Use of Lectins for Characterization of O-Linked Glycans of Herpes Simplex Virus Glycoproteins
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The existence of O
-linked glycans in viral glycoproteins was described in the early 1980s for enveloped viruses such as herpes simplex virus
type 1 (HSV-1), vaccinia virus, and mouse hepatitis virus (1
-4
). Glycoprotein C of HSV-1 (designated gC-1) was demonstrated to contain domains, in which numerous O
-linked glycans were concentrated to pronase-resistant clusters (5
-7
), thereby resembling the organization of mucins (8
). Thus glycoprotein, containing nine sites for N
-linked glycosylation in addition to the O
-linked glycans, is responsible for several important biological activities, including virus receptor binding (9
) and binding of factor C3b of the complement system (10
). The function of the O
-linked glycans in these activities remains unclear, but it is conceivable that their clustered appearance may cause gC-1
to adopt an extended fibrous conformation (11
), as originally demonstrated for the O
-linked glycans of mucins (8
). Use of lectins facilitates a structural analysis of clustered O
-linked glycans of gC-1 and it is possible that the methodology presented here may be of more general use, as similar arrangements
of clustered O
-linked glycans are present in an increasing number known glycoproteins of other enveloped viruses including herpes simplex
virus type 2 (12
,13
), Epstein-Barr virus (14
), and respiratory syncytial virus (15
).
