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Identification of the membrane association of BV/ODV E26 and the domains in BV/ODV E26 responsible for nuclear trafficking to intranuclear microvesicles

The baculovirus Autographa californica nucleopolyhedrovirus (AcNPV) has two
viral forms, budded virus (BV) and occlusion derived virus (ODV). The envelopment of
these two viral forms occurs at different locations: BV acquires envelopes at the plasma
membrane while ODV acquires envelopes in the nucleus. The two viral forms carry out
different functions in the viral life cycle. The purpose of this study is to investigate how
viral envelope proteins sort/traffic to the nucleus. Of particular interest is BV/ODV E26
(E26). E26 is an envelope protein of both BV and ODV (Braunagel and Summers,
1994); therefore it must traffic to the plasma membrane and the nucleus during infection.
Thus, E26 is a bi-directional trafficking protein, which interacts with membranes in both
locations of the cell. As such it has been shown that there are several immunoreactive
forms of E26 (Beniya, Braunagel, and Summers, 1998). The da26 gene produces at
least 2 protein products of 26 and 28 kDa with different functions respectively, which
correlate with localization, solubility, membrane association, and temporal requirements.
The 28 kDa form is likely a soluble protein that interacts with transcriptional activators
and DNA in the nucleus in the early stages of infection. A part of the 26 kDa population
is a membrane bound form interacting with an integral membrane protein in the ER and
likely functions as an INM sorting factor. The 26 kDa membrane bond form is also
found in the inner nuclear membrane, intra-nuclear microvesicles, ODV envelopes, and
ODV in the nucleus.

Identiferoai:union.ndltd.org:tamu.edu/oai:repository.tamu.edu:1969.1/4924
Date25 April 2007
CreatorsBurks, Jared K.
ContributorsSummers, Max D.
PublisherTexas A&M University
Source SetsTexas A and M University
Languageen_US
Detected LanguageEnglish
TypeBook, Thesis, Electronic Dissertation, text
Format16475435 bytes, electronic, application/pdf, born digital

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