Home List of Titles Identification of neutralizing linear epitopes from the VP1 capsid protein of Enterovirus 71 using synthetic peptides
Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/81699
- Identification of neutralizing linear epitopes from the VP1 capsid protein of Enterovirus 71 using synthetic peptides
- Foo, Damian Guang Wei; Alonso, Sylvie; Phoon, Meng Chee; Ramachandran, N. P.; Chow, Vincent Tak Kwong; Poh, Chit Laa
- Enterovirus 71 (EV71) is the main causative agent of Hand, foot and mouth disease (HFMD) and has been associated with severe neurological diseases resulting in high mortalities. Currently, there is no vaccine available and treatment is limited to palliative care. In this study, antisera were raised in mice against 95 overlapping synthetic peptides spanning the VP1 capsid protein of EV71. Two peptides, SP55 and SP70, containing amino acid 163-177 and 208-222 of VP1, respectively, are capable of eliciting neutralizing antibodies against EV71 in the in vitro microneutralization assay. SP70 was identified to be particularly potent in eliciting a neutralizing antibody titer comparable to that obtained with a whole virion-immune serum. Immunization of mice with either SP55 or SP70 triggered an EV71-specific IgG response as high as that obtained with the whole virion as immunogen. The IgG sub-typing revealed that the neutralizing antibodies elicited by both synthetic peptides are likely belonging to the IgG1 sub-type. Alignment with databases showed that the amino acid residues of SP70 are highly conserved amongst the VP1 sequences of EV71 strains from various sub-genogroups. Altogether, these data indicate that SP70 represents a promising candidate for an effective synthetic peptide-based vaccine against EV71.
- Publication type
- Journal article
- Virus Research, Vol. 125, no. 1 (Apr 2007), pp. 61-68
- Publication year
- FOR Code(s)
- 0605 Microbiology
- Enterovirus 71; Neutralizing antibodies; Synthetic peptides; VP1 capsid protein
- Publisher URL
- Copyright © 2007 Elsevier B.V. All rights reserved.
- Peer reviewed