The first step in virus replication is entry. The mechanisms used by poxviruses are complicated by the existence of two distinct infectious forms with different external membranes. Another complicating factor is the ability of vaccinia virus to enter cells through the plasma membrane and by endocytosis. We have identified a complex comprised of at least 11 proteins that are conserved in all poxviruses and required for entry of both infectious forms of virus. These proteins are conserved in all members of the poxvirus family, suggesting a common entry mechanism.

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29
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2016
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Moss, Bernard (2016) Membrane fusion during poxvirus entry. Semin Cell Dev Biol 60:89-96
Gjessing, Mona C; Yutin, Natalya; Tengs, Torstein et al. (2015) Salmon Gill Poxvirus, the Deepest Representative of the Chordopoxvirinae. J Virol 89:9348-67
Moss, Bernard (2015) Poxvirus membrane biogenesis. Virology 479-480:619-26
Laliberte, Jason P; Moss, Bernard (2014) A novel mode of poxvirus superinfection exclusion that prevents fusion of the lipid bilayers of viral and cellular membranes. J Virol 88:9751-68
Satheshkumar, P S; Chavre, James; Moss, Bernard (2013) Role of the vaccinia virus O3 protein in cell entry can be fulfilled by its Sequence flexible transmembrane domain. Virology 444:148-57
Helenius, Ari; Moss, Bernard (2013) Virus entry--an unwilling collaboration by the cell. Curr Opin Virol 3:1-2
Bengali, Zain; Satheshkumar, P S; Moss, Bernard (2012) Orthopoxvirus species and strain differences in cell entry. Virology 433:506-12
Moss, Bernard (2012) Poxvirus cell entry: how many proteins does it take? Viruses 4:688-707
Wolfe, Cindy L; Ojeda, Suany; Moss, Bernard (2012) Transcriptional repression and RNA silencing act synergistically to demonstrate the function of the eleventh component of the vaccinia virus entry-fusion complex. J Virol 86:293-301
Satheshkumar, P S; Moss, Bernard (2012) Sequence-divergent chordopoxvirus homologs of the o3 protein maintain functional interactions with components of the vaccinia virus entry-fusion complex. J Virol 86:1696-705

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