Comparative analysis of the envelope glycoproteins of foamy viruses

Sun, Yan; Wen, Di-Di; Liu, Qingmei; Yi, Xin; Wang, Tingting; Wei, Lin-Lan; Li, Zhi; Liu, Wanhong; He, Xiaohua

doi:10.4149/av_2012_04_283

Cited by 7 publications

(14 citation statements)

References 22 publications

(27 reference statements)

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“…Th e data revealed that there were three structural regions within gp47 subunits: two long helix regions at N-terminus and C-terminus respectively, and a long region of extended β-strands and loops in the middle. Th e results were similar to the previous analyses using a diff erent secondary structure prediction program (Sun et al, 2012).…”

Section: Solvent Accessibility and Secondary Structure Of Fvs Gp47supporting

confidence: 88%

“…Based on this motif, most FVs were observed budding predominantly at endomembranes (e.g., ER, Golgi). When the dilysine motif was missing, EFV was budded at the plasma membrane (Muñoz-Barroso et al, 1999;Lindemann and Rethwilm, 2011;Sun et al, 2012).…”

Section: Membrane-spanning Domain (Msd) Of Fvs Gp47mentioning

confidence: 99%

“…Foamy viruses (FVs), also called spumaretroviruses, are complex retroviruses, which constitute the only genus in transport to the cell surface (Duda et al, 2004;Lindemann and Rethwilm, 2011;Sun et al, 2012). Proteolytic cleavage of SU and TM subunits is essential for viral infectivity (Duda et al, 2004;Lindemann and Rethwilm, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…Th e SU subunit mediates the binding of viruses to the cellular receptors, whereas the TM subunit gp47 is involved in the fusion of the lipid membranes between FVs and the target cells (Pietschmann et al, 2000;Peisajovich and Shai, 2003). Although some features of several FVs gp47 have been analyzed (Wang and Mulligan, 1999;Sun et al, 2012), the fusogenic TM subunits gp47 of all 15 available FV Envs are not fully dissected. In order to better understand the features of FVs gp47, we used computer-based methods to perform sequence analyses and predictions focused on all 15 available FV gp47 sequences.…”

Section: Introductionmentioning

confidence: 99%

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Structure of transmembrane subunits gp47 of the foamy virus envelope glycoproteins

Wang¹,

Zhang²,

Qm³

et al. 2016

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Summary. -Th e successful foamy viruses (FVs) infection includes at least two essential events, attachment to the cell surface and fusion of the viral envelope with the cell membrane. For the FVs, membrane fusion between virus and cell is mediated by envelope glycoprotein (Env) transmembrane (TM) subunit gp47. Compared with other retroviruses, FV TM subunit shares a similar but not identical structural characteristic. Th is paper focuses on in sillico analyses of all 15 available FV TM subunits gp47 based on their amino acid sequences. Th e hydrophobicity analysis revealed that the 15 FVs gp47 had two prominent hydrophobic regions, the N-terminal fusion peptide (FP) and the C-terminal region, which included a membrane-spanning domain (MSD) and a membrane proximal ectodomain region (MPER). In most FVs gp47, two heptad repeats, the coiled coils characterized by repetition of 7-amino acid-motif, were found to be correspondently located downstream of FP (named "N-HR") and the upstream of MPER (named "C-HR"). Furthermore, the solvent accessibility and secondary structure were predicted for all FVs gp47. Th ese observations suggested that FVs gp47 possessed several fusion domains, which were necessary in the process of lipid membrane fusion between FVs and the target cells.Keywords: foamy virus; envelope glycoprotein; transmembrane subunit gp47; hydrophobicity analysis; fusion domain * Corresponding authors. E-mail: lizhi@snnu.edu.cn; phone: +86-29-85310581. Abbreviations: BFV = bovine foamy virus; BSV = bovine syncytial virus; C-HR = C-terminal heptad repeat; EFV = equine foamy virus; Env = envelope glycoprotein; ERRS = endoplasmic reticulum retrieval signal; FFV = feline foamy virus; FP = fusion peptide; FSV = feline syncytial virus; FV(s) = foamy virus(es); HBV = hepatitis B virus; HIV = human immunodefi ciency virus; HR = heptad repeat; MMTV = mouse mammary tumor virus; MPER = Membrane proximal ectodomain region; MSD = membrane-spanning domain; N-HR = N-terminal heptad repeat; PFV = prototype foamy virus; SFV agm = african green monkey simian foamy virus; SFV cpz = chimpanzee foamy virus; SFV gor = gorilla foamy virus; SFV mac = macaque foamy virus; SFV mar = marmoset foamy virus; SFV spm = spider monkey foamy virus; SFV sqm = squirrel monkey foamy virus; SIV = simian immunodefi ciency virus; SloEFV = sloth endogenous foamy virus; SU = central surface domain; TM = transmembrane domain the subfamily Spumaretrovirinae of the family Retroviridae (Dirk and Axel, 2011). Till now, 15 FVs have been reported, which were derived from 6 non-primate and 9 primate hosts, including cat, horse, cattle, non-human primates and human. As indicated by their names, FVs possess highly fusogenic activity, which induces infected cells in vitro to form foamlike multinucleated cells. FVs can establish lifelong persistent infections in their hosts in the absence of any pathogenicity (Linial, 2000). As with other retroviruses, the FV envelope protein (Env) harbors essential features that allow viral adsorption, uptake and fusogenic release...

