Designing a Novel Recombinant HN Protein with Multi Neutralizing Antigenic Sites and Auto Tag Removal Ability Based on NDV-VIIj for Diagnosis and Vaccination Application

Indian Journal of Microbiology
V MayahiNaser Harzandi

Abstract

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.

References

Jun 3, 2000·Annual Review of Immunology·S GurunathanR A Seder
Nov 20, 2002·Journal of Virology·Lori W McGinnesTrudy G Morrison
Sep 5, 2008·Clinical and Vaccine Immunology : CVI·Sun-Hee ChoSun-Joong Kim
Dec 2, 2011·Journal of Biomedicine & Biotechnology·Han Yuen LamNoorjahan Banu Alitheen
Dec 27, 2011·Veterinary Research·Jos C F M DortmansBen P H Peeters
Dec 23, 2016·Archives of Virology·Majid EsmaelizadHossein Goudarzi

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Datasets Mentioned

BETA
KU938925

Methods Mentioned

BETA
enzyme-linked immunosorbent assays
affinity purification
ELISA

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