ArticleThe Journal of biological chemistry2012
Critical role of leucine-valine change in distinct low pH requirements for membrane fusion between two related retrovirus envelopes.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- SERINC proteins potentiate antiviral type I IFN production and proinflammatory signaling pathways.Science signaling · 2021Article
- Enzootic nasal tumor virus type 2 envelope of goats acts as a retroviral oncogene in cell transformation.Virus genes · 2021Article
- Neutralizing antibody against SARS-CoV-2 spike in COVID-19 patients, health care workers, and convalescent plasma donors.JCI insight · 2020Article
- Investigating the genomic landscape of novel coronavirus (2019-nCoV) to identify non-synonymous mutations for use in diagnosis and drug design.Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology · 2020Article
- TIM-mediated inhibition of HIV-1 release is antagonized by Nef but potentiated by SERINC proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- IFITM Proteins Restrict HIV-1 Infection by Antagonizing the Envelope Glycoprotein.Cell reports · 2015Article
- A sorting signal suppresses IFITM1 restriction of viral entry.The Journal of biological chemistry · 2015Article
- TIM-family proteins inhibit HIV-1 release.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- IFITM proteins restrict viral membrane hemifusion.PLoS pathogens · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Many viruses use a pH-dependent pathway for fusion with host cell membrane, the mechanism of which is still poorly understood. Here we report that a subtle leucine (Leu)-valine (Val) change at position 501 in the envelope glycoproteins (Envs) of two related retroviruses, jaagsiekte sheep retrovirus (JSRV) and enzootic nasal tumor virus (ENTV), is responsible for their distinct low pH requirements for membrane fusion and infection. The Leu and Val residues are predicted to reside within the C-terminal heptad repeat (HR2) region of JSRV and ENTV Envs, particularly proximal to the hairpin turn of the putative six-helix bundle (6HB). Substitution of the JSRV Leu with a Val blocked the Env-mediated membrane fusion at pH 5.0, whereas replacement of the ENTV Val with a Leu rendered the ENTV Env capable of fusing at pH 5.0. A Leu-Val change has no apparent effect on the stability of native Env, but appears to stabilize an intermediate induced by receptor binding. These results are consistent with the existence of at least two metastable conformations of these viral glycoproteins, the native prefusion conformation and a receptor-induced metastable intermediate. Collectively, this work represents an interesting perhaps unique example whereby a simple Leu-Val change has critical impact on pH-dependent virus fusion and entry.
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