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Hemagglutinin–neuraminidase (HN) protein besides its mediation in viral pathogenesis, is composed of various antigenic sites which stimulate production of host’s antibodies. Thus, application of this protein in serological tests and vaccination plays a major role in biosecurity and control programs. In the present study, we designed a recombinant HN protein containing different neutralizing antigenic sites with velogenic patterns, and sub-cloned it into pET-43.1a+ expression vector. The expression of NusA-HN recombinant protein was induced. Affinity chromatography protein purification using HisPur? Ni–NTA was then conducted. Moreover, we performed western-blot technique using HRP-conjugated Anti His-Tag. Results revealed that following induction of recombinant protein, two distinct bands of HN-61 kDa and NusA-63 kDa were purified and identified by western-blotting. We recommend further analysis should be carried out to determine the functional role of this recombinant protein in enzyme-linked immunosorbent assays for Newcastle disease diagnosis. This HN protein containing multi neutralizing antigenic sites might also be applicable in vaccination programs to increase vaccines potency. 相似文献
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Mayahi Vafa Esmaelizad Majid Ganjalikhany Mohamad Reza 《International journal of peptide research and therapeutics》2020,26(3):1513-1522
International Journal of Peptide Research and Therapeutics - Fusion (F) and Hemagglutinin-neuraminidase (HN) glycoproteins of Newcastle disease virus containing important epitopes play crucial role... 相似文献
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Majid Esmaelizad Gholamreza Ahmadian Khosrow Aghaiypour Mehdi Shamsara Habibellah Paykari Majid Tebianian 《Memórias do Instituto Oswaldo Cruz》2013,108(4):408-413
In this study, we designed an experiment to predict a potential
immunodominant T-cell epitope and evaluate the protectivity of this antigen in
immunised mice. The T-cell epitopes of the candidate proteins (EgGST, EgA31,
Eg95, EgTrp and P14-3-3) were detected using available web-based databases. The
synthesised DNA was subcloned into the pET41a+ vector and expressed in
Escherichia coli as a fusion to glutathione-S-transferase
protein (GST). The resulting chimeric protein was then purified by affinity
chromatography. Twenty female C57BL/6 mice were immunised with the antigen
emulsified in Freund''s adjuvant. Mouse splenocytes were then cultured in
Dulbecco''s Modified Eagle''s Medium in the presence of the antigen. The
production of interferon-γ was significantly higher in the immunised mice than
in the control mice (> 1,300 pg/mL), but interleukin (IL)-10 and IL-4
production was not statistically different between the two groups. In a
challenge study in which mice were infected with 500 live protoscolices, a high
protectivity level (99.6%) was demonstrated in immunised BALB/C mice compared to
the findings in the control groups [GST and adjuvant (Adj) ]. These results
demonstrate the successful application of the predicted T-cell epitope in
designing a vaccine against Echinococcus granulosus in a mouse
model. 相似文献
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