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- W2006065181 abstract "ABSTRACT The paramyxovirus entry machinery consists of two glycoproteins that tightly cooperate to achieve membrane fusion for cell entry: the tetrameric attachment protein (HN, H, or G, depending on the paramyxovirus genus) and the trimeric fusion protein (F). Here, we explore whether receptor-induced conformational changes within morbillivirus H proteins promote membrane fusion by a mechanism requiring the active destabilization of prefusion F or by the dissociation of prefusion F from intracellularly preformed glycoprotein complexes. To properly probe F conformations, we identified anti-F monoclonal antibodies (MAbs) that recognize conformation-dependent epitopes. Through heat treatment as a surrogate for H-mediated F triggering, we demonstrate with these MAbs that the morbillivirus F trimer contains a sufficiently high inherent activation energy barrier to maintain the metastable prefusion state even in the absence of H. This notion was further validated by exploring the conformational states of destabilized F mutants and stabilized soluble F variants combined with the use of a membrane fusion inhibitor (3g). Taken together, our findings reveal that the morbillivirus H protein must lower the activation energy barrier of metastable prefusion F for fusion triggering." @default.
- W2006065181 created "2016-06-24" @default.
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- W2006065181 date "2013-01-01" @default.
- W2006065181 modified "2023-09-25" @default.
- W2006065181 title "Mechanism for Active Membrane Fusion Triggering by Morbillivirus Attachment Protein" @default.
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- W2006065181 doi "https://doi.org/10.1128/jvi.01826-12" @default.
- W2006065181 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3536382" @default.
- W2006065181 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23077316" @default.
- W2006065181 hasPublicationYear "2013" @default.
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