Glycoproteins H and L of Marek's disease virus form a hetero-oligomer essential for translocation and cell surface expression.

Glycoproteins H and L form a hetero-oligomeric complex (gH-L) which plays an important role in virus entry to host cells and cell-to-cell infection in herpesviruses. Interaction of gH and gL is considered to be critical for the biological function of these two glycoproteins. To investigate the interaction of MDV gH and gL, both gH and gL were expressed in in vitro cell culture systems using indirect immunofluorescence assay with gH and gL antibodies. The results suggested that co-expression of gH and gL in the same cells are required and necessary for both gH and gL subcellular translocation and cell surface expression. gL expressed in recombinant fowlpox virus (rFPV) infected chicken embryo fibroblasts (CEF) was consistently secreted into the culture medium. The primary peptide of gL binds with that of gH in the cytosol or ER lumen. By binding with gH, gL could anchor itself on the cell surface allowing for surface expression and viral spread to uninfected cells. The binding domain of gH was mapped to the amino acids 451-659 (SacI-HindIII) fragment and was essential for gH-L complex formation.