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Identification of group-common linear epitopes in structural and nonstructural proteins of enteroviruses by using synthetic peptides.

ABSTRACT: Synthetic peptides were employed in enzyme-linked immunosorbent assays to identify group-common linear epitopes in the structural and nonstructural proteins of enteroviruses. Nine linear epitopes were recognized by using sera from patients with heterotypic immunoglobulin G antibody responses to enterovirus infections. The most-reactive peptides were derived from conserved regions of the amino-terminal part of VP1, whereas peptides representing sequences from other conserved regions of VP1, as well as VP2, VP3, and VP4, and from a nonstructural region showed no or poor reactivity. These findings may be useful in the development of serological tests for the diagnosis of infections caused by a broad range of enteroviruses.

SUBMITTER: Cello J

PROVIDER: S-EPMC263586 | biostudies-other | 1993 Apr

REPOSITORIES: biostudies-other

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Identification of group-common linear epitopes in structural and nonstructural proteins of enteroviruses by using synthetic peptides.

Cello J J Samuelson A A Stålhandske P P Svennerholm B B Jeansson S S Forsgren M M

Journal of clinical microbiology 19930401 4

Synthetic peptides were employed in enzyme-linked immunosorbent assays to identify group-common linear epitopes in the structural and nonstructural proteins of enteroviruses. Nine linear epitopes were recognized by using sera from patients with heterotypic immunoglobulin G antibody responses to enterovirus infections. The most-reactive peptides were derived from conserved regions of the amino-terminal part of VP1, whereas peptides representing sequences from other conserved regions of VP1, as we ...[more]

PMID: 7681848

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