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Gene Review:

GP - small secreted glycoprotein

Reston ebolavirus

Silvertown, J.D. et al., Marzi, A. et al., Kuhn, J.H. et al.

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Disease relevance of GP

In summary, we identified the level of GP incorporation into virions and signal peptide-controlled glycosylation of GP as determinants of attachment factor engagement [1].
LVs engineering luciferase pseudotyped with EboZ GP, but not with vesicular stomatitis virus glycoprotein resulted in successful LV transduction and transgene expression in C57BL/6 mouse lung by as early as d 4 [2].

High impact information on GP

The GP(1,2) envelope glycoproteins (GP) of filoviruses (marburg- and ebolaviruses) mediate cell-surface attachment, membrane fusion, and entry into permissive cells [3].
To provide the virions with enhanced tropism for the lung, LVs were pseudotyped with the Zaire strain of the Ebola virus glycoprotein (EboZ GP) and delivered by endotracheal intubation [2].

References

The signal peptide of the ebolavirus glycoprotein influences interaction with the cellular lectins DC-SIGN and DC-SIGNR. Marzi, A., Akhavan, A., Simmons, G., Gramberg, T., Hofmann, H., Bates, P., Lingappa, V.R., Pöhlmann, S. J. Virol. (2006) [Pubmed]
Functional expression of mouse relaxin and mouse relaxin-3 in the lung from an Ebola virus glycoprotein-pseudotyped lentivirus via tracheal delivery. Silvertown, J.D., Walia, J.S., Summerlee, A.J., Medin, J.A. Endocrinology (2006) [Pubmed]
Conserved receptor-binding domains of Lake Victoria marburgvirus and Zaire ebolavirus bind a common receptor. Kuhn, J.H., Radoshitzky, S.R., Guth, A.C., Warfield, K.L., Li, W., Vincent, M.J., Towner, J.S., Nichol, S.T., Bavari, S., Choe, H., Aman, M.J., Farzan, M. J. Biol. Chem. (2006) [Pubmed]

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