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An Analysis of Herpesviral Effectors...

Daniel, Gina R.

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An Analysis of Herpesviral Effectors Involved in Genome Delivery, Mature Particle Formation, and Axonal Transport.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	An Analysis of Herpesviral Effectors Involved in Genome Delivery, Mature Particle Formation, and Axonal Transport./
作者:	Daniel, Gina R.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2017,
面頁冊數:	143 p.
附註:	Source: Dissertation Abstracts International, Volume: 78-10(E), Section: B.
Contained By:	Dissertation Abstracts International78-10B(E).
標題:	Virology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10269606
ISBN:	9781369817997

An Analysis of Herpesviral Effectors Involved in Genome Delivery, Mature Particle Formation, and Axonal Transport.
Daniel, Gina R.

An Analysis of Herpesviral Effectors Involved in Genome Delivery, Mature Particle Formation, and Axonal Transport. - Ann Arbor : ProQuest Dissertations & Theses, 2017 - 143 p.

Source: Dissertation Abstracts International, Volume: 78-10(E), Section: B.

Thesis (Ph.D.)--Northwestern University, 2017.

The herpes simplex virus (HSV) capsid has many critical roles during the infectious cycle. This protein shell protects the viral DNA genome, transmitting it from the periphery of the cell to the nucleus during entry, is involved in docking and genome release at the nuclear pore, and serves as a platform for tegument addition following replication. Two capsid-associated proteins bind nucleoporins, and are proposed to dock the capsid at the nuclear pore complex (NPC): capsid protein, pUL25, and tegument protein, pUL36. Study of these proteins, however, has been limited because both are essential during infection; they cannot be deleted without a loss of infectivity, making genetic approaches difficult. While early work documented that docking and uncoating are separable events, the molecular basis for the viral protein::NPC interaction and what regulates the genome to be released is still not understood. In this study, a virus encoding a novel pUL25 truncation mutant was generated that produces virions whose capsids enter cells, traffic and bind to the nuclear pore complex but fail to release their genomes efficiently. This is the first deletion mutant that successfully probes pUL25 function early in infection.

ISBN: 9781369817997Subjects--Topical Terms:

642304
Virology.

An Analysis of Herpesviral Effectors Involved in Genome Delivery, Mature Particle Formation, and Axonal Transport.
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245 1 3 $a An Analysis of Herpesviral Effectors Involved in Genome Delivery, Mature Particle Formation, and Axonal Transport.
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500 $a Source: Dissertation Abstracts International, Volume: 78-10(E), Section: B.
500 $a Adviser: Greg Smith.
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520 $a The herpes simplex virus (HSV) capsid has many critical roles during the infectious cycle. This protein shell protects the viral DNA genome, transmitting it from the periphery of the cell to the nucleus during entry, is involved in docking and genome release at the nuclear pore, and serves as a platform for tegument addition following replication. Two capsid-associated proteins bind nucleoporins, and are proposed to dock the capsid at the nuclear pore complex (NPC): capsid protein, pUL25, and tegument protein, pUL36. Study of these proteins, however, has been limited because both are essential during infection; they cannot be deleted without a loss of infectivity, making genetic approaches difficult. While early work documented that docking and uncoating are separable events, the molecular basis for the viral protein::NPC interaction and what regulates the genome to be released is still not understood. In this study, a virus encoding a novel pUL25 truncation mutant was generated that produces virions whose capsids enter cells, traffic and bind to the nuclear pore complex but fail to release their genomes efficiently. This is the first deletion mutant that successfully probes pUL25 function early in infection.
520 $a Following replication, the capsid shell acquires tegument proteins in a multi-step process. These proteins provides important functions for egress and subsequent entry into the next cell, but the mechanism of their acquisition and the position of their residency in the mature viral particle is unknown. In the alpha herpesviruses, only the C-terminus of the large tegument protein, pUL36, has been demonstrated to directly bind the capsid with a defined molecular interaction. However, other sites of capsid interaction have been proposed for pUL36 and other tegument proteins. This work investigates the binding interactions that anchor pUL36 on capsids, and the role of the protein in tethering the capsid to the broader tegument network. Because pUL36 performs multiple essential functions during infection, an approach was developed to selectively cleave pUL36 on the surface of capsids isolated from extracellular viral particles without disrupting the rest of the infectious cycle. Paired with an innovative on-particle fluorescence assay, we demonstrated that pUL36 is stably bound to the capsid through only its C-terminus. Additionally, neither pUL37 nor pUS3 are stably bound to the capsid, but are instead dependent on UL36 as a tether for capsid association.
520 $a Finally, a key step in the infectious cycle of neurotropic herpesviruses is the transmission of viral capsids to and from the peripheral nervous system. How capsids transmit from distant sites in host organisms is a key to how these viruses cause disease, but what role viral effectors play in such long-range motion is still an area of active investigation. Following reactivation from latency, virus particles leave the neuron cell body and proceed outwards down axons, a process called anterograde transport, which is the sum of at least two steps: sorting into the axon and subsequent transport. The virus-encoded protein pUS9 promotes axonal dissemination by sorting virus particles into axons, but whether it is also an effector of fast axonal transport within axons was unknown. We reported that while pUS9 increases the frequency of sorting of newly assembled pseudorabies virus particles to axons from the neural soma during egress, subsequent axonal transport of individual virus particles occurs with wild-type kinetics in the absence of the protein. We also examined the role of a related pseudorabies virus protein, pUL56, during neuronal infection. The findings indicated that pUL56 is a virulence factor that supports virus dissemination in vivo, yet along with pUS9, is dispensable for axonal transport.
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