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Journal of Virology, February 2004, p. 1540-1551, Vol. 78, No. 3
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.3.1540-1551.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Effects of Mutations in the Cytoplasmic Domain of Herpes Simplex Virus Type 1 Glycoprotein B on Intracellular Transport and Infectivity

Igor Beitia Ortiz de Zarate, Karin Kaelin, and Flore Rozenberg*

UPRES EA 3622, Faculté Cochin, Université Paris V, and INSERM U 567, CNRS UMR 8104, IFR 116, 75014 Paris, France

Received 24 July 2003/ Accepted 15 October 2003

Herpes simplex virus type 1 (HSV-1) is a human pathogen of the alphaherpesvirus family which infects and spreads in the nervous system. Glycoproteins play a key role in the process of assembly and maturation of herpesviruses, which is essential for neuroinvasion and transneuronal spread. Glycoprotein B (gB) is a main component of the HSV-1 envelope and is necessary for the production of infectious particles. The cytoplasmic domain of gB, the longest one among HSV-1 glycoproteins, contains several highly conserved peptide sequences homologous to motifs involved in intracellular sorting. To determine the specific roles of these motifs in processing, subcellular localization, and the capacity of HSV-1 gB to complement a gB-null virus, we generated truncated or point mutated forms of a green fluorescent protein (GFP)-tagged gB. GFP-gB with a deletion in the acidic cluster DGDADEDDL (amino acids [aa] 896 to 904) behaved the same as the parental form. Deletion or disruption of the YTQV motif (aa 889 to 892) abolished internalization and reduced complementation by 60%. Disruption of the LL motif (aa 871 to 872) impaired the return of the protein to the trans-Golgi network (TGN) while enhancing its recycling to the plasma membrane. Truncations from residue E 857 abolished transport and processing of the truncated proteins, which had null complementation activity, through the Golgi complex. Altogether, our results favor a model in which HSV-1 gets its final envelope in the TGN, and they suggest that endocytosis, albeit not necessary, might play a role in infectivity.

* Corresponding author. Mailing address: UPRES EA 3622, BÂtiment Gustave Roussy, Porte 636, 27, rue du Faubourg Saint Jacques, 75014 Paris, France. Phone: 33 1 44 41 23 48. Fax: 33 1 40 51 65 70. E-mail: flore.rozenberg{at}cochin.univ-paris5.fr.

Journal of Virology, February 2004, p. 1540-1551, Vol. 78, No. 3
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.3.1540-1551.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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