Agricultural Research Management Information System

Home
Research Summary
Search
About Us
- ARMIS
- Brochure
Contact Us
Report
User Request
Data Input
Help
- Operation Manual
  - PDF
  - Video
- Program Area & Commodity
We have reached 37600 number of research entries at this moment.

- Logout

Research Detail

Home
Research
Detail

Comparison Between Envelope Protein Vp19 and Tegument Protein Vp26 of White Spot Syndrome Virus in Crustaceans: an In-silico Approach

Mehedi Mahmudul Hasan
Associate Professor
Department of Fisheries and Marine Science Noakhali Science and Technology University Noakhali-3814, Bangladesh

Abstract/ Executive Summary:

This study considered previously published sequences of VP19 and VP26 structural proteins of White Spot Syndrome Virus. The sequences were retrieved from National Center for Biotechnology Information (NCBI). VP 19 sequences were from the isolates of India, China, Singapore, Mexico and the Netherlands. VP26 sequences were from the isolates of India, China, Brazil and Mexico. These were aligned using UNIPROT and the phylogenetic trees were drawn through MEGA 7. VP19 sequence of the Singapore isolate (accession no. AAK96179) and VP26 sequence of the Chinese isolate were reference proteins in this study. Mutations were observed in the amino acid position of 9, 15, 66, 71, 73 and 95 in the VP19 sequences from other geographical locations than the reference one. In the VP26 sequences, mutations started from the 127th amino acid position. Amino acid substitutions were observed in the hydrophobic, polar and charged regions of both the proteins. Although mutations were observed, the sequences of the individual proteins show a conserved nature in different geographical locations for the sequence homology.

Keywords: Sequence, Protein, Amino acids

Location:

Start Date:

End Date:

Program Area: Pest Management

Commodity: Virus, Shrimp

Objectives:

Later the classification of structural proteins changed and VP26 were included as a tegument protein. VP28, VP26 and VP24 could be the result of gene duplication because of evolution. None of these major structural proteins are glycosylated which is a very exceptional feature among the enveloped viruses. This current study compares the amino acid sequences of the major envelope protein VP19 and nucleocapsid protein VP26.

Methodology:

2.1 Sequence dataset VP19 and VP26 Sequences were downloaded from NCBI. 8 VP19 sequences and 7 VP26 sequences from different geographic locations of the world were selected for study.

2.2 Multiple sequence alignment and drawing phylogenetic tree All the sequences were aligned using MEGA 7. Phylogenetic trees for both the protein sequences were also drawn using MEGA 7. Maximum likelihood method was chosen for generating the phylogenetic trees.

2.3 Analysis of amino acid properties Annotations and the amino acid properties of both the alignment were done through UNIPROT. Similarity, hydrophobic, negative, positive, aliphatic, tiny, aromatic, charged, small, polar, big, serine-threonine were considered for the analysis.

Source of Information: International Journal of Fisheries and Aquatic Studies 2020; 8(2): 203-210

Article Link (Online Journal):

Funding Source:

Budget:

Total Budget (Tk.) :

Achievement/Findings:

The sequences show the highly conserved nature of VP19 and VP26. VP19 is an envelope protein that may have an important role in binding with the host protein. The mutations could be important for the immunogenic response of the host which can only be confirmed after challenging the crustaceans with different phylotypes of these proteins. WSSV structural proteins can be used in the search for remedies from white spot disease in crustaceans. These are structural proteins and may have evolved from gene duplication. It is important to know if there is any effect of temperature on mutation and the virulence of isolates from different geographical locations.

Knowledge Management: Journal