Bacteriophage lambda capsids can provide a highly flexible scaffold for the high density display of foreign peptides and pro-teins One commonly used method is to fuse the protein or peptide of interest to the major phage capsid protein, gpD, thereby producing phage particles that incorporate the desired protein into their capsids when propagated in E. coli host cells . However, this approach is suboptimal for glycosylated proteins such as the HIV-1 envelope glycoprotein or the influenza virus hemagglutinin (HA). Consequently, an alter-native display approach has therefore been developed which allowsone to “decorate” preformed, gpD-deficient phage with exogenously supplied gpD or recombinant gpD-fusion proteins, producedin eukaryotic cells (Mattiacio et al., 2011