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Recognition of novel viral sequences that associate with the dynein light chain LC8 identified through a pepscan technique
Author(s) -
Martı́nez-Moreno Mónica,
Navarro-Lérida Inmaculada,
Roncal Fernando,
Albar Juan Pablo,
Alonso Covadonga,
Gavilanes Francisco,
Rodrı́guez-Crespo Ignacio
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00516-7
Subject(s) - dynein , immunoglobulin light chain , biology , virology , capsid , virus , microbiology and biotechnology , microtubule , genetics , antibody
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.