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Open AccessJournal ArticleDOI

Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus.

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TLDR
A major antibody combining site on foot and mouth disease virus (FMDV) serotype O1K has been identified in a predicted surface helix of viral protein 1 (VP1) between amino acid residues 144 and 159, which elicits high titers of antibodies that specifically recognize and neutralize FMDV.
Abstract
A major antibody combining site on foot and mouth disease virus (FMDV) serotype O1K has been identified in a predicted surface helix of viral protein 1 (VP1) between amino acid residues 144 and 159. A hexadecapeptide covering this sequence elicits high titers of antibodies that specifically recognize and neutralize FMDV. The high quality of the immune response is attributed to a particularly stable conformation of the antigenic amino acid sequence, which is most likely an alpha-helix.

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Journal ArticleDOI

Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid.

TL;DR: It was found that the leucine residues at positions 148 and 151 were essential for reaction with antisera raised against intact virus, and may lead to better understanding of the basis of antigen-antibody interaction and antibody specificity.
Book ChapterDOI

Turns in peptides and proteins.

TL;DR: The aim of this chapter is to examine structural and functional roles of turns in peptides and proteins.
Journal ArticleDOI

Foot-and-Mouth Disease

TL;DR: The reemergence of FMD in developed countries that had been disease free for many years is described and the effect that this has had on disease control strategies is described.
Journal ArticleDOI

Structure of a human common cold virus and functional relationship to other picornaviruses

TL;DR: The first atomic resolution structure of an animal virus, human rhinovirus 14, strikingly similar to known icosahedral plant RNA viruses, and four neutralizing immunogenic regions have been identified.
Journal ArticleDOI

Prediction of chain flexibility in proteins

TL;DR: This work has analyzed 31 refined protein structures to develop a method for predicting flexible segments from a given amino acid sequence and found that segmental flexibility is more indicative of an antigenic determinant than the selection criteria mentioned above.
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