Literature References | 1. BLASCO, R. AND MOSS, B.
Extracellular vaccinia virus formation and cell-to-cell virus transmission
are prevented by deletion of the gene encoding the 37,000-dalton outer
envelope protein.
J.VIROL. 65 5910-5920 (1991).
2. DOMS, R.W., BLUMENTHAL, R. AND MOSS, B.
Fusion of intra- and extracellular forms of vaccinia virus with the cell
membrane.
J.VIROL. 64 4884-4892 (1990).
3. DEMKOWICZ, W.A., MAA, J.S. AND ESTEBAN, M.
Identification and characterization of vaccinia virus genes encoding
proteins that are highly antigenic in animals and are immunodominant in
vaccinated humans.
J.VIROL. 66 386-398 (1992).
4. VAZQUEZ, M.I., RIVAS, G., CREGUT, D., SERRANO, L. AND ESTEBAN, M.
The vaccinia virus 14-kilodalton (A27L) fusion protein forms a triple
coiled-coil structure and interacts with the 21-kilodalton (A17L) virus
membrane protein through a C-terminal alpha-helix.
J.VIROL. 72 10126-10137 (1997).
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Documentation | Viral fusion proteins have multiple roles in the biology of viruses. The
fusion protein is required for formation and release of the extracellular
enveloped virus and virus spread [1]. The protein is also involved in the
entry process, acting in virus-to-cell and cell-to-cell fusions [2]. An
important property of the protein is its ability to confer protection
to animals immunised with the purified protein following challenge with
lethal doses of vaccinia virus [3].
Sequence analysis studies on the vaccinia fusion protein reveal the
existence of four regions: an apparent structureless N-terminal region,
followed by a helical region from residues 29-37, a triple coiled region
from residues 44-72, and a leucine zipper motif at the C-terminus [4].
VIRALFUSION is a 3-element fingerprint that provides a signature for the
viral fusion proteins. The fingerprint was derived from an initial alignment
of 13 sequences: the motifs were drawn from the conserved C-terminal region.
Two iterations on SPTR40_20f were required to reach convergence, at which
point a true set comprising 31 sequences was identified.
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