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 human cytomegalovirus glycoprotein B (gB) was expressed. The secondary structure of the purified recombinant protein was analyzed by circular dichroism, and the quaternary structure was investigated by gel permeation chromatography, and electron microscopy. Our data indicate that the cytoplasmic gB domain contains alpha-helix structures and assembles into tetramers, suggesting that the authentic gB may represent a homotetramer.
Scheffczik
H
H
Institut für Virologie, Marburg, Germany.
Kraus
I
I
Kiermayer
S
S
Bogner
E
E
Holzenburg
A
A
Garten
W
W
Eickmann
M
M
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003587:Cytomegalovirus; D006801:Humans; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000648:ultrastructure; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure
D011993:Recombinant Fusion Proteins; D014759:Viral Envelope Proteins; C040495:glycoprotein B, Simplexvirus