Multimerization potential of the cytoplasmic domain of the human cytomegalovirus glycoprotein B

In the present study the coding sequence of the cytoplasmic tail of the hum an cytomegalovirus glycoprotein B (gB) was expressed. The secondary structu re of the purified recombinant protein was analyzed by circular dichroism, and the quaternary structure was investigated by gel permeation chromatogra phy, and electron microscopy. Our data indicate that the cytoplasmic gB dom ain contains a-helix structures and assembles into tetramers, suggesting th at the authentic gB may represent a homotetramer. (C) 2001 Federation of Eu ropean Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.