Author

Carmen Velázquez

University of the Basque CountryORCID 0000-0002-0179-5533Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Microbiology· 3

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 3 Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 3 Assay:cryo-EM· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

David Albesa-JovéiD· 3 shared Jon Altuna-AlvareziD· 3 shared Amaia Gonzalez MagañaiD· 2 shared Antonio AlcaraziD· 2 shared Cristina CivantosiD· 2 shared Jéssica Rojas-PalominoiD· 2 shared Maialen Zabala-ZearretaiD· 2 shared María Queralt-MartíniD· 2 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 44 mutual co-author links

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3 shared papersMicrobiology

David Albesa-JovéORCID

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Author profile →

3 papers

Recent·Most cited

Tke5 is a novel Pseudomonas putida toxin that depolarises membranes killing plant pathogens

Carmen Velázquez, Alejandro Arce‐Rodríguez, Jon Altuna-Alvarez, Jéssica Rojas-Palomino, Andony Flores-Cerón, Citlaly Cando Narváez, Adrián Ruiz, Javier De la Peña Noya, Cristina Civantos, Amaia Gonzalez Magaña, María Queralt-Martín, Antonio Alcaraz, David Albesa-Jové, Patricia Bernal

This study identifies Tke5, a novel Pseudomonas putida toxin that depolarizes membranes and kills plant pathogens through a unique pore-forming mechanism.

Communications Biology · Mar 14, 2026Peer-reviewedMicrobiology

The cryo-EM structure of an adaptor-effector complex reveals the mechanism of a widespread pore-forming toxin family

Carmen Velázquez, Maialen Zabala-Zearreta, Carmen Paredes, Cristina Civantos, Jon Altuna-Alvarez, Patricia Bernal, David Albesa-Jové

The paper determines the cryo-EM structure of the Tap3-Tke5 complex, revealing the mechanism of adaptor-effector binding for a pore-forming toxin family.

The EMBO Journal · Jan 12, 2026Peer-reviewedMicrobiology

The Pseudomonas aeruginosa Tse4 toxin assembles ion-selective and voltage-sensitive ion channels to couple membrane depolarisation with K+ efflux

Jéssica Rojas-Palomino, Carmen Velázquez, Jon Altuna-Alvarez, Amaia Gonzalez Magaña, Maialen Zabala-Zearreta, Matthias Müller, María Queralt-Martín, Antonio Alcaraz, David Albesa-Jové

This study identifies Tse4 as a pore-forming toxin that forms ion-selective channels, linking membrane depolarisation to K+ efflux in competing bacteria.

PLoS Pathogens · Jun 4, 2025Peer-reviewedMicrobiology