1.G.15 The Autographa californica Nuclear Polyhedrosis Virus Major Envelope Glycoprotein GP64 (GP64) Family 

The envelope glycoprotein, GP64, of the baculovirus Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) is a class III viral fusion protein that mediates pH-triggered membrane fusion during virus entry. Viral fusion glycoproteins from many viruses contain a short region in the ectodomain and near the transmembrane domain, referred to as the pre-transmembrane (PTM) domain. In some cases, the PTM domain is rich in aromatic amino acids and plays an important role in membrane fusion. Although the 23-amino-acid (aa) PTM domain of AcMNPV GP64 lacks aromatic residues, it  plays a role in membrane fusion. Li and Blissard 2009 generated point mutations in the GP64 PTM domain, focusing on amino acid positions conserved between baculovirus GP64 and thogotovirus GP75 proteins, as well as hydrophobic and charged amino acids. For each PTM-modified construct, trimerization, cell surface localization, membrane merger, pore formation and membrane fusion activity were examined. Eight non clustered residues important for membrane fusion activity were identified. While charged residues were not critical, three hydrophobic amino acids (L465, L476, and L480) played a role in membrane fusion and appeared to be involved in formation of the fusion pore.  Several conserved residues (T463, G460, G462, and G474) were not required for membrane fusion but were important for budding and viral infectivity (Li and Blissard 2009).


 

References:

Apellaniz B., Huarte N., Largo E. and Nieva JL. (2014). The three lives of viral fusion peptides. Chem Phys Lipids. 181:40-55.

Li, Z. and G.W. Blissard. (2008). Functional analysis of the transmembrane (TM) domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: substitution of heterologous TM domains. J. Virol. 82: 3329-3341.

Li, Z. and G.W. Blissard. (2009). The pre-transmembrane domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein is critical for membrane fusion and virus infectivity. J. Virol. 83: 10993-11004.

Examples:

TC#NameOrganismal TypeExample
1.G.15.1.1

The major envelope protein, GP64, of 512 aas and 2 TMSs (N- and C-terminal).  The two fusion peptides of this type III bipartite system are residues 75 - 88 and 145 - 160 (Apellániz et al. 2014). The GP64 transmembrane domain is essential for GP64 trafficking, membrane fusion, virion budding, and virus infectivity but could be replaced only by transmembrane domains from related viral membrane proteins (Li and Blissard 2008).

Viruses (Baculoviridae)

GP64 of Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV).

 
1.G.15.1.2

Envelope glycoprotein of 520 aas and 2 TMSs, N- and C-terminal.

Thogotoviruses

GP of Dhori virus

 
1.G.15.1.3

Envelope glycoprotein (GP) of 519 aas and 2 TMSs.

Viruses

GP of Jos virus

 
1.G.15.1.4

Envelope glycoprotein (GP) of 512 aas and 2 TMSs.

Thogoto viruses

GP of Thogoto virus