YLMY Tyrosine Residue within the Cytoplasmic Tail of Newcastle Disease Virus Fusion Protein Regulates Its Surface Expression to Modulate Viral Budding and Pathogenicity

Bu, Yawen; Feng, Delan; Sun, Lihua; Xue, Jia; Zhang, Guozhong

doi:10.1128/spectrum.02173-21

Cited by 6 publications

(5 citation statements)

References 46 publications

(47 reference statements)

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“…The CTs of envelope proteins contain one or more critical residues related to intracellular transport, viral assembly, and budding [ 31 , 32 ]. For NDV, according to sequence analysis of the F protein CTs, there are two typical transport motifs: a YXXφ motif and an LL motif, of which the YXXφ motif has been shown to affect the replication and pathogenicity of the virus [ 20 ]. In the present study, we evaluated the effect of LL-motif mutations on NDV syncytial formation, infectivity, pathogenicity, and protein transport.…”

Section: Discussionmentioning

confidence: 99%

“…DF-1 cells (a chicken embryo fibroblast cell line), and BSR T7/5 cells (a baby hamster kidney cell line stably expressing T7 RNA polymerase) were cultured in Dulbecco’s modified Eagle’s medium (DMEM; Gibco, Grand Island, NY, USA) with 10% fetal bovine serum (FBS; Gibco) and were maintained in DMEM with 2% FBS at 37 °C in a 5% CO 2 incubator (Thermo Forma, Marietta, OH, USA). The recombinant NDV strain rSG10* with artificially introduced Pme I and Sac II restriction sites was generated from rSG10 and kept in our laboratory [ 20 , 26 ]. The rSG10* was propagated in 9–11 day-old specific-pathogen-free (SPF) embryonated eggs by allantoic cavity inoculation.…”

Section: Methodsmentioning

confidence: 99%

“…The F protein CT of the NDV has typical transport motifs, including a tyrosine motif (YXXφ) at position 524-527 and a di-leucine motif (LL) at position 536-537 [19]. Recently, the YXXφ motif of the NDV has been shown to be related to the transport of F proteins to the cell membrane surface, which affects the viral pathogenicity [20]. The LL motif has been shown to affect internalization of the virus, targeting specific compartments within cells, and resulting in basolateral targeting in polarized epithelial cells [21][22][23].…”

Section: Introductionmentioning

confidence: 99%

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Mutagenesis of the di-leucine motif in the cytoplasmic tail of newcastle disease virus fusion protein modulates the viral fusion ability and pathogenesis

Tang

Huang

Yang

et al. 2023

Virol J

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Background Newcastle disease virus (NDV) is a highly infectious viral disease, which can affect chickens and many other kinds of birds. The main virulence factor of NDV, the fusion (F) protein, is located on the viral envelope and plays a major role in the virus’ ability to penetrate cells and cause host cell fusion during infection. Multiple highly conserved tyrosine and di-leucine (LL) motifs in the cytoplasmic tail (CT) of the virus may contribute to F protein functionality in the viral life cycle. Methods To examine the contribution of the LL motif in the biosynthesis, transport, and function of the F protein, we constructed and rescued a NDV mutant strain, rSG10*-F/L537A, with an L537A mutation using a reverse genetic system. Subsequently, we compared the differences in the syncytium formation ability, pathogenicity, and replication levels of wild-type rSG10* and the mutated strain. Results Compared with rSG10*, rSG10*-F/L537A had attenuated syncytial formation and pathogenicity, caused by a viral budding defect. Further studies showed that the LL-motif mutation did not affect the replication, transcription, or translation of the virus genome but affected the expression of the F protein at the cell surface. Conclusions We concluded that the LL motif in the NDV F CT affected the regulation of F protein expression at the cell surface, thus modulating the viral fusion ability and pathogenic phenotype.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Mutagenesis of the di-leucine motif in the cytoplasmic tail of newcastle disease virus fusion protein modulates the viral fusion ability and pathogenesis

Tang

Huang

Yang

et al. 2023

Virol J

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“…Corresponding cell lysates were prepared by using a ProteinExt mammalian total protein extraction kit (TransGen, Beijing, China). The virions/VLPs together with cell lysates were then analyzed via Western blotting as described previously ( 49 ).…”

Section: Methodsmentioning

confidence: 99%

Mutation of Phenylalanine 23 of Newcastle Disease Virus Matrix Protein Inhibits Virus Release by Disrupting the Interaction between the FPIV L-Domain and Charged Multivesicular Body Protein 4B

