Detection and initial characterization of protein entities consisting of the HIV glycoprotein cytoplasmic C-terminal domain alone
Employing antibodies against the cytoplasmic tail of the HIV-1 glycoprotein (Env-CT), in addition to gp160/gp41, we have identified several novel small Env proteins (<25kD) in HIV-1 transfected and infected cells. Mass spectrometric and mutational analyses show that two mechanisms contribute to t...
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| Main Authors: | , , , |
|---|---|
| Format: | Article (Journal) |
| Language: | English |
| Published: |
3 April 2013
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| In: |
Virology
Year: 2013, Volume: 441, Issue: 1, Pages: 85-94 |
| ISSN: | 1096-0341 |
| DOI: | 10.1016/j.virol.2013.03.009 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.virol.2013.03.009 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0042682213001499 |
| Author Notes: | Tanya Pfeiffer, Thomas Ruppert, Heiner Schaal, Valerie Bosch |
MARC
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| 520 | |a Employing antibodies against the cytoplasmic tail of the HIV-1 glycoprotein (Env-CT), in addition to gp160/gp41, we have identified several novel small Env proteins (<25kD) in HIV-1 transfected and infected cells. Mass spectrometric and mutational analyses show that two mechanisms contribute to their generation. Thus the protein, designated Tr-Env-CT (for truncated Env-CT), consists of the C-terminal 139 amino acids (aa) of Env (aa 718-856) with the N-terminal Q718 modified to pyroglutamic acid. It is likely derived from full-length Env protein by proteolytic processing. A further heterogeneous set of slightly larger proteins, termed Env-CT* species, are rather derived from spliced mRNAs containing only those Env C-terminal residues (aa 719-856) which overlap with the second tat and rev coding exons. They are N-terminally extended in the same reading frame. It is conceivable that essential Env-CT functions may be fulfilled by these novel species rather than by the full-length glycoprotein itself. | ||
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