Bacteriophage lambda capsids can provide a highly flexiblescaffold 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 majorphage capsid protein, gpD, thereby producing phage particles thatincorporate the desired protein into their capsids when propa-gated in E. coli host cells . However, this approach is suboptimalfor glycosylated proteins such as the HIV-1 envelope glycoproteinor the influenza virus hemagglutinin (HA). Consequently, an alter-native display approach has therefore been developed which allowsone to “decorate” preformed, gpD-deficient phage with exoge-nously supplied gpD or recombinant gpD-fusion proteins, producedin eukaryotic cells (Mattiacio et al., 2011