Open AccessAdenovirus Assembly
Author(s) -
Boulanger Pierre A.,
Puvion Francine
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03433.x
Subject(s) - trimer , capsomere , capsid , glutaraldehyde , dimer , random hexamer , protein quaternary structure , monomer , mastadenovirus , crystallography , chemistry , adenoviridae , biology , virology , virus , biochemistry , protein subunit , polymer , recombinant dna , chromatography , organic chemistry , gene
Cross‐linking of adenovirus hexon capsomers by glutaraldehyde in vitro has been studied as a chemical probe for quaternary structure of hexon protein and virus capsid assembly. Glutaraldehyde cross‐linking of hexons gave rise to three main oligomeric species, trimer, hexamer and nonamer, as analyzed on dodecylsulfate‐acrylamide gels, which corresponded in terms of complete hexon capsomers, to single hexon capsomer, capsomer dimer and trimer. The major species was found to be the trimer of the hexon polypeptide unit, viz. the intramolecularly cross‐linked hexon capsomer. This result indicated that intraoligomeric cross‐linking took place more readily than the interoligomeric reactions. As shown by electron microscopy the spatial arrangement of the cross‐linked hexon capsomer trimer was reminiscent of the structure of groups of three hexons clustered with 3‐fold symmetry to form the groups of nine hexons isolated from disrupted adenovirus capsid.