Abstract
Vaccinia virus (VACV) has two infectious forms called intracellular mature virus and extracellular enveloped virus (EEV). Two of the seven viral proteins in the EEV outer envelope, A33 and A34, are type II membrane glycoproteins that each interact with another EEV protein called B5; however, evidence for direct A33–A34 interaction is lacking. The localization and stability of A34 is affected by B5 and here data are presented showing that A34 is also affected by A33. In the absence of A33, just as without B5, the level, localization and glycosylation profile of A34 was altered. However, the glycosylation profile of A34 without A33 is different to that observed in the absence of B5, and A34 accumulates in the Golgi apparatus rather than in the endoplasmic reticulum. Thus, A34 requires more than one other EEV protein for its processing and cellular transport.
Highlights
Vaccinia virus (VACV) has two infectious forms called intracellular mature virus and extracellular enveloped virus (EEV)
The glycosylation profile of A34 without A33 is different to that observed in the absence of B5, and A34 accumulates in the Golgi apparatus rather than in the endoplasmic reticulum
Some intracellular mature virus (IMV) are transported via microtubules to the early endosomes or trans-Golgi network where they are wrapped by two cellular membranes containing several VACV proteins
Summary
Vaccinia virus (VACV) has two infectious forms called intracellular mature virus and extracellular enveloped virus (EEV). Both A34 (Rottger et al, 1999; Earley et al, 2008; Perdiguero et al, 2008; Roberts et al, 2009) and A33 (Perdiguero & Blasco, 2006) interact with the B5 protein, a 42 kDa type I glycoprotein present in the EEV membrane (Engelstad et al, 1992; Isaacs et al, 1992).
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