African swine fever virus protein p54 interacts with the microtubular motor complex through direct binding to light-chain dynein
| Autor: | Ignacio Rodríguez-Crespo, Covadonga Alonso, Carmen Cantó, James E. Miskin, Patricia Fernandez-Zapatero, Linda K. Dixon, José M. Escribano, Bruno Hernáez, Lourdes Soto |
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| Jazyk: | angličtina |
| Rok vydání: | 2001 |
| Předmět: |
viruses
Immunology Dynein macromolecular substances Virus Replication Microbiology African swine fever virus Virus VP40 Microtubule Virology Chlorocebus aethiops Viral structural protein Animals Drosophila Proteins Amino Acid Sequence Vero Cells Viral Structural Proteins biology Dyneins DNA virus Dynactin Complex biology.organism_classification African Swine Fever Virus Virus-Cell Interactions Insect Science Dynactin Protein Tyrosine Phosphatases Vanadates Carrier Proteins Microtubule-Associated Proteins Microtubule-Organizing Center Protein Binding |
| Zdroj: | Repositorio de Resultados de Investigación del INIA INIA: Repositorio de Resultados de Investigación del INIA Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria INIA |
| Popis: | Dynein is a minus-end-directed microtubule-associated motor protein involved in cargo transport in the cytoplasm. African swine fever virus (ASFV), a large DNA virus, hijacks the microtubule motor complex cellular transport machinery during virus infection of the cell through direct binding of virus protein p54 to the light chain of cytoplasmic dynein (LC8). Interaction of p54 and LC8 occurs both in vitro and in cells, and the two proteins colocalize at the microtubular organizing center during viral infection. p50/dynamitin, a dominant-negative inhibitor of dynein-dynactin function, impeded ASFV infection, suggesting an essential role for dynein during virus infection. A 13-amino-acid domain of p54 was sufficient for binding to LC8, an SQT motif within this domain being critical for this binding. Direct binding of a viral structural protein to LC8, a small molecule of the dynein motor complex, could constitute a molecular mechanism for microtubule-mediated virus transport. |
| Databáze: | OpenAIRE |
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