alexa Characterization of Molecular Mimicry Between UL18 Glycoprotein of Human Cytomegalovirus [HCMV] and Class-I MHC Molecule through Pattern-based Analysis: An In-silico Approach
ISSN: 2157-7420

Journal of Health & Medical Informatics
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Research Article

Characterization of Molecular Mimicry Between UL18 Glycoprotein of Human Cytomegalovirus [HCMV] and Class-I MHC Molecule through Pattern-based Analysis: An In-silico Approach

Sarkar A*, Chatterjee A, Ansari S and Chakraborty N

ICMR Virus Unit, GB4, ID and BG Hospital, 57, Dr. S. C. Banerjee Road, Beliaghata, Kolkata, West Bengal, India

*Corresponding Author:
Sarkar A
Virology and Biotechnology
ICMR Virus Unit, GB4, ID and BG Hospital
57, Dr. S. C. Banerjee Road, Beliaghata, Kolkata, West Bengal, India
Tel: +91-9734320302
E-mail: [email protected]

Received date: May 02, 2016; Accepted date: May 17, 2016; Published date: May 24, 2016

Citation: Sarkar A, Chatterjee A, Ansari S, Chakraborty N (2016) Characterization of Molecular Mimicry Between UL18 Glycoprotein of Human Cytomegalovirus [HCMV] and Class-I MHC Molecule through Pattern-based Analysis: An In-silico Approach. J Health Med Informat 7:230. doi: 10.4172/2157-7420.1000230

Copyright: © 2016 Sarkar A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

Viral replication occurs using the host cell synthesis mechanisms and they are able to exploit the mechanisms of nucleic acid replication and protein translation machinery. Viral proteins require a target to fit subcellular compartments of the host cell and localized in different cellular compartments including the nucleus. Human Cytomegalovirus downregulates expression of traditional class-I MHC [Major Histocompatibility Complex] molecules at the infected cell surface and allows the infected cells to avoid acknowledgment by cytotoxic T-cells. In the present study, we have focused on generally accessible online and offline computational tools to examine practical and fundamental characteristics of the most conserved domain [CD] of UL18 gene along with the viral class-I MHC molecule. Six open reading frames [ORF] were reanalyzed by selecting start codon. Site-specific homology was determined to the MHC class-I molecule [19 to 197 residual position; ID: pfam00129, E-value: 3.26e-14]. The predicted protein architecture contained about 28.90% helices [107 residues] and 10.32% strands [38 residues]. The tertiary structure represented that 276 residues [75% of sequence] were modeled by the single highest scoring template with 100% confidence and the structure represents a peptide-binding viral MHC mimic, apprenticed to a host inhibitory receptor [pdb code-3d2u]. Thus, our analysis suggests that the homologous sequence corresponding to MHC class-I gene is situated between 19 and 200th residues of UL18 ORF and the recognition domain was identified with significant E-value. Our study also demonstrated that the ORF18 is homologous to the Ig-superfamily in 229-289th position. Therefore, these domains were found to date homologous in HCMV proteins suggesting a particular functional role during infection. In light of the above, further experimental steps are needed to elucidate the exact role of the UL18 during infections.

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