channel (IC) activity, an important function ... -
Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance
Verdiá Báguena, Carmen; Aguilella, Vicente; Queralt-Martín, María; Alcaraz, Antonio Elsevier (2021-06-01)The envelope protein E of the SARS-CoV coronavirus is an archetype of viroporin. It is a small hydrophobic protein displaying ion channel activity that has proven highly relevant in virus-host interaction and virulence. ...