Summary: A synthetic peptide (peptide 10) representing a surface-exposed, linear B cell epitope from outer-membrane (OM) protein F of was shown previously to afford protection in mice from infection. This peptide was expressed in tandem with the protein F peptide 18 on each of the two coat proteins of cowpea mosaic virus (CPMV). The chimaeric virus particles (CVPs) expressing the peptides on the S (small) coat protein (CPMV-PAE4) and L (large) coat protein (CPMV-PAE5) were used to immunize mice. Following subcutaneous immunization in Freund's and QuilA adjuvants, CPMV-PAE4 induced antibodies predominantly against peptide 18, whereas CPMV-PAE5 produced antibodies exclusively against peptide 10, indicating that the site of peptide expression on CPMV influences its immune recognition. The anti-peptide antibodies elicited by CPMV-PAE5 were predominantly of the IgG isotype, indicating a highly polarized TH1-type response. The peptide-specific IgG strongly recognized the whole F protein, but more importantly, recognized protein F in all seven Fisher-Devlin immunotypes of Furthermore, the peptide-specific IgG in CVP/QS-21 adjuvant-immunized mice was shown to bind complement and to augment phagocytosis of by human neutrophils The ability of CPMV-PAE5 to induce -specific opsonic IgG gives it potential for further development as a protective vaccine against .


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