Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains.

Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains. Research Abstract Details 

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Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains. Abstract Text:

April A Saunders,Joey P C Ting,Jeffrey Meisner,Benjamin W Neuman,Mar Perez,Juan Carlos de la Torre,Michael J Buchmeier,

The stable signal peptide (SSP) of the lymphocytic choriomeningitis virus surface glycoprotein precursor has several unique characteristics. The SSP is unusually long, at 58 amino acids, and contains two hydrophobic domains, and its sequence is highly conserved among both Old and New World arenaviruses. To better understand the functions of the SSP, a panel of point and deletion mutants was created by in vitro mutagenesis to target the highly conserved elements within the SSP. We were also able to confirm critical residues required for separate SSP functions by trans-complementation. Using these approaches, it was possible to resolve functional domains of the SSP. In characterizing our SSP mutants, we discovered that the SSP is involved in several distinct functions within the viral life cycle, beyond translocation of the viral surface glycoprotein precursor into the endoplasmic reticulum lumen. The SSP is required for efficient glycoprotein expression, posttranslational maturation cleavage of GP1 and GP2 by SKI-1/S1P protease, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.

Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains. Publishing Authors By Initials

AA Saunders,JP Ting,J Meisner,BW Neuman,M Perez,JC de la Torre,MJ Buchmeier,

For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

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Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of virology

VOLUME: 81

Page Numbers: 5649-57

Journal Abbreviation: J. Virol.

ISSN: 0022-538X

DAY: 21

MONTH: 03

YEAR: 2007

Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains. Information

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LANGUAGE: eng

NlmUniqueID: 113724

Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains. Keywords Mesh Terms:

KEYWORDS: Viral Proteins

MESH TERMS: physiology

Chemical & Substance for Abstract: Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains. Information

Substance Name: Viral Proteins

Registry Number: 0

Grant and Affiliation Information for Mapping the landscape of the lymphocytic choriomeningitis virus stable signal peptide reveals novel functional domains.

AFFILIATION: The Scripps Research Institute, Molecular and Integrative Neurosciences Department, Mailstop SP30-2020, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.

Country: United States

AGENCY: United States NIAID

GRANT: AI-065359

ACRONYM: AI

MEDLINETA: J Virol

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