The role of conserved arginine and proline residues in enterovirus VP1 protein

Ya-Ling Huang; Tsun-Mei Lin; Shu-Ying Wang; Jen-Ren Wang

doi:10.1016/j.jmii.2022.01.004

The role of conserved arginine and proline residues in enterovirus VP1 protein

J Microbiol Immunol Infect. 2022 Aug;55(4):590-597. doi: 10.1016/j.jmii.2022.01.004. Epub 2022 Feb 17.

Authors

Ya-Ling Huang¹, Tsun-Mei Lin², Shu-Ying Wang³, Jen-Ren Wang⁴

Affiliations

¹ Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Department of Laboratory Medicine, E-Da Hospital, Kaohsiung, Taiwan; Department of Medical Laboratory Science, I-Shou University, Kaohsiung, Taiwan.
² Department of Medical Laboratory Science, I-Shou University, Kaohsiung, Taiwan; Department of Medical Research, E-Da Hospital, Kaohsiung, Taiwan.
³ Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Department of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Center of Infectious Disease and Signaling Research, National Cheng Kung University, Tainan, Taiwan.
⁴ Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan; Center of Infectious Disease and Signaling Research, National Cheng Kung University, Tainan, Taiwan; Department of Medical Laboratory Science and Biotechnology, College of Medicine, National Cheng Kung University, Tainan, Taiwan; National Institute of Infectious Diseases and Vaccinology, National Health Research Institutes, Tainan, Taiwan. Electronic address: jrwang@mail.ncku.edu.tw.

PMID: 35232679
DOI: 10.1016/j.jmii.2022.01.004

Abstract

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.

Keywords: Arginine; Conserved residues; Enterovirus; Flexibility; Proline; VP1.

MeSH terms

Amino Acid Sequence
Antigens, Viral
Arginine
Capsid Proteins
Enterovirus Infections*
Enterovirus*
Humans
Proline

Substances

Antigens, Viral
Capsid Proteins
Arginine
Proline