{"ok":true,"nota":{"id":"5bc9f87558b49dab","slug":"una-proteina-del-vih-se-pega-a-una-molecula-humana-para-moverse-dentro-5bc9f8","titulo":"Una proteína del VIH se pega a una molécula humana para moverse dentro de la célula","resumen":"Investigadores estudiaron cómo se une la proteína MA del VIH con la calmodulina, una proteína humana que depende del calcio. Midieron la fuerza de esa unión y cómo cambia su forma al engancharse con fragmentos de la proteína viral.","fuente":"biorxiv","fuenteNombre":"bioRxiv · preprints","color":"#be2628","autor":"Saffarian Delkhosh, A., Ogunbowale, A., Hadadianpour, E., Mahmud, K. M., Borbat, P. P., Georgieva, E. R.","url":"https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1?rss=1","imagen":"/hoy/portada/5bc9f87558b49dab","tema":"ciencia","subtemas":["vih","proteinas virales","calmodulina","biologia molecular","inhibidores"],"entidades":["VIH-1","calmodulina"],"formato":"dato","entretenimiento":false,"pubTs":"2026-10-24T00:00:00.000Z","indexTs":"2026-10-24T15:51:15.058Z","hash":"78a2c2cf46fc5d99d12897b05099dc40d5b820fb7d9ff6ebcb1b6e001bd9a21e","tsa":{"time":"Oct 24 15:51:34 2026 GMT","provider":"freetsa.org","sobre":"sello"},"stats":{"views":0,"likes":0,"clicks":0,"dwell":0},"tipo":"normal","registro":"hallazgo","porQueImporta":"El trabajo muestra que el virus usa una pieza de la célula para llevar su material hasta la membrana, paso necesario para armar nuevas partículas virales. Entender esa unión ayuda a imaginar bloqueos futuros, aunque todavía falta mucho para cualquier tratamiento. Para un paciente o un investigador argentino, es un mapa más de cómo el VIH se apropia de nuestras propias defensas y herramientas.","quienFirma":"bioRxiv (preprint; institución principal no identificada en el resumen)","confianza":"preprint","consulta":null},"sello":{"hash":"78a2c2cf46fc5d99d12897b05099dc40d5b820fb7d9ff6ebcb1b6e001bd9a21e","sello":"6c59dfbe3a2850408913144fec1fd28f077bb04c24bd66e90e85fdb3e9a368d7","beacon":{"drand":{"cadena":"8990e7a9aaed2ffed73dbd7092123d6f289930540d7651336225dc172e51b2ce","ronda":6580868,"aleatorio":"d446ab85d2a54a02312d75dedfa22ede70a463319299c8faa87805acc3ce8c52","tiempo":"2026-10-24T15:51:00.000Z"},"nist":{"cadena":2,"pulso":1997627,"salida":"93705C7BB1B7D67A616D78DAD026F17972E793E92107F852A41532A7BAD3299306AA3A88C81A5D59313E87EB39370ED775F0CF6DA33958D42DA2288B1F85A13B","tiempo":"2026-10-24T15:50:00.000Z"},"noAntes":"2026-10-24T15:51:00.000Z"},"verificacion":{"drand":true,"nist":true},"tsa":{"time":"Oct 24 15:51:34 2026 GMT","provider":"freetsa.org","sobre":"sello"},"original":{"titulo":"Affinity and Conformations of Ca2+-Calmodulin Bound to Peptides Containing the Calmodulin-Binding Motif of HIV-1 Matrix Protein","descripcion":"Background: Protein-protein interactions enable viruses to adapt and replicate by modifying host factors. Thermodynamic characterization of viral-host complexes can reveal viral mechanisms, broader principles of protein interactions, and properties relevant to anti-HIV-1 inhibitor development. Here, we examine the binding of the HIV-1 matrix (MA) protein to host calmodulin (CaM). MA, the N-terminal domain of Gag (group-specific antigen), directs Gag to the plasma membrane for viral assembly and maturation and may recruit CaM to facilitate this trafficking. However, the MA-CaM interaction remains poorly characterized. MA contains a noncanonical N-terminal CaM-binding motif with hydrophobic re","pubDate":"2026-10-24","url":"https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1?rss=1"},"indexado":"2026-10-24T15:51:15.058Z"}}