Novel peptides screened by phage display peptide library can mimic epitopes of the FnBPA ‐A protein and induce protective immunity against Staphylococcus aureus in mice

In this study, the purified rabbit anti ‐FnBPA‐A antibodies were used to screen a phage random 12‐mer peptide library for FnBPA‐A epitopes. After four rounds of panning, eight positive phage were detected by sandwich and competitive ELISA and then sequenced. Five peptides mimicking FnBPA‐A protein epitopes were obtained, and a p artially protective immunity againstStaphylococcus aureus infection can be stimulated by these peptides in mice. AbstractFibronectin ‐binding protein A (FnBPA) is a key adhesin ofStaphylococcus aureus, and the protein binding to fibrinogen and elastin is mediated by its N ‐terminal A domain. Thus, FnBPA‐A has been considered a potential vaccine candidate, but the relevant epitopes are not fully understood. Here, purified rabbit anti‐FnBPA‐A antibodies were produced and used to screen for peptides corresponding to or mimicking the epitope of native FnBPA‐A p rotein by using a phage random 12‐mer peptide library. After four rounds of panning, 25 randomly selected phage clones were detected by phage‐ELISA and competition‐inhibition ELISA. Then, eight anti‐rFnBPA‐A antibody‐binding phage clones were selected for sequencing, and six different 12 ‐mer peptides were displayed by these phages. Although these displayed peptides shared no more than three consecutive amino acid residues identical to the sequence of FnBPA‐A, they could be recognized by the FnBPA‐A‐specific antibodies in vitro and could induce specific ant...
Source: MicrobiologyOpen - Category: Microbiology Authors: Tags: ORIGINAL ARTICLE Source Type: research