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Identification of a glycosylation site in the woodchuck hepatitis virus preS2 protein and its role in protein trafficking

O. Schildgen

Institut für Virologie, Universitätsklinikum Essen, Hufelandstraße 55, 45122 Essen, Germany

Correspondence
M. Lu
mengji.lu{at}uni-essen.de

The middle surface antigen (M-sAg) of hepadnaviruses is one of three envelope proteins that share a common C-terminal S domain. M-sAg contains the preS2 domain in addition to the S region. The preS2 region of woodchuck hepatitis virus (WHV) contains a potential glycosylation site Asn-Gln-Thr at amino acid (aa) positions 3–5. In this study, we mutated this site by site-directed mutagenesis and confirmed that glycosylation occurs here. In in vitro translation assays, the mutation Thr to Asn at aa 5 significantly impaired glycosylation of M-sAg. The mutated M-sAg formed abnormal clustered structures in transfected cells as determined by immunofluorescent staining. Confocal microscopic analysis showed that an enrichment of this glycosylation-deficient protein in the Golgi apparatus occurred, which is not typical for the wild-type protein. These results are consistent with earlier findings that incorrect glycosylation of viral proteins may interfere with virus assembly.

Present address: Institute for Medical Microbiology and Immunology, University of Bonn, Sigmund-Freud-Strasse 25, 53105 Bonn, Germany.