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The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins.

The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. Research Abstract Details 

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  • The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. Abstract Text:

    kelly elizabeth collerKelly Elizabeth Coller,joy i-hsuan leeJoy I-Hsuan Lee,aki uedaAki Ueda,gregory allan smithGregory Allan Smith,

    How alphaherpesvirus capsids acquire tegument proteins remains a key question in viral assembly. Using pseudorabies virus (PRV), we have previously shown that the 62 carboxy-terminal amino acids of the VP1/2 large tegument protein are essential for viral propagation and when transiently expressed as a fusion to green fluorescent protein relocalize to nuclear capsid assemblons following viral infection. Here, we show that localization of the VP1/2 capsid-binding domain (VP1/2cbd) into assemblons is conserved in herpes simplex virus type 1 (HSV-1) and that this recruitment is specifically on capsids. Using a mutant virus screen, we find that the protein product of the UL25 gene is essential for VP1/2cbd association with capsids. An interaction between UL25 and VP1/2 was corroborated by coimmunoprecipitation from cells transiently expressing either HSV-1 or PRV proteins. Taken together, these findings suggest that the essential function of the VP1/2 carboxy terminus is to anchor the VP1/2 tegument protein to capsids. Furthermore, UL25 encodes a multifunctional capsid protein involved in not only encapsidation, as previously described, but also tegumentation.

    The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. Publishing Authors By Initials

    ke collerKE Coller,ji leeJI Lee,a uedaA Ueda,ga smithGA Smith,

    For similar abstracts research abstracts see: abstracts research

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    The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of virology

    VOLUME: 81

    Page Numbers: 11790-7

    Journal Abbreviation: J. Virol.

    ISSN: 0022-538X

    DAY: 22

    MONTH: 08

    YEAR: 2007

    The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. Information

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    LANGUAGE: eng

    NlmUniqueID: 113724

    The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. Keywords Mesh Terms:

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    Grant and Affiliation Information for The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins.

    AFFILIATION: Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIAID

    GRANT: T32 AI 07476

    ACRONYM: AI

    MEDLINETA: J Virol

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