Modification of carboxy-terminal amino acid composition to enhance expression of foot-and-mouth disease virus VP4 protein

• 영문명: Modification of carboxy-terminal amino acid composition to enhance expression of foot-and-mouth disease virus VP4 protein
• 발행기관: 한국예방수의학회
• 저자명: Sun Young Park Dohyun Kim Sang Hyun Park Jong-Hyeon Park Young-Joon Ko
• 간행물 정보: 『Journal of Preventive Veterinary Medicine』Vol.46, No.3, 114~120쪽, 전체 7쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 2022.09.30

영문 초록

Foot-and-mouth disease (FMD) is a highly contagious vesicular disease that affects cloven-hoofed animals, causing substantial economic losses to the livestock industry. The causative FMD virus (FMDV) comprises four structural proteins (VP1, VP2, VP3, and VP4) and several non-structural proteins. Among the capsid proteins, VP4 is the most conserved, making it an attractive target as a diagnostic and vaccine antigen, regardless of FMDV serotype. In this study, we attempted to express the VP4 protein N-terminally fused to a glutathione S-transferase (GST) tag in Escherichia coli. Whereas VP0 and VP2 proteins were expressed in the soluble fraction, we failed to detect VP4, even in the insoluble fraction. To investigate the effect of VP4 C-terminal amino acid residues on protein expression, we constructed three VP4 mutants fused to GST, among which the mutant in which the C-terminal 15 amino acid residues had been deleted showed the highest level of protein expression. Furthermore, protein expression was observed even in the mutant in which three amino acid residues (DKK) had been fused to the C terminus. However, unlike the other two mutants, the wild-type VP4 mutant was poorly expressed, thereby indicating that the C-terminal amino acid residues could play a pivotal role in determining expression of the VP4 protein in E. coli.

목차

INTRODUCTION

MATERIALS AND METHODS

RESULTS

DISCUSSION

ACKNOWLEDGEMENTS

REFERENCES

키워드

Foot-and-mouth disease virus VP4 protein expression carboxy-terminal amino acid residue