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conferenceseries
.com
Volume 7, Issue 5 (Suppl)
J Biotechnol Biomater
ISSN: 2155-952X JBTBM, an open access journal
Biotechnology 2017
November 13-14, 2017
November 13-14, 2017 Osaka, Japan
19
th
World Congress on
Biotechnology
A novel marvelous evolutionary detection: Lack of a large 2888 bp intron region within
HA03
gene
from
Hyalomma anatolicum anatolicum
, unlike its commercial recombinant anti-tick orthologue,
Bm86
, from
Boophilus microplus
Khosrow Aghaiypour Kolyani and Mohsen Aali
Razi Vaccine and Serum Research Institute, Iran
H
yalomma anatolicum anatolicum
(
H. a. anatolicum
) as the most widespread tick species in Iran and other parts of the
middle east is responsible for the hugely serious economic losses in livestock industry. This study was conducted to
investigate genetic variability of the
Bm86
orthologous gene,
HA03
, in five different Iranian
H. a. anatolicum
isolates including
Kordan, Qom, Boinzahra, Lorestan and Bushehr. Likewise, a number of
in silico
analyses were performed in order to predict
the possible impact of the amino acid substitutions on antigenicity of the protein. Comparative sequence analysis of the
Bm86
orthologous gene sequence among five tick isolates allowed for identification of four non-synonymous single nucleotide
polymorphisms (SNPs) including c.995A>C, c.1150G>C, c.1151A>C/T and c.1152G>T which would result in p.Asn 332 Thr,
p.Glu 384 Leu and p.Glu 384 Ala substitutions. As much as antigenicity is concerned, based on our
in silico
studies, the amino
acid position 384 was located in a putative antigenic peptide of the protein. Our subsequent physicochemical and structural
analyses illustrated that two out of three amino acid substitutions including p.Glu 384 Leu and p.Glu 384 Ala considerably
influenced the 3-dimensional structure and physicochemical properties of
HA03
protein including hydrophobicity,
amphiphilicity and net charge; thus, they might affect the antigen-antibody reaction and consequently immunogenicity of the
antigen. In conclusion, it is a rational measure not only to replace
Bm86
with
HA03
in formulation of the recombinant anti-tick
vaccine, but also to combine various antigens extracted from different isolates of the tick species.
Biography
Khosrow Aghaiypour Kolyani has completed his PhD from Tehran University of Medical Sciences and Postdoctoral studies from National Institute of Health,
National Cancer Institute at frederick, USA. He is the Head of Genomics and Genetic Engineering, Department of Razi Vaccine and Serum Research Institute,
which organizes the main human and animal vaccine research in Iran. He has published more than 30 papers in reputed journals and has been serving as an
Editorial-Board member of repute.
Khosrow@rvsri.ac.irKhosrow Aghaiypour Kolyani et al., J Biotechnol Biomater 2017, 7:5 (Suppl)
DOI: 10.4172/2155-952X-C1-082