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Soluble Respiratory Syncytial Virus Fusion Protein in the Fully Cleaved, Pretriggered State is Triggered by Exposure to Low-Molarity Buffer

The respiratory syncytial virus (RSV) fusion (F) protein is a major target for vaccine and small-molecule antiviral drug development related to this virus. The authors of this article, published in the Journal of Virology, describe how they produced a fully cleaved paramyxoviral soluble F (sF) protein in its pretriggered form for the first time without the addition of a foreign trimerization domain. They also identified molarity of the solution containing the sF protein as an unexpected but critical component in the production of the pretriggered RSV sF protein and used it as a novel, surrogate method for triggering a viral fusion protein. The availability of pretriggered sF protein should enable studies of the RSV sF protein attachment and triggering mechanisms, which are important to the development of an RSV vaccine. ABSTRACT ONLY. (Learn how users in developing countries can gain free access to journal articles.)

Author: Chaiwatpongsakorn S, Epand RF, Collins PL, Epand RM, Peeples ME

Published: 2011

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(Located at jvi.asm.org)

Citation: Chaiwatpongsakorn S, Epand RF, Collins PL, Epand RM, Peeples ME. Soluble Respiratory Syncytial Virus Fusion Protein in the Fully Cleaved, Pretriggered State is Triggered by Exposure to Low-Molarity Buffer. Journal of Virology. 2011;85(8):3968-3977.

Resource types: Peer-reviewed journal

Diseases/vaccines: Respiratory syncytial virus (RSV)

Topics: Disease/vaccine specific information

Regions: Global