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

FEBS Lett. 2003 Jun 5;544(1-3):262-7. doi: 10.1016/s0014-5793(03)00516-7.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoviridae / metabolism
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Biochemistry / methods*
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism
  • Cellulose / chemistry
  • Drosophila Proteins*
  • Dyneins
  • Herpesviridae / genetics
  • Molecular Sequence Data
  • Peptide Biosynthesis
  • Peptides / chemistry
  • Protein Binding
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Retroviridae / metabolism
  • Sequence Homology, Amino Acid
  • Viral Proteins / chemistry*


  • Carrier Proteins
  • Drosophila Proteins
  • Peptides
  • Recombinant Proteins
  • Viral Proteins
  • Cellulose
  • Dyneins