| Literature DB >> 26912609 |
Kathryn M Hastie1, Michelle Zandonatti1, Tong Liu2, Sheng Li2, Virgil L Woods2, Erica Ollmann Saphire3.
Abstract
UNLABELLED: The arenavirus matrix protein Z is highly multifunctional and occurs in both monomeric and oligomeric forms. The crystal structure of a dodecamer of Z from Lassa virus, presented here, illustrates a ring-like structure with a highly basic center. Mutagenesis demonstrates that the dimeric interface within the dodecamer and a Lys-Trp-Lys triad at the center of the ring are important for oligomerization. This structure provides an additional template to explore the many functions of Z. IMPORTANCE: The arenavirus Lassa virus causes hundreds of thousands of infections each year, many of which develop into fatal hemorrhagic fever. The arenavirus matrix protein Z is multifunctional, with at least four distinct roles. Z exists in both monomeric and oligomeric forms, each of which likely serves a specific function in the viral life cycle. Here we present the dodecameric form of Lassa virus Z and demonstrate that Z forms a "wreath" with a highly basic center. This structure and that of monomeric Z now provide a pair of critical templates by which the multiple roles of Z in the viral life cycle may be interpreted.Entities:
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Year: 2016 PMID: 26912609 PMCID: PMC4836352 DOI: 10.1128/JVI.02896-15
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103