Computational comparison of T-cell epitopes of gp120 of Iranian HIV-1 with different subtypes of the virus.
In the present study, T-cell epitopes of gp120 of an Iranian isolate have been compared to different subtypes of HIV-1. At first, the amino acid sequences of gp120 were fetched from data banks. Then T-cell epitopes, disulfide bonding states, protein kinase C phosphorylation sites, cAMP-dependent protein kinase phosphorylation sites, casein kinase II phosphorylation sites, N-myristoylation sites and amidation sites were predicted using different soft wares. According to this computational analysis 6 good disulfide binding states in Iranian gp120 were predicted. From the viewpoint of cAMP-dependent protein kinase phosphorylation site (1 site) Iranian isolate was similar to clades B and F. Like subtype C 1 amidation site was predicted in the Iranian subtype. In the Iranian isolate 7 sites protein kinase C phosphorylation sites and 4 N-myristoylation sites were predicted. Since the number of individuals infected with HIV-1 in Iran, like many other countries is increasing, study of similarities and differences between the Iranian samples and different clades of HIV-1 can help us in identification of the origin and understanding the changes in the virus.
Mohabatkar
Hassan
H
Department of Biology, College of Sciences, Shiraz University, Shiraz 71454, Iran.
Mohammadzadegan
Reza
R
D000595:Amino Acid Sequence; D000939:Epitopes / Q000276:immunology*; D015699:HIV Envelope Protein gp120 / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D015497:HIV-1 / Q000145:classification / Q000276:immunology*; D007492:Iran; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D013045:Species Specificity; D013601:T-Lymphocytes / Q000276:immunology*
D000939:Epitopes; D015699:HIV Envelope Protein gp120; D011493:Protein Kinase C