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The major surface glycoprotein glycoprotein H (gH) of human herpesvirus 6 is produced on the surface of infected cells and plays a role in the attachment of virions to host cells. A second gene product, glycoprotein K (gK), is produced inside the cell as a nuclear transcript from a readthrough of the gH message. gH and gK are co-transcribed, and there is evidence that they are encoded on a single transcript. The two glycoproteins are synthesized with their respective short consensus sequences (SCR) at the amino terminus; there is evidence for the presence of a highly hydrophobic SCR in gH that is not seen in gK. The hydrophobic SCR may be responsible for the association of gH and gK. We have used a cell-free translation system to study the initiation of translation of human herpesvirus 6 transcripts. The viral transcript coding for gH or gK was translated in a cell-free system with any of the three initiation factors eIF4E, eIF4G, and eIF3. However, only full-length gH was initiated when the gH transcript was combined with eIF4G but only in the presence of eIF4E. Based on these results, we propose that there is a novel proline-rich transmembrane domain (PRTD) near the amino terminus of the gH protein. The length of this domain is much less than that of other transmembrane domains known for enveloped viruses. Furthermore, its presence is correlated with the use of eIF4E in the initiation of translation of the gH transcript in vitro.Babur Avenue

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