Recognition of novel viral sequences that associate with the dynein light chain LC8 identified through a pepscan technique

FEBS Letters

Gavilanes, Francisco²  Albar, Juan Pablo¹  Navarro-Lérida, Inmaculada²  Rodrı́guez-Crespo, Ignacio²  Alonso, Covadonga³  Roncal, Fernando¹  Martı́nez-Moreno, Mónica² 

[1] Departamento de Inmunologı́a y Oncologı́a, Centro Nacional de Biotecnologı́a, CSIC, Campus de la Universidad Autónoma, 28049 Madrid, Spain;Departamento de Bioquı́mica y Biologı́a Molecular, Facultad de Ciencias Quı́micas, Universidad Complutense, 28040 Madrid, Spain;Departamento de Biotecnologı́a, INIA, Ctra. de la Coruña Km 7, 28040 Madrid, Spain

关键词: Migration;    Microtubule;    Infection;    Dynein;    Pepscan;   

DOI  :  10.1016/S0014-5793(03)00516-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recent data from multiple laboratories indicate that upon infection, many different families of viruses hijack the dynein motor machinery and become transported in a retrograde manner towards the cell nucleus. In certain cases, one of the dynein light chains, LC8, is involved in this interaction. Using a library of overlapping dodecapeptides synthesized on a cellulose membrane (pepscan technique) we have analyzed the interaction of the dynein light chain LC8 with 17 polypeptides of viral origin. We demonstrate the strong binding of two herpesvirus polypeptides, the human adenovirus protease, vaccinia virus polymerase, human papillomavirus E4 protein, yam mosaic virus polyprotein, human respiratory syncytial virus attachment glycoprotein, human coxsackievirus capsid protein and the product of the AMV179 gene of an insect poxvirus to LC8. Our data corroborate the manipulation of the dynein macromolecular complex of the cell during viral infection and point towards the light chain LC8 as one of the most frequently used targets of virus manipulation.

【 授权许可】

Unknown