G3p: Difference between revisions
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==Functional Implications== | ==Functional Implications== | ||
===Infectivity=== | ===Infectivity=== | ||
[[Image:F1_holliger_and_riechmann.jpg |frame|center|Figure Adapted from Holliger and Riechmann, 1997<ref name="holliger 97"> PMID:9032075 </ref>]] | [[Image:F1_holliger_and_riechmann.jpg |frame|center|Figure Adapted from Holliger and Riechmann, 1997<ref name="holliger 97"> PMID:9032075 </ref>]] {{STRUCTURE_1tol | PDB=1tol | SCENE= }} | ||
The function of the protein has a close correlation with its structural domains. The D1 domain interacts with TolA protein in the periplasm of the bacterial cell. <ref name="lubkowski"/><ref name="cabilly"/><ref name="holliger 99"/>. (The C terminal domain of TolA is the coreceptor for filamentous phage infection of E coli(Cell 90, 351-360 (1997)). The D2 domain binds to F pilus on the outer membrane of ''Escherichia coli'', however, it is also blocks TolA binding to D1 in the absence of the F pilus <ref name="chatellier"> PMID:10606756 </ref>. In fact, without the D2 domain, infectivity is very low<ref name="lubkowski"/>. It has been speculated that D2 interacts with the F pilus first, drawing the phage closer to the bacterial cell, thus allowing D1-TolA interactions to occur<ref name="holliger 99"/>. Chatellier et al suggest that the complex formed by D1 and D2 may prevent destruction of the protein from bacterial proteases, and upon binding the protein opens up and D3 can then reach the inner membrane of the bacteria<ref name="chatellier"/>. Lubkowski et al like the interaction between D1 and D2 to a horseshoe shaped molecule attributing hydrophobic molecules facing toward the center as stabilizing factors <ref name="lubkowski"/>. | The function of the protein has a close correlation with its structural domains. The D1 domain interacts with TolA protein in the periplasm of the bacterial cell. <ref name="lubkowski"/><ref name="cabilly"/><ref name="holliger 99"/>. (The C terminal domain of TolA is the coreceptor for filamentous phage infection of E coli(Cell 90, 351-360 (1997)). The D2 domain binds to F pilus on the outer membrane of ''Escherichia coli'', however, it is also blocks TolA binding to D1 in the absence of the F pilus <ref name="chatellier"> PMID:10606756 </ref>. In fact, without the D2 domain, infectivity is very low<ref name="lubkowski"/>. It has been speculated that D2 interacts with the F pilus first, drawing the phage closer to the bacterial cell, thus allowing D1-TolA interactions to occur<ref name="holliger 99"/>. Chatellier et al suggest that the complex formed by D1 and D2 may prevent destruction of the protein from bacterial proteases, and upon binding the protein opens up and D3 can then reach the inner membrane of the bacteria<ref name="chatellier"/>. Lubkowski et al like the interaction between D1 and D2 to a horseshoe shaped molecule attributing hydrophobic molecules facing toward the center as stabilizing factors <ref name="lubkowski"/>. | ||
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===Phage Display=== | ===Phage Display=== | ||
[[Image:wt_and_pIII.jpg |frame|right|Figure Adapted from Hill and Stockley et al, 1996 <ref name="hill"> PMID:8793867 </ref>]] N terminus can be truncated and the peptide of choice can be inserted (Cabilly) | [[Image:wt_and_pIII.jpg |frame|right|Figure Adapted from Hill and Stockley et al, 1996 <ref name="hill"> PMID:8793867 </ref>]] | ||
N terminus can be truncated and the peptide of choice can be inserted (Cabilly) | |||
Insertions can also be done between D2 and D3 (H and R, 9032075) | Insertions can also be done between D2 and D3 (H and R, 9032075) | ||
Peptides can be fused to CT domain or to the N1 domain, neither areas are near the central area of the horseshoe <ref name="lubkowski"/>. | Peptides can be fused to CT domain or to the N1 domain, neither areas are near the central area of the horseshoe <ref name="lubkowski"/>. | ||
