Reprogramming the infection mechanism of a filamentous phage

Molecular Microbiology

Volumn 80, Issue 3, 2011, Pages 827-834

  Lorenz, Stefan H ^a   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIUM PILUS; BINDING SITE; CONTROLLED STUDY; ESCHERICHIA COLI; ESCHERICHIA COLI INFECTION; HINGE REGION; ISOMERIZATION; MYCOBACTERIOPHAGE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY;

AMINO ACID SUBSTITUTION; BINDING SITES; ESCHERICHIA COLI; INOVIRUS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, VIRUS; VIRAL PROTEINS; VIRUS ATTACHMENT;

ENTEROBACTERIA PHAGE FD; ENTEROBACTERIA PHAGE IF1; ESCHERICHIA COLI; GOSSWEILERODENDRON BALSAMIFERUM;

EID: 79955012080     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07617.x     Document Type: Article

References (27)

1. Chatellier, J., Hartley, O., Griffiths, A.D., Fersht, A.R., Winter, G., and Riechmann, L. (1999) Interdomain interactions within the gene 3 protein of filamentous phage. FEBS Lett 463: 371-374.
2. Click, E.M., and Webster, R.E. (1997) Filamentous phage infection: required interactions with the TolA protein. J Bacteriol 179: 6464-6471.
3. Deng, L.W., and Perham, R.N. (2002) Delineating the site of interaction on the pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli. J Mol Biol 319: 603-614.
4. Deng, L.W., Malik, P., and Perham, R.N. (1999) Interaction of the globular domains of pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli. Virology 253: 271-277.
5. Eckert, B., and Schmid, F.X. (2007) A conformational unfolding reaction activates phage fd for the infection of Escherichia coli. J Mol Biol 373: 452-461.
6. Eckert, B., Martin, A., Balbach, J., and Schmid, F.X. (2005) Prolyl isomerization as a molecular timer in phage infection. Nat Struct Mol Biol 12: 619-623.
7. Holliger, P., Riechmann, L., and Williams, R.L. (1999) Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 Angström: evidence for conformational lability. J Mol Biol 288: 649-657.
8. Jakob, R.P., and Schmid, F.X. (2008) Energetic coupling between native-state prolyl isomerization and conformational protein folding. J Mol Biol 377: 1560-1575.
9. Jakob, R.P., Zierer, B.K., Weininger, U., Hofmann, S.D., Lorenz, S.H., Balbach, J., etal. (2010) Elimination of a cis-proline-containing loop and turn optimization stabilizes a protein and accelerates its folding. J Mol Biol 399: 331-346.
10. Karlsson, F., Borrebaeck, C.A., Nilsson, N., and Malmborg-Hager, A.C. (2003) The mechanism of bacterial infection by filamentous phages involves molecular interactions between TolA and phage protein 3 domains. J Bacteriol 185: 2628-2634.
11. Krebber, C., Spada, S., Desplancq, D., Krebber, A., Ge, L., and Plückthun, A. (1997) Selectively-infective phage (SIP): a mechanistic dissection of a novel in vivo selection for protein-ligand interactions. J Mol Biol 268: 607-618.
12. Levengood, S.K., Beyer, W.F., Jr, and Webster, R.E. (1991) TolA: a membrane protein involved in colicin uptake contains an extended helical region. Proc Nat Acad Sci USA 88: 5939-5943.
13. Lorenz, S.H., Jakob, R.P., Weininger, U., Balbach, J., Dobbek, H., and Schmid, F.X. (2011) The filamentous phages fd and IF1 use different mechanisms to infect Escherichia coli. J Mol Biol 405: 989-1003.
14. Lubkowski, J., Hennecke, F., Plückthun, A., and Wlodawer, A. (1998) The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of G3P. Nat Struct Biol 5: 140-147.
15. Lubkowski, J., Hennecke, F., Plückthun, A., and Wlodawer, A. (1999) Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA. Structure 7: 711-722.
16. Martin, A., and Schmid, F.X. (2003a) Evolutionary stabilization of the gene-3-protein of phage fd reveals the principles that govern the thermodynamic stability of two-domain proteins. J Mol Biol 328: 863-875.
17. Martin, A., and Schmid, F.X. (2003b) A proline switch controls folding and domain interactions in the gene-3-protein of the filamentous phage fd. J Mol Biol 331: 1131-1140.
18. Martin, A., and Schmid, F.X. (2003c) The folding mechanism of a two-domain protein: folding kinetics and domain docking of the gene-3-protein of phage fd. J Mol Biol 329: 599-610.
19. Meynell, G.G., and Lawn, A.M. (1968) Filamentous phages specific for the I sex factor. Nature 217: 1184-1186.
20. Meynell, E., Meynell, G.G., and Datta, N. (1968) Phylogenetic relationships of drug-resistance factors and other transmissible bacterial plasmids. Bacteriol Rev 32: 55-83.
21. Model, P., and Russel, M. (1988) Filamentous bacteriophage. In The Bacteriophages, Vol. 2. Calendar, R. (ed.). New York: Plenum Publishing, pp. 375-456.
22. Myers, J.K., Pace, C.N., and Scholtz, J.M. (1995) Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Prot Sci 4: 2138-2148.
23. Riechmann, L., and Holliger, P. (1997) The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli. Cell 90: 351-360.
24. Santoro, M.M., and Bolen, D.W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27: 8063-8068.
25. Sieber, V., Plückthun, A., and Schmid, F.X. (1998) Selecting proteins with improved stability by a phage-based method. Nat Biotech 16: 955-960.
26. Stengele, I., Bross, P., Garces, X., Giray, J., and Rasched, I. (1990) Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites. J Mol Biol 212: 143-149.
27. Weininger, U., Jakob, R.P., Eckert, B., Schweimer, K., Schmid, F.X., and Balbach, J. (2009) A remote prolyl isomerization controls domain assembly via a hydrogen bonding network. Proc Nat Acad Sci USA 106: 12335-12340.