Disease relevance of Bacteriophage P22

• Moreover, the RNA-binding, anti-terminator N proteins of lambda, phi21 and P22 phages show sequence similarities with HIV Nef at the Arg-rich motif [1].

High impact information on Bacteriophage P22

• Proteins with the parallel beta helix fold include three pectate lyases and the tailspike protein from P22 phage [2].
• These results are discussed in terms of a model in which Abc2 converts the RecBCD exonuclease for use in the P22 phage recombination pathway [3].
• Three bacterial pectate lyases, a pectin lyase from Aspergillus niger, the structures of rhamnogalacturonase A from Aspergillus aculeatus, RGase A, and the P22-phage tailspike protein, TSP, display the right-handed parallel beta-helix architecture first seen in pectate lyase [4].
• The effect of a recipient recD mutation was eliminated if the donor P22 phage expressed its Abc (anti-RecBC) function [5].
• A hybrid P22 phage, in which the T7 18.5 gene replaces the P22 gene 15, exhibits the plating properties of wild-type P22, strongly suggesting that the two genes have similar functions [6].

Chemical compound and disease context of Bacteriophage P22

• Eclipse of P22 phage particles to whole bacteria was likewise uninfluenced by the cation concentration in the reaction mixture, but eclipse by isolated receptor containing LPS required cations [7].

Gene context of Bacteriophage P22

• The identity of the cloned Isi1 gene, as a functional rfaF homologue, was confirmed by the complementation of a S. typhimurium rfaF mutant using a P22 phage sensitivity test [8].

References