Wu P, Reed W M, Lee L F
Department of Pathology, Michigan State University, East Lansing, USA.
Arch Virol. 2001;146(5):983-92. doi: 10.1007/s007050170130.
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.
糖蛋白H和L形成一种异源寡聚体复合物（gH-L），它在疱疹病毒进入宿主细胞以及细胞间感染过程中发挥着重要作用。gH和gL的相互作用被认为对这两种糖蛋白的生物学功能至关重要。为了研究马立克氏病病毒（MDV）的gH和gL之间的相互作用，利用gH和gL抗体通过间接免疫荧光法在体外细胞培养系统中表达了gH和gL。结果表明，gH和gL在同一细胞中共表达对于gH和gL的亚细胞转运以及细胞表面表达都是必需的。在重组鸡痘病毒（rFPV）感染的鸡胚成纤维细胞（CEF）中表达的gL持续分泌到培养基中。gL的主要肽段在细胞质或内质网腔中与gH的肽段结合。通过与gH结合，gL能够将自身锚定在细胞表面，从而实现表面表达以及病毒向未感染细胞的传播。gH的结合结构域被定位到氨基酸451 - 659（SacI - HindIII）片段，并且对于gH-L复合物的形成至关重要。
