PMID:19780551

Citation	Kageyama, Y, Murayama, M, Onodera, T, Yamada, S, Fukada, H, Kudou, M, Tsumoto, K, Toyama, Y, Kado, S, Kubota, K and Takeda, S (2009) Observation of the membrane binding activity and domain structure of gpV, which comprises the tail spike of bacteriophage P2. Biochemistry 48:10129-35
Abstract	The P2 phage virion has tail spike proteins beneath the baseplate and uses them to adsorb to the outer membrane of Escherichia coli during the infection process. Previous immunoelectron microscopic studies suggested that the tail spikes are composed of the gene V product (gpV); however, experimental evidence of its membrane binding activity has yet to be reported. In this study, we purified and characterized recombinant full-length gpV and its C-terminal domain. Limited chymotrypsin proteolysis of gpV produced a C-terminal domain composed of Ser86-Leu211. Our experiments demonstrated that the N- and C-terminal domains have very different melting temperatures: 50 and 74 degrees C, respectively. We also found that gpV binds the E. coli membrane via its C-terminal domain. We conclude that the C-terminal domain of gpV is a stable trimer and serves as the receptor-binding domain for the second step in the phage adsorption process.
Links	PubMed Online version:10.1021/bi900928n
Keywords	Bacteriophage P2/metabolism; Binding Sites; Escherichia coli/genetics; Escherichia coli/metabolism; Models, Molecular; Molecular Weight; Protein Conformation; Protein Structure, Tertiary; Temperature; Viral Structural Proteins/chemistry; Viral Structural Proteins/metabolism; Viral Tail Proteins/chemistry; Viral Tail Proteins/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BPP2:SPIKE		GO:0019062: virion attachment to host cell	ECO:0000247:	UniProtKB:Q9T1V4	P		Tail spikes in Escherichia phage P2 (Bacteriophage P2) is composed of gpV. In Fig 9 B, P2 gpV gets compared to Mu gp45. The results indicate that P2 gpV has typical features of phage tail spikes, such as a protease-sensitive N-terminal domain, a host-binding C-terminal domain, and a trimeric structure. This shows that gpV is a receptor-binding protein involved in the second step of phage adsorption.	complete
BPP2:SPIKE		GO:0019062: virion attachment to host cell	ECO:0000333:		P		Tail spikes in Escherichia phage P2 (Bacteriophage P2) are composed of gpV. In Fig 7, gpV-C was found in the precipitant with the membrane when purified gpV-C and E. coli membranes were mixed and centrifuged. This suggests that gpV-C bound to and precipitated with the E. coli membranes. No used in manual assertion child term.	complete

References

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