Effects of Truncation of the Carboxy Terminus of Pseudorabies Virus Glycoprotein B on Infectivity

doi:10.1128/JVI.74.15.7137-7145.2000

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Journal of Virology, August 2000, p. 7137-7145, Vol. 74, No. 15
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Effects of Truncation of the Carboxy Terminus of Pseudorabies Virus Glycoprotein B on Infectivity

Ralf Nixdorf, Barbara G. Klupp, Axel Karger, and Thomas C. Mettenleiter^*

Institute of Molecular Biology, Friedrich-Loeffler-Institutes, Federal Research Centre for Virus Diseases of Animals, D-17498 Insel Riems, Germany

Received 22 February 2000/Accepted 28 April 2000

Glycoproteins homologous to the type I membrane glycoprotein B (gB) of herpes simplex virus 1 (HSV-1) are the most highlyconserved glycoproteins within the family Herpesviridae and arepresent in members of each herpesvirus subfamily. In the alphaherpesviruspseudorabies virus (PrV), gB is required for entry into targetcells and for direct viral cell-to-cell spread. These processes,though related, appear to be distinct, and thus it was interestingto analyze whether they require different functions of gB. Tothis end, we established cell lines stably expressing differentcarboxy-terminally truncated versions of PrV gB by deleting either(i) one predicted intracytoplasmic $alpha$ -helical domain encompassingputative YQRL and dileucine internalization signals, (ii) twopredicted intracytoplasmic $alpha$ -helical domains, (iii) the completeintracytoplasmic domain, or (iv) the intracytoplasmic domain andthe transmembrane anchor region. Confocal laser scanning microscopyshowed that gB derivatives lacking at least the last 29 aminoacids (aa) localize close to the plasma membrane, while the full-lengthprotein accumulates in intracellular aggregations. Trans-complementationstudies with a gB-deleted PrV (PrV-gB) demonstrated that the 29-aa truncated form lacking the putativeinternalization signals and the C-terminal $alpha$ -helical domain (gB-008)was efficiently incorporated into PrV-gB virions and efficiently complemented infectivity and cell-to-cellspread. Moreover, gB-008 exhibited an enhanced fusogenic activity.In contrast, gB proteins lacking both $alpha$ -helical domains (gB-007),the complete intracytoplasmic domain, or the intracytoplasmicdomain and transmembrane anchor were only inefficiently or notat all incorporated into PrV-gB virions and did not complement infectivity. However, gB-007 wasable to mediate cell-to-cell spread of PrV-gB. Similar phenotypes were observed when virus recombinants expressinggB-008 or gB-007, respectively, instead of wild-type gB were isolatedand analyzed. Thus, our data show that internalization of gB isnot required for gB incorporation into virions nor for its functionin either entry or cell-to-cell spread. Moreover, they indicatedifferent requirements for gB in these membrane fusionprocesses.

^* Corresponding author. Mailing address: Federal Research Centre for Virus Diseases of Animals, D-17498 Insel Riems, Germany.Phone: 49-38351-7250. Fax: 49-38351-7151. E-mail: mettenleiter{at}rie.bfav.de.

Journal of Virology, August 2000, p. 7137-7145, Vol. 74, No. 15
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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