Application of molecular biology techniques to
the production of new vaccines against different strains of
the Newcastle disease virus (NDV) has been the subject of
recent research reports. Development of improved techniques
for genome sequencing has led to the recognition of
protective mechanisms and the identification of possible
candidate antigens. Such procedures could generate meaningful
results regarding the virulence determinants of NDV.
This study proposed an in silico approach by assembling
potential and conserved epitopic regions of hemagglutinin–
neuraminidase (HN) and fusion (F) glycoproteins of NDV to
induce multiepitopic responses against the virus. Epitope
predictions showed that the hypothetic... More
Application of molecular biology techniques to
the production of new vaccines against different strains of
the Newcastle disease virus (NDV) has been the subject of
recent research reports. Development of improved techniques
for genome sequencing has led to the recognition of
protective mechanisms and the identification of possible
candidate antigens. Such procedures could generate meaningful
results regarding the virulence determinants of NDV.
This study proposed an in silico approach by assembling
potential and conserved epitopic regions of hemagglutinin–
neuraminidase (HN) and fusion (F) glycoproteins of NDV to
induce multiepitopic responses against the virus. Epitope
predictions showed that the hypothetical synthetic construct
could induce immature B and T cell epitopes that expect a
high immune response because of their location in four
distinct parts of the construct, namely the head, stalk and the
heptad repeated regions known as the HRA and HRB
domains. Most regions of the chimeric construct were found
to have high antigenic propensity and surface accessibility,
which further confirmed the strategy for selection of precise
continuous and discontinuous epitopes of HN and F antigens.
Thermodynamic folding of mRNA structures revealed
correct folding of the RNA construct, indicating good stability
of the mRNA to increase the efficiency of translation
in the target host. The three-dimensional structure of the
native HN-F chimeric protein was successfully generated
and validated as a proper model which may define reliability,
structural quality and conformation.
