This page has only limited features, please log in for full access.

Unclaimed
Débora Marques Da Silveira E Santos
Institute for Interfacial Engineering and Plasma Technology IGVP, University of Stuttgart, 70174 Stuttgart, Germany

Basic Info

Basic Info is private.

Honors and Awards

The user has no records in this section


Career Timeline

The user has no records in this section.


Short Biography

Bachelors in Biological Sciences (Universidade Federal de Lavras, UFLA), Masters in Microbiology (Universidade Federal de Minas Gerais (UFMG) and PhD (Universität Stuttgart).

Following
Followers
Co Authors
The list of users this user is following is empty.
Following: 0 users

Feed

Journal article
Published: 05 August 2021 in Viruses
Reads 0
Downloads 0

Herpes simplex virus type 1 nucleocapsids are released from the host nucleus by a budding process through the nuclear envelope called nuclear egress. Two viral proteins, the integral membrane proteins pUL34 and pUL31, form the nuclear egress complex at the inner nuclear membrane, which is critical for this process. The nuclear import of both proteins ensues separately from each other: pUL31 is actively imported through the central pore channel, while pUL34 is transported along the peripheral pore membrane. With this study, we identified a functional bipartite NLS between residues 178 and 194 of pUL34. pUL34 lacking its NLS is mislocalized to the TGN but retargeted to the ER upon insertion of the authentic NLS or a mimic NLS, independent of the insertion site. If co-expressed with pUL31, either of the pUL34-NLS variants is efficiently, although not completely, targeted to the nuclear rim where co-localization with pUL31 and membrane budding seem to occur, comparable to the wild-type. The viral mutant HSV1(17+)Lox-UL34-NLS mt is modestly attenuated but viable and associated with localization of pUL34-NLS mt to both the nuclear periphery and cytoplasm. We propose that targeting of pUL34 to the INM is facilitated by, but not dependent on, the presence of an NLS, thereby supporting NEC formation and viral replication.

ACS Style

Christina Funk; Débora Marques Da Silveira E Santos; Melanie Ott; Verena Raschbichler; Susanne Bailer. The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex. Viruses 2021, 13, 1544 .

AMA Style

Christina Funk, Débora Marques Da Silveira E Santos, Melanie Ott, Verena Raschbichler, Susanne Bailer. The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex. Viruses. 2021; 13 (8):1544.

Chicago/Turabian Style

Christina Funk; Débora Marques Da Silveira E Santos; Melanie Ott; Verena Raschbichler; Susanne Bailer. 2021. "The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex." Viruses 13, no. 8: 1544.