TY - JOUR
T1 - The role of conserved arginine and proline residues in enterovirus VP1 protein
AU - Huang, Ya Ling
AU - Lin, Tsun Mei
AU - Wang, Shu Ying
AU - Wang, Jen Ren
N1 - Funding Information:
We would like to thank Dayna Cheng for English editing and Prof. Hsiao-Sheng Liu and Prof. Shun-Hua Chen for critical review and comment of this manuscript. This work was supported by grants from E-Da Hospital and National Cheng Kung University (grant nos. EDAHT104011 , NCKUEDA10313 ). Ministry of Science and Technology, Taiwan ( 109-2320-B-006-053 , 110-2320-B-006-031-MY3 ); National Health Research Institutes, Taiwan ( IV-109-PP-13, IV-110-PP-11 ).
Funding Information:
We would like to thank Dayna Cheng for English editing and Prof. Hsiao-Sheng Liu and Prof. Shun-Hua Chen for critical review and comment of this manuscript. This work was supported by grants from E-Da Hospital and National Cheng Kung University (grant nos. EDAHT104011, NCKUEDA10313). Ministry of Science and Technology, Taiwan (109-2320-B-006-053, 110-2320-B-006-031-MY3); National Health Research Institutes, Taiwan (IV-109-PP-13, IV-110-PP-11).
Publisher Copyright:
© 2022
PY - 2022/8
Y1 - 2022/8
N2 - Background: High diversity of VP1 protein among enteroviruses has been a barrier in developing universally effective antiviral drugs. To maintain structure stability during evolution, several residues of VP1 protein of enteroviruses are conserved. Therefore, investigation of highly conserved residues in VP1 protein may provide information for antiviral drug candidates against enteroviruses. Methods: To identify highly conserved amino acid sequences of the VP1 in enterovirus genus, the Consurf and CABS-flex 2.0 web software were applied. Through the combination with secondary structure information, we focused on conserved amino acids of VP1 property analysis. Results: Most conserved residues of VP1 were in the interior and interacted with VP2, VP3 and VP4 capsid proteins. Structure of EV-A71 (PDB code 4AED) showed conserved residues were at hydrophobic pocket and close to the junction between the loop and β-barrel. Interestingly, arginine was the most common conserved residue of VP1. Proline was the second most common conserved residue and was found in the loop and β-barrel intersection areas. VP1 protein flexibility was associated with the secondary structure. Conserved residues of VP1 in β-barrel showed significantly low flexibility. Conclusion: Through large scale sequence analysis, we identified the amino acid distribution and location of conserved residues in VP1. This knowledge can be extrapolated for the Enterovirus genus and may contribute to developing the potential compound as an anti-enteroviral agent.
AB - Background: High diversity of VP1 protein among enteroviruses has been a barrier in developing universally effective antiviral drugs. To maintain structure stability during evolution, several residues of VP1 protein of enteroviruses are conserved. Therefore, investigation of highly conserved residues in VP1 protein may provide information for antiviral drug candidates against enteroviruses. Methods: To identify highly conserved amino acid sequences of the VP1 in enterovirus genus, the Consurf and CABS-flex 2.0 web software were applied. Through the combination with secondary structure information, we focused on conserved amino acids of VP1 property analysis. Results: Most conserved residues of VP1 were in the interior and interacted with VP2, VP3 and VP4 capsid proteins. Structure of EV-A71 (PDB code 4AED) showed conserved residues were at hydrophobic pocket and close to the junction between the loop and β-barrel. Interestingly, arginine was the most common conserved residue of VP1. Proline was the second most common conserved residue and was found in the loop and β-barrel intersection areas. VP1 protein flexibility was associated with the secondary structure. Conserved residues of VP1 in β-barrel showed significantly low flexibility. Conclusion: Through large scale sequence analysis, we identified the amino acid distribution and location of conserved residues in VP1. This knowledge can be extrapolated for the Enterovirus genus and may contribute to developing the potential compound as an anti-enteroviral agent.
UR - http://www.scopus.com/inward/record.url?scp=85125436883&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85125436883&partnerID=8YFLogxK
U2 - 10.1016/j.jmii.2022.01.004
DO - 10.1016/j.jmii.2022.01.004
M3 - Article
C2 - 35232679
AN - SCOPUS:85125436883
SN - 1684-1182
VL - 55
SP - 590
EP - 597
JO - Journal of Microbiology, Immunology and Infection
JF - Journal of Microbiology, Immunology and Infection
IS - 4
ER -