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Section: Solvent Accessibility and Secondary Structure Of Fvs Gp47supporting

confidence: 88%

Section: Membrane-spanning Domain (Msd) Of Fvs Gp47mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Structure of transmembrane subunits gp47 of the foamy virus envelope glycoproteins

Wang¹,

Zhang²,

Qm³

et al. 2016

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“…The number and position of N-glycosylation sites in FV Env differ from HIV-1 and MLV [32,33]. However, post-translational modifications such as the attachment of oligosaccharides to viral Env asparagine residues are not only known to promote proper folding or intracellular trafficking but also to ensure for specific interaction with receptor molecules (reviewed in [34]).…”

Section: Early Events In Virus-host Interaction: Attachment and Entrymentioning

confidence: 99%

Early Events in Foamy Virus—Host Interaction and Intracellular Trafficking

Berka

Hamann

Lindemann

2013

Viruses

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Here we review viral and cellular requirements for entry and intracellular trafficking of foamy viruses (FVs) resulting in integration of viral sequences into the host cell genome. The virus encoded glycoprotein harbors all essential viral determinants, which are involved in absorption to the host membrane and triggering the uptake of virus particles. However, only recently light was shed on some details of FV’s interaction with its host cell receptor(s). Latest studies indicate glycosaminoglycans of cellular proteoglycans, particularly heparan sulfate, to be of utmost importance. In a species-specific manner FVs encounter endogenous machineries of the target cell, which are in some cases exploited for fusion and further egress into the cytosol. Mostly triggered by pH-dependent endocytosis, viral and cellular membranes fuse and release naked FV capsids into the cytoplasm. Intact FV capsids are then shuttled along microtubules and are found to accumulate nearby the centrosome where they can remain in a latent state for extended time periods. Depending on the host cell cycle status, FV capsids finally disassemble and, by still poorly characterized mechanisms, the preintegration complex gets access to the host cell chromatin. Host cell mitosis finally allows for viral genome integration, ultimately starting a new round of viral replication.

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Microbial evolutionary reconstruction in the presence of mosaic sequences

Aiewsakun

2024

Phylogenomics

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Comparative analysis of the envelope glycoproteins of foamy viruses

Cited by 7 publications

References 22 publications

Structure of transmembrane subunits gp47 of the foamy virus envelope glycoproteins

Structure of transmembrane subunits gp47 of the foamy virus envelope glycoproteins

Early Events in Foamy Virus—Host Interaction and Intracellular Trafficking

Microbial evolutionary reconstruction in the presence of mosaic sequences

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