Publication: Variation at position 350 in the Chikungunya virus 6K-E1 protein determines the sensitivity of detection in a rapid E1-antigen test
Issued Date
2018-12-01
Resource Type
ISSN
20452322
Other identifier(s)
2-s2.0-85040782089
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Scientific Reports. Vol.8, No.1 (2018)
Suggested Citation
Aekkachai Tuekprakhon, Emi E. Nakayama, Koen Bartholomeeusen, Orapim Puiprom, Tadahiro Sasaki, Ralph Huits, Natthanej Luplertlop, Nathamon Kosoltanapiwat, Pannamas Maneekan, Kevin K. Ariën, Tatsuo Shioda, Pornsawan Leaungwutiwong Variation at position 350 in the Chikungunya virus 6K-E1 protein determines the sensitivity of detection in a rapid E1-antigen test. Scientific Reports. Vol.8, No.1 (2018). doi:10.1038/s41598-018-19174-8 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/47486
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Variation at position 350 in the Chikungunya virus 6K-E1 protein determines the sensitivity of detection in a rapid E1-antigen test
Abstract
© 2018 The Author(s). Chikungunya virus (CHIKV), a mosquito-borne pathogen, consists of three genotypes: East/Central/South African (ECSA), West African (WA), and Asian. Although a current rapid immunochromatographic (IC) test detecting CHIKV E1-antigen showed high sensitivity to ECSA-genotype viruses, it showed poor performance against the Asian-genotype virus that is spreading in the American continents. To understand the basis for the low performance of this IC test against Asian-genotype virus, we re-examined the anti-CHIKV monoclonal antibodies (mAbs) used in the assay for their interaction with E1-antigen of the three CHIKV genotypes. We found that the reactivity of one mAb for Asian-genotype virus was lower than that for ECSA virus. Comparison of E1 amino acid sequences revealed that the ECSA virus used to generate these mAbs possesses glutamic acid (E) at position 350, in contrast to WA and Asian, which possess aspartic acid (D) at this position. Site-directed mutagenesis confirmed that the mutation altered mAb reactivity, since E-to-D substitution at position 350 in ECSA reduced recognition by the mAb, while D-to-E substitution at this position in Asian and WA increased affinity for the mAb. Taken together, these results indicate that residue 350 of the CHIKV 6K-E1 is a key element affecting the performance of this IC assay.