Role of N-linked glycosylation of the human parainfluenza virus type 3 hemagglutinin-neuraminidase protein

Chu, Fulu; Wen, Hao; Hou, Guihua; Lin, Bingliang; Song, Yue; Ren, Guijie; Sun, Chengxi; Li, Zhenmei; Wang, Zhiyu

doi:10.1016/j.virusres.2013.03.012

Cited by 23 publications

(20 citation statements)

References 47 publications

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“…Regardless of whether Asn189 and/or Asn619 are glycosylated, it is highly unusual for a paramyxoviral attachment glycoprotein to lack N -linked glycans throughout the β-propeller domain proper, given their crucial role in virulence, host immune evasion, glycoprotein folding and assembly, and the activation of fusion cascades363738474849. Therefore, the absence of N -linked glycans in the β-propeller domain appears to be a distinguishing feature of MojV-G, differentiating it not only from classical HNV-Gs182436373839 but also HN1920212223 and H3546 glycoproteins and the glycoproteins of the recently emerged feline morbillivirus404142, Mossman43, Nariva44 and Salem45 viruses.…”

Section: Resultsmentioning

confidence: 99%

Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses

et al. 2017

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In 2012, cases of lethal pneumonia among Chinese miners prompted the isolation of a rat-borne henipavirus (HNV), Mòjiāng virus (MojV). Although MojV is genetically related to highly pathogenic bat-borne henipaviruses, the absence of a conserved ephrin receptor-binding motif in the MojV attachment glycoprotein (MojV-G) indicates a differing host-cell recognition mechanism. Here we find that MojV-G displays a six-bladed β-propeller fold bearing limited similarity to known paramyxoviral attachment glycoproteins, in particular at host receptor-binding surfaces. We confirm the inability of MojV-G to interact with known paramyxoviral receptors in vitro, indicating an independence from well-characterized ephrinB2/B3, sialic acid and CD150-mediated entry pathways. Furthermore, we find that MojV-G is antigenically distinct, indicating that MojV would less likely be detected in existing large-scale serological screening studies focused on well-established HNVs. Altogether, these data indicate a unique host-cell entry pathway for this emerging and potentially pathogenic HNV.

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Section: Resultsmentioning

confidence: 99%

Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses

et al. 2017

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“…Site-directed mutagenesis was performed according to protocols previously described [22]. The hPIV-3 F recombinant plasmid vector was used as the template in each PCR mutagenesis to generate alanine codon substitutions.…”

Section: Methodsmentioning

confidence: 99%

“…The content-mixing assay, based on the cytoplasmic activation of the reporter gene β-galactosidase, was essentially performed as previously described [22], with slight modifications. One population of BHK-21 cells was infected with the recombinant vTF7-3 vaccinia virus as described above and cotransfected with the desired F and hPIV-3 HN genes.…”

Section: Methodsmentioning

confidence: 99%

“…The dye transfer assay was performed as previously described [22,25]. Fresh human RBC were washed, resuspended in cold PBS (1% hematocrit), and incubated with 15 μl octadecyl rhodamine B (R18; Invitrogen) (1 mg/ml in ethanol) for 30 min at room temperature in the dark.…”

Section: Methodsmentioning

confidence: 99%

“…The abilities of hPIV-3 wt or mutated F proteins to interact with hPIV-3 HN proteins at the surface of transfected BHK-21 cells were assayed using a modification of a coimmunoprecipitation assay as previously described [22,28,29]. BHK-21 monolayers were grown in 6-well plates (∼80% confluence) and transfected with cDNA encoding the HN protein as well as wt or mutated F proteins as described above.…”

Section: Methodsmentioning

confidence: 99%

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Mutations in the Leucine Zipper-Like Motif of the Human Parainfluenza Virus 3 Fusion Protein Impair Fusion Activity

Xie¹,

Wen²,

Chu

et al. 2015

Intervirology

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Objective: To investigate the effect of the leucine zipper-like motif between HRA and HRB of the human parainfluenza virus 3 fusion protein on fusion activity. Methods: Site-directed mutagenesis was utilized to substitute the heptadic residues at 257, 264, 271, 278, 285, 292, and 299 in this motif with alanine. Additionally, 3middle heptadic leucine residues at 271, 278, and 285 were replaced with alanine singly or in combination. A vaccinia virus-T7 RNA polymerase transient expression system was employed to express the wild-type or mutated fusion (F) proteins. Three different types of membrane fusion assays were performed to analyze the fusogenic activity, fluorescence-activated cell sorting (FACS) analysis was executed to examine the cell surface expression level, and a coimmunoprecipitation assay was conducted to probe the hemagglutinin-neuraminidase (HN)-F interaction at the cell surface. Results: All of the substitutions in this motif exhibited diminished or even lost fusion activity in all stages of fusion, although they all had no effect on cell surface expression. In the coimmunoprecipitation assay, all mutants resulted in decreased detection of the HN-F complexes compared with that of the wild-type F protein. Conclusions: This motif has an important influence on fusion activity, and its integrality is indispensable for membrane fusion.

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Prenylation of viral proteins by enzymes of the host: Virus‐driven rationale for therapy with statins and FT/GGT1 inhibitors

et al. 2017

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Intracellular bacteria were recently shown to employ eukaryotic prenylation system for modifying activity and ensuring proper intracellular localization of their own proteins. Following the same logic, the proteins of viruses may also serve as prenylation substrates. Using extensively validated high‐confidence prenylation predictions by PrePS with a cut‐off for experimentally confirmed farnesylation of hepatitis delta virus antigen, we compiled in silico evidence for several new prenylation candidates, including IRL9 (CMV) and few other proteins encoded by Herpesviridae, Nef (HIV‐1), E1A (human adenovirus 1), NS5A (HCV), PB2 (influenza), HN (human parainfluenza virus 3), L83L (African swine fever), MC155R (molluscum contagiosum virus), other Poxviridae proteins, and some bacteriophages of human associated bacteria. If confirmed experimentally, these findings may aid in dissection of molecular functions of uncharacterized viral proteins and provide a novel rationale for statin and FT/GGT1‐based inhibition of viral infections. Prenylation of bacteriophage proteins may aid in moderation of microbial infections. Also see the video abstract here: https://youtu.be/0qVW3ym1R1g

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Role of N-linked glycosylation of the human parainfluenza virus type 3 hemagglutinin-neuraminidase protein

Cited by 23 publications

References 47 publications

Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses

Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses

Mutations in the Leucine Zipper-Like Motif of the Human Parainfluenza Virus 3 Fusion Protein Impair Fusion Activity

Prenylation of viral proteins by enzymes of the host: Virus‐driven rationale for therapy with statins and FT/GGT1 inhibitors

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