The Lipid Rafts in Caprine herpesvirus type 1: Preliminary Study on Viral Infection in vitro

Caprine herpesvirus type 1 (CpHV.1) is an alpha-herpesvirus of the Herpesviridae, a large and various family of DNA virus encased in an icosahedral capsid and in an envelope composed of about a dozen viral proteins and glycoproteins. All herpesviruses have a relatively broad host range for cultured cells, and consequently, each of these viruses can use multiple cell surface receptors for entry [1]. Herpesvirus employes five major viral glycoproteins, designed gB, gC, gD, gH,
and gLT as fusion machinery for virus entry, although additional receptors may also be required [1]. Cell entry receptors are required to trigger this fusion, but the molecule that herpesvirus glycoproteins associated with is not necessarily a protein [2]. Most, but not all herpesviruses, binding viral glycoproteins to glycosaminoglycans, usually heparan sulfate, on cell surface proteoglycans, that greatly increases the efficiency of viral entry, even if they may not be essential
for virus infection. Since it has been supposed that the interactions of one or more viral glycoproteins with cellular receptors could trigger envelope-membrane fusion or cell-to-cell fusion [3,4], the identification of the viral and the cellular domains involved in the interaction of virus and cell were the objective of several studies.