Recombinant haemagglutinin neuraminidase antigen-based single serum dilution ELISA for rapid serological profiling of Newcastle disease virus

Mohan, C. Madhan; Dey, Sohini; A, Rai; Kataria, J.M.

doi:10.1016/j.jviromet.2006.08.002

Cited by 27 publications

(19 citation statements)

References 10 publications

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“…Sensitivity, specificity, accuracy, and agreement (κappa coefficient) values for rNP-ELISA were determined in comparison to the IDEXX kit according to Mohan et al (2006). For the kappa coefficient (k), k < 0.2 indicates low agreement, 0.2 < k < 0.4 indicates weak agreement, 0.4 < k < 0.6 indicates moderate agreement, 0.6 < k < 0.8 indicates good agreement, and k > 0.8 indicates a high level of concordance between tests (Landis and Koch, 1977).…”

Section: Discussionmentioning

confidence: 99%

Development and application of an enzyme-linked immunosorbent assay (ELISA) using a soluble recombinant nucleoprotein for the detection of antibodies to avian influenza virus

Borzi¹,

Silva²,

Montassier³

et al. 2017

Afr. J. Microbiol. Res.

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Avian influenza (AI) causes significant impact on industrial poultry farming, besides infecting a variety of vertebrates. The detection of antibodies against viral antigens by serological methods is important for the epidemiology, control and prevention of AI because their high simplicity and speed for assaying a large number of samples. Obtaining antigenic preparations used for detection of anti-avian influenza virus (AIV) antibodies usually requires complex and expensive procedures and Escherichia coli system expression may be an alternative. The nucleoprotein (NP) of AIV is an ideal antigen candidate because it is highly conserved across AIV strains, resulting in high cross-reactivity and immunogenicity for avian hosts. The NP gene segment was cloned and expressed from AIV isolate H4N6 in E. coli fused to a small ubiquitin-like modifier (SUMO) polypeptide and a poly-histidine tag, obtaining a soluble recombinant NP (rNP) containing the most important epitopes. After purification, the rNP was used as an antigen to develop an indirect rNP-enzyme-linked immunosorbent assay (ELISA) to effectively detect anti-AIV antibodies in chicken serum samples. This rNP-ELISA had high sensitivity (95%), specificity (97%), accuracy (96.7%) and agreement (k=0.88) in a comparative analysis with a commercial ELISA kit. The results suggest that rNP-ELISA offers a viable alternative to improve immunodiagnosis of AIV infection in chickens.

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Section: Discussionmentioning

confidence: 99%

Development and application of an enzyme-linked immunosorbent assay (ELISA) using a soluble recombinant nucleoprotein for the detection of antibodies to avian influenza virus

Borzi¹,

Silva²,

Montassier³

et al. 2017

Afr. J. Microbiol. Res.

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“…Hence, the HN protein has been explored for the development of rapid antigen detection kit and subunit vaccines. Mohan et al (2006) expressed the HN protein of NDV in Escherichia coli, a typical prokaryotic expression system. The prokaryotic host does not offer any posttranslational glycosylation of proteins.…”

Section: Introductionmentioning

confidence: 99%

Antigenic validation of recombinant hemagglutinin-neuraminidase protein of Newcastle disease virus expressed in Saccharomyces cerevisiae

Sa¹,

Maity²,

Dc³

et al. 2015

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Summary. -The outer membrane glycoprotein, hemagglutinin-neuraminidase (HN) of Newcastle disease virus (NDV) is important for virus infection and subsequent immune response by host, and offers target for development of recombinant antigen-based immunoassays and subunit vaccines. In this study, the expression of HN protein of NDV is attempted in yeast expression system. Yeast offers eukaryotic environment for protein processing and posttranslational modifications like glycosylation, in addition to higher growth rate and easy genetic manipulation. Saccharomyces cerevisiae was found to be better expression system for HN protein than Pichia pastoris as determined by codon usage analysis. The complete coding sequence of HN gene was amplified with the histidine tag, cloned in pESC-URA under GAL10 promotor and transformed in Saccharomyces cerevisiae. The recombinant HN (rHN) protein was characterized by western blot, showing glycosylation heterogeneity as observed with other eukaryotic expression systems. The recombinant protein was purified by affinity column purification. The protein could be further used as subunit vaccine.

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“…Moreover, the recombinant protein has an advantage over whole virus preparation as it forms immunodominant epitopes and is devoid of any non-specific moieties in whole cell preparation. 2) IBV genome encodes four structural proteins, spike glycoprotein (S), membrane glycoprotein (M), phosphorylated nucleocapsid protein (N), and the small membrane glycoprotein (E). S glycoprotein on the outside of the virus is cleaved post-translationally by cellular proteases into amino-terminal S1 (535 amino acids; 90 kDa) and carboxyl-terminal S2 (627 amino acids; 84 kDa) subunits.…”

mentioning

confidence: 99%

Development of a multi-epitope antigen of S protein-based ELISA for antibodies detection against infectious bronchitis virus

Ding

Wang

Cao

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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Recombinant haemagglutinin neuraminidase antigen-based single serum dilution ELISA for rapid serological profiling of Newcastle disease virus

Cited by 27 publications

References 10 publications

Development and application of an enzyme-linked immunosorbent assay (ELISA) using a soluble recombinant nucleoprotein for the detection of antibodies to avian influenza virus

Development and application of an enzyme-linked immunosorbent assay (ELISA) using a soluble recombinant nucleoprotein for the detection of antibodies to avian influenza virus

Antigenic validation of recombinant hemagglutinin-neuraminidase protein of Newcastle disease virus expressed in Saccharomyces cerevisiae

Development of a multi-epitope antigen of S protein-based ELISA for antibodies detection against infectious bronchitis virus

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