Analysis of methyltransferase (MTase) domain from Zika virus (ZIKV)

A comprehensive analysis of methyltransferase (MTase) from Zika virus (ZIKV) is of interest in the development of drugs and biomarkers in the combat and care of ZIKA fever with impulsive joint pain and conjunctivitis. MTase sequence is homologous in several viral species. We analyzed the MTase domain from ZIKV using Bioinformatics tools such as SMART, PROSITE, PFAM, PANTHER, and InterProScan to glean insights on the sequence to structure to function data. We document inclusive information on MTase from ZIKV for application in the design of drugs and biomarkers to fight against the disease.


Abstract:
A comprehensive analysis of methyltransferase (MTase) from Zika virus (ZIKV) is of interest in the development of drugs and biomarkers in the combat and care of ZIKA fever with impulsive joint pain and conjunctivitis. MTase sequence is homologous in several viral species. We analyzed the MTase domain from ZIKV using Bioinformatics tools such as SMART, PROSITE, PFAM, PANTHER, and InterProScan to glean insights on the sequence to structure to function data. We document inclusive information on MTase from ZIKV for application in the design of drugs and biomarkers to fight against the disease.
Keywords: ZIKV, methyltransferase, beta turn, α-helix, SMART, Prosite, Pfam and InterProScan Initially, the C-terminal end has the conserved MTase crease framed by 7 strands β-sheet encompassed by 4 αhelices. In some structures an SAH (S-adenosyl-L-homocysteine) molecule is discovered bound to this domain [9]. The second subdomain contains a helix-turn-helix theme, a β-strand and a α-helix structure at its N-terminals end. This domain was proposed to organize the GTP (guanosine-5′-triphosphate) moiety of 7methylguanosine-GTP amid the 2'-O-ribose methylation as observed in the crystal structures bound to m7Gppp-RNA (7methylguanosine cap at the 5' end of mRNA) [9]. The 3 rd subdomain is situated between the two previous ones and is made out of an α-helix and two β strands [10]. Therefore, it is of interest to document broad information on MTase from ZIKV for application in the fight against the disease.

Methodology: Sequence and conserved domain analysis MTase:
The sequence of the MTase domain was retrieved from the NCBI genome database followed by protein BLAST (BLASTp) analysis. The sequence was further subject to SMART, Prosite, Pfam, PANTHER, and InterProScan as described elsewhere [11][12][13].

Analysis of predicted secondary structure:
The secondary structures were assigned using PSIPRED available at http://bioinf.cs.ucl.ac.uk/psipred.

Structure analysis
The sequence was further analyzed for structural features such as beta turns, helices and disallowed regions using tools as described elsewhere

Figures 4:
The plots for turns demonstrate a Ramachandaran plot with residues i+1 (brown circle) and i+2 (green square) plotted on it. The following is a graphic plot of the turn with the four amino acid residues and marked C alpha (i) C alpha (i+3) distance. A red arrow, if present, indicates that residue I donate a hydrogen bond to residue i+3. The numbers of residue and type of turn are demonstrated over the Ramachandaran plot.

Figures 5:
The Helical haggle, and net' color diagrams represent the organization of the amino acid residues in every helix. The amino acid residues are in green color for hydrophobic, blue color for polar and red color for charged amino acid. Haggles and nets accepted the helical estimation of 3.6 residues per turn.
©Biomedical Informatics (2020) Turns excluded from all the above categories The nomenclature describes the regions of the Ramachandaran plot occupied by residues i + 1 and i + 2 of the turn. Number of beta turns in chain 17; *Asterisked motifs correspond to those illustrated in the motif plots ( Figure 4).   Figure 2A. Different residues at the same location are scaled on the basis of residue frequency as shown in Figure 2B. Secondary structure and antigenic determinant of the MTase domain is shown in Figure 3. The major epitope peptides are six that are highlighted in color boxes (Figure 3). Data on beta turns in the MTase is given in Table 1 and Table 2. Data on helices in the MTase domain is given in Table 3. Thus, we document inclusive information on MTase from ZIKV for application through a comprehensive understanding in the design of drugs and biomarkers to fight against the disease caused by the virus.

Conclusion:
We document prelimianary information from a comprehensive analysis on MTase from ZIKV using Bioinformatics tools such as SMART, PROSITE, PFAM, PANTHER, and InterProScan to glean insights on the sequence to structure to function data for combat and care of ZIKA fever.

Conflict of Interests:
There is no conflict of interests among the authors regarding the present publication.