Archives of Clinical Infectious DiseasesVolume 11, Issue 4, October 2016, Article number e36270, 9p

Immunoinformatics study of gp120 of human immunodeficiency virus type 1 subtype CRF35_AD isolated from Iranian patients(Article)

  • aDepartment of Virology, Iran University of Medical Sciences, Tehran, Iran
  • bProteomics Research Center, Department of Medical Lab Technology, Faculty of Paramedical Sciences, Shahid Beheshti University of Medical Sciences, Tehran, Iran
  • cDepartment of Immunology, Razi Vaccine and Sera Research Instute, Karaj, Iran
  • dDepartment of Immunology, School of Medicine, AJA University of Medical Sciences, Tehran, Iran
  • eDepartment Infectious Diseases, School of Medicine, AJA University of Medical Sciences, Tehran, Iran

Abstract

Background: Human Immunodeficiency Virus (HIV)-1 infection is one of the most important infectious diseases in Iran, and common isolates belong to the new CRF35_AD subtypes. The Gp120 protein, which is located on the surface of the HIV envelope, plays a role in entrance into host cells and immune responses. As there isn’t any clear analysis of the envelope protein of Iranian isolates regarding potential variations, structural andimmunological properties, in the current studyweattempted to research in this area. Objectives: The present study was designed to demonstrate the immunoinformatics of gp120 of human immunodeficiency virus Type 1 subtype CRF35_AD, isolated from Iranian patients. Methods: In this analytical perspective bioinformatics study, the steps were as follows; data collection and sequence classification (303 sequences), finding the mutational/conserved regions, evaluation of N-linked glycosylation sites, prediction of tertiary structures, model validation, and prediction of conformational and linear B-cell epitopes. Results: High degrees of sequence variation in the CRF35_AD subtype and also more than 10 variation sites in gp120 protein segments were identified. The total N-linked glycosylation sites for selected complete env sequences in NX [ST] pattern and the NXS and NXT combination count revealed that most of the glycosylation sites were conserved. Tertiary structure was obtained by homology modeling, and the Ramachandran plot assessment showed model validity. Finally, mappedconsensus discontinuous immunogenic regions (epitopes) were AA25-65, AA337-365 and AA443-505. Conclusions: The obtained results provide a background for understanding CRF35_AD molecular characteristics, as well as design and development of effective HIV-1 vaccines and immunotherapeutic regimens against CRF35_AD subtype. © 2016, Infectious Diseases and Tropical Medicine Research Center.

Author keywords

  • CRF35_AD subtype
  • gp120
  • HIV-1
  • Immunoinformatics
  • Iran

Indexed keywords

EMTREE drug terms:epitopeglycoprotein gp 120
EMTREE medical terms:amino acid sequenceArticleB lymphocytecontrolled studyenvelope genegene mutationHuman immunodeficiency virus 1Human immunodeficiency virus type 1 subtype CRF35 ADimmunogenicityimmunoinformaticsIranian peoplemedical informaticsmolecular modelnonhumanpredictionprotein conformationprotein glycosylationprotein tertiary structuresequence analysisvalidation studyvirus isolation
  • ISSN: 23452641
  • Source Type: Journal
  • Original language: English
  • DOI: 10.5812/archcid.36270
  • Document Type: Article
  • Publisher: Kowsar Medical Publishing Company

  Ahmadi, N.A.; Proteomics Research Center, Department of Medical Lab Technology, Faculty of Paramedical Sciences, Shahid Beheshti University of Medical Sciences, Tehran, Iran; email:[email protected]
© Copyright 2017 Elsevier B.V., All rights reserved.

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