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Figure 1.

The structure of insertion sites of the H9N2-AIV-NA and NDV-F gene under the control of the bi-directional promoters on MZC13NA/F genome (GX0101/Δmeq/Kan/gpt/NA/F).

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Figure 1 Expand

Table 1.

List of primers used for construction of different recombinant plasmids.

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Figure 2.

Demonstration of H9N2-NA or NDV-F expressing cells in IFA with monospecific sera in CEF transfected with different plasmids or their combinations (×200).

(a) IFA with mouse anti-NA polyclonal serum to NA in CEF co-transfected with pPpp38-NA and pBud-pp38-pp24; (b) IFA with chicken polyclonal anti-F serum to F in CEF co-transfected with pP1.8kb-F and pBud-pp38-pp24; (c) IFA with mouse anti-NA polyclonal serum and chicken polyclonal anti-F serum to NA and F in CEF co-transfected with pPpp38-NA/1.8kb-F and pBud-pp38-pp24; (d) Detection of NA and F in CEF transfected with pPpp38-NA/1.8kb-F only.

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Figure 2 Expand

Figure 3.

Demonstration of H9N2-NA or NDV-F expressing cells in IFA with specific antibodies in GX0101-CEF transfected with different plasmids (×200).

(a) IFA with mouse anti-NA polyclonal serum to NA in GX0101-CEF transfected with pPpp38-NA; (b) IFA with chicken polyclonal anti-F serum to F in GX0101-CEF transfected with pP1.8kb-F; (c) IFA with mouse anti-NA polyclonal serum to NA in GX0101-CEF transfected with pPpp38-NA/1.8kb-F; (d) IFA with chicken polyclonal anti-F serum to F in GX0101-CEF transfected with pPpp38-NA/1.8kb-F; (e,f) IFA with mouse anti-NA polyclonal antibody against NA in GX0101-CEF; (g,h) IFA with chicken polyclonal anti-F serum against F protein in GX0101-CEF.

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Figure 3 Expand

Table 2.

Comparison of the expression of NDV-F or AIV-NA in the presence or absence of pp38/pp24 dimers via IFA.

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Figure 4.

Southern blot of PCR products amplified from GX0101 and its recombinant genomes to demonstrate foreign genes.

(a) Amplification of MZC13NA/F and GX0101 US2 gene by PCR. The US2 gene was amplified from DNAs prepared from the MZC13NA/F-infected CEF cells, or GX0101-infected CEF cells. The reaction products were submitted to agarose gel electrophoresis and stained with ethidium bromide; (b) The same DNAs and the NA ORF amplified from DNAs prepared from MZC13NA/F-infected CEF cells were processed for Southern blot analysis with the NA probe; (c) The same DNAs and the F ORF amplified from DNAs prepared from MZC13NA/F-infected CEF cells were processed for Southern blot analysis with the F probe.

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Figure 5.

Growth curves (one-step growth kinetics) of GX0101 and its recombinant MZC13NA/F.

After inoculation of CEFs with 100-infection until maximal titers were reached. The data of the growth curve of MZC13NA/F were cited from reference [40]. The results represent the mean±standard deviations of three independent replicates.

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Figure 6.

Plaque sizes of Meq-deleted MDV GX0101 and its recombinant MZC13NA/F in infected CEF cells at second passage (×200).

The mouse anti-pp38 monoclonal antibody H19 bound to the MZC13NA/F (a) or its parent GX0101 (b) infected CEF cells by IFA, or to the CEF cells (c). MZC13NA/F plaque size was similar to GX0101 at some level, 96 hours post-infection showing bulging and aggregation of rounded cells.

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Figure 7.

Standard curve of NA, F and pp38 assay.

Copy number for the plasmid pMD18-NA, -F or -pp38 were respectively determined spectrophotometrically and diluted serially from 109 copies/µL to 101 copies/µL for use as standard controls. Standard curve (y = 39.369−3.122x, y = 31.533−3.332x and y = 37.614−3.299x) for NA, F and pp38 genes quantification (R2 = 0.9918, 0.9906 and 0.9978; Efficiency = 100±1.5%) was analyzed with the GraphPad Software 5.0®. The concentration refers to the template copy number per reaction.

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Table 3.

The absolute quantification (AQ) values of cDNAs of different genes (copies/ul).

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Table 3 Expand

Figure 8.

Demonstration of H9N2-NA or NDV-F expressing cells in IFA with monospecific sera in the MZC13NA/F-infected CEF (×200).

(a) Distribution of NA was detected by staining with mouse anti-NA polyclonal antibody and Fluorescein Isothiocyanate-labelled anti-mouse secondary antibody (green fluorescence); (b) Distribution of F expression was detected using NDV virus-specific chicken antiserum and phycoerythrin-conjugated goat anti-chicken IgG (red fluorescence); (c) The merge including the visualization of red and green images showed that the co-expression proteins were visible in the cytoplasm or on the cell surface; (d) Photo was taken under regular light from the same plaque in the same visual field.

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Figure 9.

Western blot analyses of recombinant NA and F proteins co-expressed in MZC13NA/F infected CEF cells.

CEF lysates prepared from the MZC13NA/F-infected CEF cells were subjected to SDS-polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane. The blotted membrane was blocked and reacted with mouse anti-pp38 monoclonal antibodies H19, mouse anti-NA polyclonal serum and chicken antiserum raised against NDV followed by HRPO-conjugated goat anti-mouse or chicken IgG antibodies and ECL Western blotting detection reagents. The prestained molecular size marker was included in the same gel and three experiments were accomplished independently.

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Table 4.

Comparison of relative expression levels of H9N2-NA and NDV-F to MDV-pp38 in MDV- GX0101 and its recombinant with H9N2-NA and NDV-F genes.

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