Xue

Feng

et al. 2023

Microbiol Spectr

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“…Specific Rab GTPases may also serve different roles in different cell types [47]. Importantly, they have also been shown to be required for basal trafficking of host and viral proteins [48][49][50][51][52][53][54]. Rab GTPases are engaged in the establishment and maintenance of cell polarization [55,56] and the specific subcellular localization of some Rab GTPases may differ in different cell types or tissues.…”

Section: Specific Rab Gtpases Are Important For Basal Trafficking Of ...mentioning

confidence: 99%

Variations in polarized trafficking of viral envelope proteins from insect-specific and insect-vectored viruses in insect midgut and salivary gland cells

Hodgson,

Chen,

Blissard

et al. 2024

Preprint

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Systemic viral infection of insects typically begins with primary infection of midgut epithelial cells (enterocytes) and subsequent transit of virus in an apical-to-basal orientation through the polarized enterocytes into the hemocoel. In the case of insect-vectored viruses, a similar yet oppositely oriented process (basal-to-apical virus transit) occurs upon secondary infection of salivary glands, and is necessary for virus transmission to non-insect hosts. To examine this inversely oriented virus transit in these polarized tissues, we assessed the intracellular trafficking of two model viral envelope proteins (baculovirus GP64 and vesicular stomatitis virus glycoprotein, VSV G) in the midgut and salivary gland cells of the model insect,Drosophila melanogaster. Using transgenicDrosophilafly lines that inducibly express either GP64 or VSV G, we found that both proteins were trafficked basally in midgut enterocytes. In salivary gland cells, VSV G was trafficked to apical membranes in most but not all cells, whereas GP64 was trafficked consistently to basal membranes. We further examined the mechanism of polarized trafficking in midgut and salivary gland epithelia and found that a cytoplasmic YxxØ motif in both VSV G and GP64 proteins is critical for basal trafficking of each envelope protein in midgut enterocytes, but dispensable for their trafficking in salivary gland epithelial cells. Using RNAi, we found that clathrin adapter protein complexes AP1 and AP3, as well as several Rab GTPases (Rab1, 4, 8, 10, 23, 30, and - 35), were involved in polarized VSV G trafficking in midgut enterocytes. Our results indicate that these viral envelope proteins encode the requisite information and require no other viral factors for appropriately polarized trafficking. In addition, they exploit tissue-specific differences in protein trafficking pathways to facilitate virus egress in the appropriate orientation for establishing systemic infections and vectoring infection to other hosts.Author SummaryViruses that use insects as hosts must navigate specific routes through the insect’s tissues to complete their life cycles. The routes may differ substantially depending on the life cycle of the virus. Some insect pathogenic viruses, such as baculoviruses, establish a systemic infection and this represents an endpoint in the infection cycle in the insect. In contrast, many insect-vectored viruses establish a systemic infection in the insect, but must also deliver infectious virus to the insect’s non-insect host. In both cases, the virus must first navigate through the midgut epithelium to establish a systemic infection, but insect-vectored viruses must also navigate through the salivary gland epithelium. Both midgut and salivary gland cells are polarized, and insect-vectored viruses appear to traffic in opposite directions in these two tissues. In this study, we asked whether two viral envelope proteins alone encode the signals necessary for polarized trafficking associated with their respective life cycles. Using two representative viral envelope proteins (VSV G and baculovirus GP64) andDrosophilaas a model insect to examine tissue-specific polarized trafficking of viral envelope proteins, we identified one of the virus-encoded signals and several host proteins associated with regulating the polarized trafficking in the midgut epithelium.

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YLMY Tyrosine Residue within the Cytoplasmic Tail of Newcastle Disease Virus Fusion Protein Regulates Its Surface Expression to Modulate Viral Budding and Pathogenicity

Cited by 6 publications

References 46 publications

Mutagenesis of the di-leucine motif in the cytoplasmic tail of newcastle disease virus fusion protein modulates the viral fusion ability and pathogenesis

Mutagenesis of the di-leucine motif in the cytoplasmic tail of newcastle disease virus fusion protein modulates the viral fusion ability and pathogenesis

Mutation of Phenylalanine 23 of Newcastle Disease Virus Matrix Protein Inhibits Virus Release by Disrupting the Interaction between the FPIV L-Domain and Charged Multivesicular Body Protein 4B

Variations in polarized trafficking of viral envelope proteins from insect-specific and insect-vectored viruses in insect midgut and salivary gland cells

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