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Journal of Virology, December 1998, p. 9738-9746, Vol. 72, No. 12
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Viral Glycoproteins Accumulate in Newly Formed Annulate Lamellae following Infection of Lymphoid Cells by Human Herpesvirus 6

Giorgia Cardinali,1 Massimo Gentile,2 Mara Cirone,1 Claudia Zompetta,1 Luigi Frati,1,3 Alberto Faggioni,1 and Maria Rosaria Torrisi1,*

Dipartimento di Medicina Sperimentale e Patologia1 and Istituto di Virologia,2 Università di Roma "La Sapienza," Rome, and Istituto Neurologico Mediterraneo "Neuromed," Pozzilli,3 Italy

Received 28 May 1998/Accepted 14 September 1998

Ultrastructural analysis of HSB-2 T-lymphoid cells and human cord blood mononuclear cells infected with human herpesvirus 6 revealed the presence, in the cell cytoplasm, of annulate lamellae (AL), which were absent in uninfected cells. Time course analysis of the appearance of AL following viral infection showed that no AL were visible within the first 72 h postinfection and that their formation correlated with the expression of the late viral glycoprotein gp116. The requirement of active viral replication for AL neoformation was further confirmed by experiments using inactivated virus or performed in presence of the viral DNA polymerase inhibitor phosphonoacetic acid. Both conventional electron microscopic examination and immunogold fracture labeling with anti-endoplasmic reticulum antibodies indicated a close relationship of AL with the endoplasmic reticulum and nuclear membranes. However, when the freeze-fractured cells were immunogold labeled with an anti-gp116 monoclonal antibody, AL membranes were densely labeled, whereas nuclear membranes and endoplasmic reticulum cisternae appeared virtually unlabeled, showing that viral envelope glycoproteins selectively accumulate in AL. In addition, gold labeling with Helix pomatia lectin and wheat germ agglutinin indicated that AL cisternae, similar to cis-Golgi membranes, contain intermediate, but not terminal, forms of glycoconjugates. Taken together, these results suggest that in this cell-virus system, AL function as a viral glycoprotein storage compartment and as a putative site of O-glycosylation.

* Corresponding author. Mailing address: Dip. Medicina Sperimentale e Patologia, Viale Regina Elena 324, 00161 Rome, Italy. Phone: 396-4468450. Fax: 396-4468450 or -4452850. E-mail: torrisi{at}axrma.uniroma1.it.

Journal of Virology, December 1998, p. 9738-9746, Vol. 72, No. 12
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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