Mutations that alter an Arg-Gly-Asp (RGD) sequence in the adenovirus type 2 penton base protein abolish its cell-rounding activity and delay virus reproduction in flat cells - PubMed (original) (raw)

Comparative Study

Mutations that alter an Arg-Gly-Asp (RGD) sequence in the adenovirus type 2 penton base protein abolish its cell-rounding activity and delay virus reproduction in flat cells

M Bai et al. J Virol. 1993 Sep.

Abstract

The adenovirus penton base protein has a cell rounding activity and may lyse endosomes during virus entry into the cytoplasm. We found that penton base that was expressed in Escherichia coli also caused cell rounding and that cells adhered to polystyrene wells that were coated with the protein. Mutant analysis showed that both properties required an Arg-Gly-Asp (RGD) sequence at residues 340 to 342 of penton base. In flat adherent cells, virus mutants with amino acid substitutions in the RGD sequence were delayed in virus reproduction and in the onset of viral DNA synthesis. In nonadherent or poorly spread cells, the kinetics of mutant virus reproduction were similar to those of wild-type adenovirus type 2. Expression of the mutant phenotype exclusively in the flat cells that we tested supports a model in which penton base interacts with an RGD-directed cell adhesion molecule during adenovirus uptake or uncoating.

PubMed Disclaimer

References

    1. Virology. 1975 Oct;67(2):415-26 - PubMed
    1. Science. 1992 Nov 6;258(5084):987-91 - PubMed
    1. J Mol Biol. 1978 Mar 25;120(1):97-120 - PubMed
    1. Annu Rev Biochem. 1978;47:251-76 - PubMed
    1. Virology. 1979 Jan 15;92(1):125-38 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources